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Literature summary extracted from

  • Kumar, B.; Kaur, C.; Pareek, A.; Sopory, S.K.; Singla-Pareek, S.L.
    Tracing the evolution of plant glyoxalase III enzymes for structural and functional divergence (2021), Antioxidants (Basel), 10, 648.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.1.130 cytoplasm
-
 Natronobacterium gregoryi 5737
-
4.2.1.130 cytoplasm
-
 Vulcanisaeta distributa 5737
-
4.2.1.130 cytoplasm
-
 Methanobacterium sp. 5737
-
4.2.1.130 cytoplasm
-
 Natronococcus occultus 5737
-
4.2.1.130 cytoplasm
-
 Natrinema pellirubrum 5737
-
4.2.1.130 cytoplasm
-
 Mobiluncus mulieris 5737
-
4.2.1.130 cytoplasm
-
 Schaalia georgiae 5737
-
4.2.1.130 cytoplasm
-
 Acetobacter pasteurianus 5737
-
4.2.1.130 cytoplasm
-
 Rhizobium sp. 5737
-
4.2.1.130 cytoplasm
-
 Hydrogenobaculum sp. 5737
-
4.2.1.130 cytoplasm
-
 Prevotella denticola 5737
-
4.2.1.130 cytoplasm
-
 Ralstonia solanacearum 5737
-
4.2.1.130 cytoplasm
-
 Coraliomargarita akajimensis 5737
-
4.2.1.130 cytoplasm
-
 Verrucomicrobiia bacterium 5737
-
4.2.1.130 cytoplasm
-
 Pseudanabaena biceps 5737
-
4.2.1.130 cytoplasm
-
 Synechococcus sp. 5737
-
4.2.1.130 cytoplasm
-
 Caldithrix abyssi 5737
-
4.2.1.130 cytoplasm
-
 Denitrovibrio acetiphilus 5737
-
4.2.1.130 cytoplasm
-
 Alkalidesulfovibrio alkalitolerans 5737
-
4.2.1.130 cytoplasm
-
 Campylobacter jejuni 5737
-
4.2.1.130 cytoplasm
-
 Helicobacter bilis 5737
-
4.2.1.130 cytoplasm
-
 Fibrobacter succinogenes 5737
-
4.2.1.130 cytoplasm
-
 Gemella haemolysans 5737
-
4.2.1.130 cytoplasm
-
 Bacillus cereus 5737
-
4.2.1.130 cytoplasm
-
 Cetobacterium somerae 5737
-
4.2.1.130 cytoplasm
-
 Leptotrichia wadei 5737
-
4.2.1.130 cytoplasm
-
 Escherichia coli 5737
-
4.2.1.130 cytoplasm
-
 Pseudomonas sp. 5737
-
4.2.1.130 cytoplasm
-
 Winmispira thermophila 5737
-
4.2.1.130 cytoplasm
-
 Spiroplasma chrysopicola 5737
-
4.2.1.130 cytoplasm
-
 Mycoplasmopsis synoviae 5737
-
4.2.1.130 cytoplasm
-
 Trypanosoma cruzi 5737
-
4.2.1.130 cytoplasm
-
 Leishmania donovani 5737
-
4.2.1.130 cytoplasm
-
 Dictyostelium discoideum 5737
-
4.2.1.130 cytoplasm
-
 Entamoeba histolytica 5737
-
4.2.1.130 cytoplasm
-
 Paramecium tetraurelia 5737
-
4.2.1.130 cytoplasm
-
 Plasmodium falciparum 5737
-
4.2.1.130 cytoplasm
-
 Saccharomyces cerevisiae 5737
-
4.2.1.130 cytoplasm
-
 Schizosaccharomyces pombe 5737
-
4.2.1.130 cytoplasm
-
 Schizosaccharomyces japonicus 5737
-
4.2.1.130 cytoplasm
-
 Aspergillus niger 5737
-
4.2.1.130 cytoplasm
-
 Colletotrichum gloeosporioides 5737
-
4.2.1.130 cytoplasm
-
 Phaeodactylum tricornutum 5737
-
4.2.1.130 cytoplasm
-
 Thalassiosira pseudonana 5737
-
4.2.1.130 cytoplasm
-
 Ectocarpus siliculosus 5737
-
4.2.1.130 cytoplasm
-
 Chlorella variabilis 5737
-
4.2.1.130 cytoplasm
-
 Chlamydomonas reinhardtii 5737
-
4.2.1.130 cytoplasm
-
 Genlisea aurea 5737
-
4.2.1.130 cytoplasm
-
 Selaginella moellendorffii 5737
-
4.2.1.130 cytoplasm
-
 Physcomitrium patens 5737
-
4.2.1.130 cytoplasm
-
 Solanum tuberosum 5737
-
4.2.1.130 cytoplasm
-
 Populus trichocarpa 5737
-
4.2.1.130 cytoplasm
-
 Oryza sativa 5737
-
4.2.1.130 cytoplasm
-
 Triticum aestivum 5737
-
4.2.1.130 cytoplasm
-
 Zea mays 5737
-
4.2.1.130 cytoplasm
-
 Arabidopsis thaliana 5737
-
4.2.1.130 cytoplasm
-
 Brassica rapa 5737
-
4.2.1.130 cytoplasm
-
 Toxoplasma gondii 5737
-
4.2.1.130 cytoplasm
-
 Hydra vulgaris 5737
-
4.2.1.130 cytoplasm
-
 Xenopus laevis 5737
-
4.2.1.130 cytoplasm
-
 Drosophila melanogaster 5737
-
4.2.1.130 cytoplasm
-
 Ascaris suum 5737
-
4.2.1.130 cytoplasm
-
 Caenorhabditis elegans 5737
-
4.2.1.130 cytoplasm
-
 Echinops telfairi 5737
-
4.2.1.130 cytoplasm
-
 Tupaia chinensis 5737
-
4.2.1.130 cytoplasm
-
 Mus musculus 5737
-
4.2.1.130 cytoplasm
-
 Homo sapiens 5737
-
4.2.1.130 membrane inner membrane Rhizobium sp. 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.130 2-oxopropanal + H2O Natronobacterium gregoryi
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Vulcanisaeta distributa
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Methanobacterium sp.
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Natronococcus occultus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Natrinema pellirubrum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Mobiluncus mulieris
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Schaalia georgiae
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Acetobacter pasteurianus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Rhizobium sp.
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Hydrogenobaculum sp.
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Prevotella denticola
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Ralstonia solanacearum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Coraliomargarita akajimensis
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Verrucomicrobiia bacterium
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Pseudanabaena biceps
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Synechococcus sp.
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Caldithrix abyssi
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Denitrovibrio acetiphilus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Alkalidesulfovibrio alkalitolerans
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Campylobacter jejuni
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Helicobacter bilis
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Fibrobacter succinogenes
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Gemella haemolysans
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Bacillus cereus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Cetobacterium somerae
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Leptotrichia wadei
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Escherichia coli
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Pseudomonas sp.
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Winmispira thermophila
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Spiroplasma chrysopicola
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Mycoplasmopsis synoviae
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Trypanosoma cruzi
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Leishmania donovani
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Dictyostelium discoideum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Entamoeba histolytica
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Paramecium tetraurelia
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Plasmodium falciparum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Saccharomyces cerevisiae
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Schizosaccharomyces pombe
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Schizosaccharomyces japonicus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Aspergillus niger
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Colletotrichum gloeosporioides
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Phaeodactylum tricornutum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Thalassiosira pseudonana
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Ectocarpus siliculosus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Chlorella variabilis
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Chlamydomonas reinhardtii
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Genlisea aurea
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Selaginella moellendorffii
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Physcomitrium patens
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Solanum tuberosum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Populus trichocarpa
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Oryza sativa
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Triticum aestivum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Zea mays
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Arabidopsis thaliana
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Brassica rapa
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Toxoplasma gondii
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Hydra vulgaris
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Xenopus laevis
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Drosophila melanogaster
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Ascaris suum
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Caenorhabditis elegans
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Echinops telfairi
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Tupaia chinensis
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Mus musculus
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Homo sapiens
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Schizosaccharomyces pombe ATCC 24843
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Toxoplasma gondii ME49
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Trypanosoma cruzi CL Brener
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Phaeodactylum tricornutum CCAP 1055/1
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Denitrovibrio acetiphilus DSM 12809
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Mycoplasmopsis synoviae 53
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Thalassiosira pseudonana CCMP1335
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Colletotrichum gloeosporioides Nara gc5
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Vulcanisaeta distributa DSM 14429
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Schizosaccharomyces japonicus FY16936
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Natronobacterium gregoryi ATCC 43098
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Methanobacterium sp. Maddingley MBC34
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Natronococcus occultus SP4
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Natrinema pellirubrum DSM 15624
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Rhizobium sp. CF080
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Pseudanabaena biceps PCC 7429
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Synechococcus sp. PCC 7502
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Alkalidesulfovibrio alkalitolerans DSM 16529
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Helicobacter bilis ATCC 43879
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Gemella haemolysans ATCC 10379
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Cetobacterium somerae ATCC BAA-474
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Leptotrichia wadei F0279
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Pseudomonas sp. GM30
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Winmispira thermophila ATCC 49972
-
 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O Spiroplasma chrysopicola DF-1
-
 (R)-lactate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.130 Acetobacter pasteurianus A0A1A0CGZ8
-
-
4.2.1.130 Alkalidesulfovibrio alkalitolerans S7TBV8
-
-
4.2.1.130 Alkalidesulfovibrio alkalitolerans DSM 16529 S7TBV8
-
-
4.2.1.130 Arabidopsis thaliana Q9M1G8
-
-
4.2.1.130 Arabidopsis thaliana Q9FPF0
-
-
4.2.1.130 Arabidopsis thaliana Q9MAH3
-
-
4.2.1.130 Arabidopsis thaliana Q8VY09
-
-
4.2.1.130 Arabidopsis thaliana Q9ZV19
-
-
4.2.1.130 Arabidopsis thaliana Q9M8R4
-
-
4.2.1.130 Ascaris suum
-
-
-
4.2.1.130 Aspergillus niger A0A3F3RGY7
-
-
4.2.1.130 Bacillus cereus
-
-
-
4.2.1.130 Brassica rapa
-
-
-
4.2.1.130 Caenorhabditis elegans O16228
-
-
4.2.1.130 Caenorhabditis elegans P90994
-
-
4.2.1.130 Caldithrix abyssi H1XQM6
-
-
4.2.1.130 Campylobacter jejuni
-
-
-
4.2.1.130 Cetobacterium somerae U7VB12
-
-
4.2.1.130 Cetobacterium somerae U7V9C1
-
-
4.2.1.130 Cetobacterium somerae ATCC BAA-474 U7VB12
-
-
4.2.1.130 Cetobacterium somerae ATCC BAA-474 U7V9C1
-
-
4.2.1.130 Chlamydomonas reinhardtii A0A2K3E8F4
-
-
4.2.1.130 Chlorella variabilis E1ZIT1
-
-
4.2.1.130 Colletotrichum gloeosporioides L2FT05
-
-
4.2.1.130 Colletotrichum gloeosporioides L2GFD0
-
-
4.2.1.130 Colletotrichum gloeosporioides L2G6P3
-
-
4.2.1.130 Colletotrichum gloeosporioides L2FSK4
-
-
4.2.1.130 Colletotrichum gloeosporioides L2FW83
-
-
4.2.1.130 Colletotrichum gloeosporioides Nara gc5 L2FT05
-
-
4.2.1.130 Colletotrichum gloeosporioides Nara gc5 L2GFD0
-
-
4.2.1.130 Colletotrichum gloeosporioides Nara gc5 L2G6P3
-
-
4.2.1.130 Colletotrichum gloeosporioides Nara gc5 L2FSK4
-
-
4.2.1.130 Colletotrichum gloeosporioides Nara gc5 L2FW83
-
-
4.2.1.130 Coraliomargarita akajimensis D5EPG3
-
-
4.2.1.130 Denitrovibrio acetiphilus D4H2Q0
-
-
4.2.1.130 Denitrovibrio acetiphilus DSM 12809 D4H2Q0
-
-
4.2.1.130 Dictyostelium discoideum Q54MG7
-
-
4.2.1.130 Drosophila melanogaster Q9VA37
-
-
4.2.1.130 Echinops telfairi
-
-
-
4.2.1.130 Ectocarpus siliculosus D7FQJ0
-
-
4.2.1.130 Entamoeba histolytica C4M1U6
-
-
4.2.1.130 Escherichia coli P45470
-
-
4.2.1.130 Escherichia coli Q46948
-
-
4.2.1.130 Escherichia coli P0ABU5
-
-
4.2.1.130 Fibrobacter succinogenes
-
-
-
4.2.1.130 Gemella haemolysans C5NVZ3
-
-
4.2.1.130 Gemella haemolysans ATCC 10379 C5NVZ3
-
-
4.2.1.130 Genlisea aurea S8CKY5
-
-
4.2.1.130 Helicobacter bilis C3XF88
-
-
4.2.1.130 Helicobacter bilis ATCC 43879 C3XF88
-
-
4.2.1.130 Homo sapiens Q99497
-
-
4.2.1.130 Hydra vulgaris T2M6B2
-
-
4.2.1.130 Hydrogenobaculum sp. B4U9D2
-
-
4.2.1.130 Leishmania donovani A0A3Q8IHS5
-
-
4.2.1.130 Leptotrichia wadei U2PWT7
-
-
4.2.1.130 Leptotrichia wadei F0279 U2PWT7
-
-
4.2.1.130 Methanobacterium sp. K6TL78
-
-
4.2.1.130 Methanobacterium sp. K6TV48
-
-
4.2.1.130 Methanobacterium sp. Maddingley MBC34 K6TL78
-
-
4.2.1.130 Methanobacterium sp. Maddingley MBC34 K6TV48
-
-
4.2.1.130 Mobiluncus mulieris
-
-
-
4.2.1.130 Mus musculus Q99LX0
-
-
4.2.1.130 Mycoplasmopsis synoviae Q4A733
-
-
4.2.1.130 Mycoplasmopsis synoviae 53 Q4A733
-
-
4.2.1.130 Natrinema pellirubrum L0JNV0
-
-
4.2.1.130 Natrinema pellirubrum L0JFS2
-
-
4.2.1.130 Natrinema pellirubrum L0JL06
-
-
4.2.1.130 Natrinema pellirubrum DSM 15624 L0JNV0
-
-
4.2.1.130 Natrinema pellirubrum DSM 15624 L0JFS2
-
-
4.2.1.130 Natrinema pellirubrum DSM 15624 L0JL06
-
-
4.2.1.130 Natronobacterium gregoryi L0AMG1
-
-
4.2.1.130 Natronobacterium gregoryi L0AGN5
-
-
4.2.1.130 Natronobacterium gregoryi L0ALD9
-
-
4.2.1.130 Natronobacterium gregoryi ATCC 43098 L0AMG1
-
-
4.2.1.130 Natronobacterium gregoryi ATCC 43098 L0AGN5
-
-
4.2.1.130 Natronobacterium gregoryi ATCC 43098 L0ALD9
-
-
4.2.1.130 Natronococcus occultus L0K220
-
-
4.2.1.130 Natronococcus occultus L0K4F7
-
-
4.2.1.130 Natronococcus occultus L0K5I0
-
-
4.2.1.130 Natronococcus occultus SP4 L0K220
-
-
4.2.1.130 Natronococcus occultus SP4 L0K4F7
-
-
4.2.1.130 Natronococcus occultus SP4 L0K5I0
-
-
4.2.1.130 Oryza sativa
-
-
-
4.2.1.130 Paramecium tetraurelia A0BZM8
-
-
4.2.1.130 Phaeodactylum tricornutum B7FPE0
-
-
4.2.1.130 Phaeodactylum tricornutum CCAP 1055/1 B7FPE0
-
-
4.2.1.130 Physcomitrium patens
-
-
-
4.2.1.130 Plasmodium falciparum C6KTB1 isolate 3D7
-
4.2.1.130 Populus trichocarpa
-
-
-
4.2.1.130 Prevotella denticola B4U9D2
-
-
4.2.1.130 Pseudanabaena biceps L8N6I4
-
-
4.2.1.130 Pseudanabaena biceps PCC 7429 L8N6I4
-
-
4.2.1.130 Pseudomonas sp. W6VVY7
-
-
4.2.1.130 Pseudomonas sp. W6VXU6
-
-
4.2.1.130 Pseudomonas sp. W6VXI4
-
-
4.2.1.130 Pseudomonas sp. W6VNQ8
-
-
4.2.1.130 Pseudomonas sp. W6VF67
-
-
4.2.1.130 Pseudomonas sp. W6VVW0
-
-
4.2.1.130 Pseudomonas sp. W6VRI9
-
-
4.2.1.130 Pseudomonas sp. W6VNC8
-
-
4.2.1.130 Pseudomonas sp. W6VT23
-
-
4.2.1.130 Pseudomonas sp. W6VR72
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VVY7
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VXU6
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VXI4
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VNQ8
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VF67
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VVW0
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VRI9
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VNC8
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VT23
-
-
4.2.1.130 Pseudomonas sp. GM30 W6VR72
-
-
4.2.1.130 Ralstonia solanacearum B4U9D2
-
-
4.2.1.130 Rhizobium sp. W6VYT4
-
-
4.2.1.130 Rhizobium sp. W6VYG0
-
-
4.2.1.130 Rhizobium sp. CF080 W6VYT4
-
-
4.2.1.130 Rhizobium sp. CF080 W6VYG0
-
-
4.2.1.130 Saccharomyces cerevisiae C6KTB1
-
-
4.2.1.130 Schaalia georgiae J1HHW5
-
-
4.2.1.130 Schizosaccharomyces japonicus B6JZR1
-
-
4.2.1.130 Schizosaccharomyces japonicus FY16936 B6JZR1
-
-
4.2.1.130 Schizosaccharomyces pombe Q10356
-
-
4.2.1.130 Schizosaccharomyces pombe O74914
-
-
4.2.1.130 Schizosaccharomyces pombe Q09675
-
-
4.2.1.130 Schizosaccharomyces pombe O43084
-
-
4.2.1.130 Schizosaccharomyces pombe Q10092
-
-
4.2.1.130 Schizosaccharomyces pombe Q09918
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 Q10356
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 O74914
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 Q09675
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 O43084
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 Q10092
-
-
4.2.1.130 Schizosaccharomyces pombe ATCC 24843 Q09918
-
-
4.2.1.130 Selaginella moellendorffii D8QW13
-
-
4.2.1.130 Solanum tuberosum
-
-
-
4.2.1.130 Spiroplasma chrysopicola R4U3R9
-
-
4.2.1.130 Spiroplasma chrysopicola DF-1 R4U3R9
-
-
4.2.1.130 Synechococcus sp. K9SQE8
-
-
4.2.1.130 Synechococcus sp. PCC 7502 K9SQE8
-
-
4.2.1.130 Thalassiosira pseudonana B8BUW9
-
-
4.2.1.130 Thalassiosira pseudonana CCMP1335 B8BUW9
-
-
4.2.1.130 Toxoplasma gondii S8GP52
-
-
4.2.1.130 Toxoplasma gondii ME49 S8GP52
-
-
4.2.1.130 Triticum aestivum
-
-
-
4.2.1.130 Trypanosoma cruzi Q4D6D8
-
-
4.2.1.130 Trypanosoma cruzi Q4D586
-
-
4.2.1.130 Trypanosoma cruzi CL Brener Q4D6D8
-
-
4.2.1.130 Trypanosoma cruzi CL Brener Q4D586
-
-
4.2.1.130 Tupaia chinensis L9KRY1
-
-
4.2.1.130 Tupaia chinensis L9LCY1
-
-
4.2.1.130 Tupaia chinensis L9L0V9
-
-
4.2.1.130 Tupaia chinensis L9KSA3
-
-
4.2.1.130 Tupaia chinensis L9KT89
-
-
4.2.1.130 Tupaia chinensis L9L4K0
-
-
4.2.1.130 Verrucomicrobiia bacterium B5JP08
-
-
4.2.1.130 Vulcanisaeta distributa E1QNI0
-
-
4.2.1.130 Vulcanisaeta distributa E1QR47
-
-
4.2.1.130 Vulcanisaeta distributa DSM 14429 E1QNI0
-
-
4.2.1.130 Vulcanisaeta distributa DSM 14429 E1QR47
-
-
4.2.1.130 Winmispira thermophila E0RPI3
-
-
4.2.1.130 Winmispira thermophila ATCC 49972 E0RPI3
-
-
4.2.1.130 Xenopus laevis Q6DKB1
-
-
4.2.1.130 Xenopus laevis Q90XE4
-
-
4.2.1.130 Xenopus laevis Q6NTU4
-
-
4.2.1.130 Zea mays
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.130 2-oxopropanal + H2O
-
 Natronobacterium gregoryi (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Vulcanisaeta distributa (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Methanobacterium sp. (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Natronococcus occultus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Natrinema pellirubrum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Mobiluncus mulieris (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Schaalia georgiae (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Acetobacter pasteurianus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Rhizobium sp. (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Hydrogenobaculum sp. (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Prevotella denticola (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Ralstonia solanacearum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Coraliomargarita akajimensis (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Verrucomicrobiia bacterium (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Pseudanabaena biceps (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Synechococcus sp. (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Caldithrix abyssi (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Denitrovibrio acetiphilus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Alkalidesulfovibrio alkalitolerans (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Campylobacter jejuni (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Helicobacter bilis (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Fibrobacter succinogenes (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Gemella haemolysans (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Bacillus cereus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Cetobacterium somerae (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Leptotrichia wadei (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Escherichia coli (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Pseudomonas sp. (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Winmispira thermophila (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Spiroplasma chrysopicola (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Mycoplasmopsis synoviae (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Trypanosoma cruzi (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Leishmania donovani (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Dictyostelium discoideum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Entamoeba histolytica (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Paramecium tetraurelia (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Plasmodium falciparum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Saccharomyces cerevisiae (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Schizosaccharomyces pombe (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Schizosaccharomyces japonicus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Aspergillus niger (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Colletotrichum gloeosporioides (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Phaeodactylum tricornutum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Thalassiosira pseudonana (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Ectocarpus siliculosus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Chlorella variabilis (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Chlamydomonas reinhardtii (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Genlisea aurea (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Selaginella moellendorffii (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Physcomitrium patens (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Solanum tuberosum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Populus trichocarpa (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Oryza sativa (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Triticum aestivum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Zea mays (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Arabidopsis thaliana (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Brassica rapa (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Toxoplasma gondii (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Hydra vulgaris (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Xenopus laevis (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Drosophila melanogaster (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Ascaris suum (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Caenorhabditis elegans (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Echinops telfairi (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Tupaia chinensis (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Mus musculus (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Homo sapiens (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Schizosaccharomyces pombe ATCC 24843 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Toxoplasma gondii ME49 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Trypanosoma cruzi CL Brener (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Phaeodactylum tricornutum CCAP 1055/1 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Denitrovibrio acetiphilus DSM 12809 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Mycoplasmopsis synoviae 53 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Thalassiosira pseudonana CCMP1335 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Colletotrichum gloeosporioides Nara gc5 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Vulcanisaeta distributa DSM 14429 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Schizosaccharomyces japonicus FY16936 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Natronobacterium gregoryi ATCC 43098 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Methanobacterium sp. Maddingley MBC34 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Natronococcus occultus SP4 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Natrinema pellirubrum DSM 15624 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Rhizobium sp. CF080 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Pseudanabaena biceps PCC 7429 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Synechococcus sp. PCC 7502 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Alkalidesulfovibrio alkalitolerans DSM 16529 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Helicobacter bilis ATCC 43879 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Gemella haemolysans ATCC 10379 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Cetobacterium somerae ATCC BAA-474 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Leptotrichia wadei F0279 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Pseudomonas sp. GM30 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Winmispira thermophila ATCC 49972 (R)-lactate
-
 ?
4.2.1.130 2-oxopropanal + H2O
-
 Spiroplasma chrysopicola DF-1 (R)-lactate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.130 GLYIII
-
 Campylobacter jejuni
4.2.1.130 GLYIII
-
 Helicobacter bilis
4.2.1.130 GLYIII
-
 Fibrobacter succinogenes
4.2.1.130 GLYIII
-
 Gemella haemolysans
4.2.1.130 GLYIII
-
 Bacillus cereus
4.2.1.130 GLYIII
-
 Physcomitrium patens
4.2.1.130 GLYIII
-
 Solanum tuberosum
4.2.1.130 GLYIII
-
 Populus trichocarpa
4.2.1.130 GLYIII
-
 Oryza sativa
4.2.1.130 GLYIII
-
 Triticum aestivum
4.2.1.130 GLYIII
-
 Zea mays
4.2.1.130 GLYIII
-
 Brassica rapa
4.2.1.130 GLYIII
-
 Drosophila melanogaster
4.2.1.130 GLYIII
-
 Echinops telfairi
4.2.1.130 GLYIII1
-
 Natronobacterium gregoryi
4.2.1.130 GLYIII1
-
 Vulcanisaeta distributa
4.2.1.130 GLYIII1
-
 Methanobacterium sp.
4.2.1.130 GLYIII1
-
 Natronococcus occultus
4.2.1.130 GLYIII1
-
 Natrinema pellirubrum
4.2.1.130 GLYIII1
-
 Mobiluncus mulieris
4.2.1.130 GLYIII1
-
 Schaalia georgiae
4.2.1.130 GLYIII1
-
 Acetobacter pasteurianus
4.2.1.130 GLYIII1
-
 Rhizobium sp.
4.2.1.130 GLYIII1
-
 Hydrogenobaculum sp.
4.2.1.130 GLYIII1
-
 Prevotella denticola
4.2.1.130 GLYIII1
-
 Ralstonia solanacearum
4.2.1.130 GLYIII1
-
 Coraliomargarita akajimensis
4.2.1.130 GLYIII1
-
 Verrucomicrobiia bacterium
4.2.1.130 GLYIII1
-
 Pseudanabaena biceps
4.2.1.130 GLYIII1
-
 Synechococcus sp.
4.2.1.130 GLYIII1
-
 Caldithrix abyssi
4.2.1.130 GLYIII1
-
 Denitrovibrio acetiphilus
4.2.1.130 GLYIII1
-
 Alkalidesulfovibrio alkalitolerans
4.2.1.130 GLYIII1
-
 Cetobacterium somerae
4.2.1.130 GLYIII1
-
 Escherichia coli
4.2.1.130 GLYIII1
-
 Winmispira thermophila
4.2.1.130 GLYIII1
-
 Spiroplasma chrysopicola
4.2.1.130 GLYIII1
-
 Mycoplasmopsis synoviae
4.2.1.130 GLYIII1
-
 Trypanosoma cruzi
4.2.1.130 GLYIII1
-
 Leishmania donovani
4.2.1.130 GLYIII1
-
 Dictyostelium discoideum
4.2.1.130 GLYIII1
-
 Entamoeba histolytica
4.2.1.130 GLYIII1
-
 Paramecium tetraurelia
4.2.1.130 GLYIII1
-
 Plasmodium falciparum
4.2.1.130 GLYIII1
-
 Saccharomyces cerevisiae
4.2.1.130 GLYIII1
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII1
-
 Schizosaccharomyces japonicus
4.2.1.130 GLYIII1
-
 Aspergillus niger
4.2.1.130 GLYIII1
-
 Colletotrichum gloeosporioides
4.2.1.130 GLYIII1
-
 Phaeodactylum tricornutum
4.2.1.130 GLYIII1
-
 Thalassiosira pseudonana
4.2.1.130 GLYIII1
-
 Ectocarpus siliculosus
4.2.1.130 GLYIII1
-
 Chlorella variabilis
4.2.1.130 GLYIII1
-
 Chlamydomonas reinhardtii
4.2.1.130 GLYIII1
-
 Genlisea aurea
4.2.1.130 GLYIII1
-
 Selaginella moellendorffii
4.2.1.130 GLYIII1
-
 Arabidopsis thaliana
4.2.1.130 GLYIII1
-
 Toxoplasma gondii
4.2.1.130 GLYIII1
-
 Hydra vulgaris
4.2.1.130 GLYIII1
-
 Xenopus laevis
4.2.1.130 GLYIII1
-
 Ascaris suum
4.2.1.130 GLYIII1
-
 Caenorhabditis elegans
4.2.1.130 GLYIII1
-
 Tupaia chinensis
4.2.1.130 GLYIII1
-
 Mus musculus
4.2.1.130 GLYIII1
-
 Homo sapiens
4.2.1.130 GLYIII10
-
 Pseudomonas sp.
4.2.1.130 GLYIII11
-
 Pseudomonas sp.
4.2.1.130 GLYIII2
-
 Natronobacterium gregoryi
4.2.1.130 GLYIII2
-
 Vulcanisaeta distributa
4.2.1.130 GLYIII2
-
 Methanobacterium sp.
4.2.1.130 GLYIII2
-
 Natronococcus occultus
4.2.1.130 GLYIII2
-
 Natrinema pellirubrum
4.2.1.130 GLYIII2
-
 Rhizobium sp.
4.2.1.130 GLYIII2
-
 Cetobacterium somerae
4.2.1.130 GLYIII2
-
 Leptotrichia wadei
4.2.1.130 GLYIII2
-
 Pseudomonas sp.
4.2.1.130 GLYIII2
-
 Dictyostelium discoideum
4.2.1.130 GLYIII2
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII2
-
 Colletotrichum gloeosporioides
4.2.1.130 GLYIII2
-
 Arabidopsis thaliana
4.2.1.130 GLYIII2
-
 Xenopus laevis
4.2.1.130 GLYIII2
-
 Caenorhabditis elegans
4.2.1.130 GLYIII2
-
 Tupaia chinensis
4.2.1.130 GLYIII3
-
 Natronobacterium gregoryi
4.2.1.130 GLYIII3
-
 Natronococcus occultus
4.2.1.130 GLYIII3
-
 Natrinema pellirubrum
4.2.1.130 GLYIII3
-
 Escherichia coli
4.2.1.130 GLYIII3
-
 Pseudomonas sp.
4.2.1.130 GLYIII3
-
 Trypanosoma cruzi
4.2.1.130 GLYIII3
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII3
-
 Colletotrichum gloeosporioides
4.2.1.130 GLYIII3
-
 Arabidopsis thaliana
4.2.1.130 GLYIII3
-
 Xenopus laevis
4.2.1.130 GLYIII3
-
 Tupaia chinensis
4.2.1.130 GLYIII4
-
 Escherichia coli
4.2.1.130 GLYIII4
-
 Pseudomonas sp.
4.2.1.130 GLYIII4
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII4
-
 Colletotrichum gloeosporioides
4.2.1.130 GLYIII4
-
 Arabidopsis thaliana
4.2.1.130 GLYIII4
-
 Tupaia chinensis
4.2.1.130 GLYIII5
-
 Pseudomonas sp.
4.2.1.130 GLYIII5
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII5
-
 Colletotrichum gloeosporioides
4.2.1.130 GLYIII5
-
 Arabidopsis thaliana
4.2.1.130 GLYIII5
-
 Tupaia chinensis
4.2.1.130 GLYIII6
-
 Pseudomonas sp.
4.2.1.130 GLYIII6
-
 Schizosaccharomyces pombe
4.2.1.130 GLYIII6
-
 Arabidopsis thaliana
4.2.1.130 GLYIII6
-
 Tupaia chinensis
4.2.1.130 GLYIII7
-
 Pseudomonas sp.
4.2.1.130 GLYIII8
-
 Pseudomonas sp.
4.2.1.130 GLYIII9
-
 Pseudomonas sp.
4.2.1.130 glyoxalase III
-
 Natronobacterium gregoryi
4.2.1.130 glyoxalase III
-
 Vulcanisaeta distributa
4.2.1.130 glyoxalase III
-
 Methanobacterium sp.
4.2.1.130 glyoxalase III
-
 Natronococcus occultus
4.2.1.130 glyoxalase III
-
 Natrinema pellirubrum
4.2.1.130 glyoxalase III
-
 Mobiluncus mulieris
4.2.1.130 glyoxalase III
-
 Schaalia georgiae
4.2.1.130 glyoxalase III
-
 Acetobacter pasteurianus
4.2.1.130 glyoxalase III
-
 Rhizobium sp.
4.2.1.130 glyoxalase III
-
 Hydrogenobaculum sp.
4.2.1.130 glyoxalase III
-
 Prevotella denticola
4.2.1.130 glyoxalase III
-
 Ralstonia solanacearum
4.2.1.130 glyoxalase III
-
 Coraliomargarita akajimensis
4.2.1.130 glyoxalase III
-
 Verrucomicrobiia bacterium
4.2.1.130 glyoxalase III
-
 Pseudanabaena biceps
4.2.1.130 glyoxalase III
-
 Synechococcus sp.
4.2.1.130 glyoxalase III
-
 Caldithrix abyssi
4.2.1.130 glyoxalase III
-
 Denitrovibrio acetiphilus
4.2.1.130 glyoxalase III
-
 Alkalidesulfovibrio alkalitolerans
4.2.1.130 glyoxalase III
-
 Campylobacter jejuni
4.2.1.130 glyoxalase III
-
 Helicobacter bilis
4.2.1.130 glyoxalase III
-
 Fibrobacter succinogenes
4.2.1.130 glyoxalase III
-
 Gemella haemolysans
4.2.1.130 glyoxalase III
-
 Bacillus cereus
4.2.1.130 glyoxalase III
-
 Cetobacterium somerae
4.2.1.130 glyoxalase III
-
 Leptotrichia wadei
4.2.1.130 glyoxalase III
-
 Escherichia coli
4.2.1.130 glyoxalase III
-
 Pseudomonas sp.
4.2.1.130 glyoxalase III
-
 Winmispira thermophila
4.2.1.130 glyoxalase III
-
 Spiroplasma chrysopicola
4.2.1.130 glyoxalase III
-
 Mycoplasmopsis synoviae
4.2.1.130 glyoxalase III
-
 Trypanosoma cruzi
4.2.1.130 glyoxalase III
-
 Leishmania donovani
4.2.1.130 glyoxalase III
-
 Dictyostelium discoideum
4.2.1.130 glyoxalase III
-
 Entamoeba histolytica
4.2.1.130 glyoxalase III
-
 Paramecium tetraurelia
4.2.1.130 glyoxalase III
-
 Plasmodium falciparum
4.2.1.130 glyoxalase III
-
 Saccharomyces cerevisiae
4.2.1.130 glyoxalase III
-
 Schizosaccharomyces pombe
4.2.1.130 glyoxalase III
-
 Schizosaccharomyces japonicus
4.2.1.130 glyoxalase III
-
 Aspergillus niger
4.2.1.130 glyoxalase III
-
 Colletotrichum gloeosporioides
4.2.1.130 glyoxalase III
-
 Phaeodactylum tricornutum
4.2.1.130 glyoxalase III
-
 Thalassiosira pseudonana
4.2.1.130 glyoxalase III
-
 Ectocarpus siliculosus
4.2.1.130 glyoxalase III
-
 Chlorella variabilis
4.2.1.130 glyoxalase III
-
 Chlamydomonas reinhardtii
4.2.1.130 glyoxalase III
-
 Genlisea aurea
4.2.1.130 glyoxalase III
-
 Selaginella moellendorffii
4.2.1.130 glyoxalase III
-
 Physcomitrium patens
4.2.1.130 glyoxalase III
-
 Solanum tuberosum
4.2.1.130 glyoxalase III
-
 Populus trichocarpa
4.2.1.130 glyoxalase III
-
 Oryza sativa
4.2.1.130 glyoxalase III
-
 Triticum aestivum
4.2.1.130 glyoxalase III
-
 Zea mays
4.2.1.130 glyoxalase III
-
 Arabidopsis thaliana
4.2.1.130 glyoxalase III
-
 Brassica rapa
4.2.1.130 glyoxalase III
-
 Toxoplasma gondii
4.2.1.130 glyoxalase III
-
 Hydra vulgaris
4.2.1.130 glyoxalase III
-
 Xenopus laevis
4.2.1.130 glyoxalase III
-
 Drosophila melanogaster
4.2.1.130 glyoxalase III
-
 Ascaris suum
4.2.1.130 glyoxalase III
-
 Caenorhabditis elegans
4.2.1.130 glyoxalase III
-
 Echinops telfairi
4.2.1.130 glyoxalase III
-
 Tupaia chinensis
4.2.1.130 glyoxalase III
-
 Mus musculus
4.2.1.130 glyoxalase III
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Natronobacterium gregoryi
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Vulcanisaeta distributa
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Methanobacterium sp.
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Natronococcus occultus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Natrinema pellirubrum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Mobiluncus mulieris
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Schaalia georgiae
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Acetobacter pasteurianus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Rhizobium sp.
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Hydrogenobaculum sp.
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Prevotella denticola
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Ralstonia solanacearum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Coraliomargarita akajimensis
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Verrucomicrobiia bacterium
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Pseudanabaena biceps
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Synechococcus sp.
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Caldithrix abyssi
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Denitrovibrio acetiphilus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Alkalidesulfovibrio alkalitolerans
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Campylobacter jejuni
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Helicobacter bilis
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Fibrobacter succinogenes
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Gemella haemolysans
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Bacillus cereus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Cetobacterium somerae
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Leptotrichia wadei
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Escherichia coli
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Pseudomonas sp.
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Winmispira thermophila
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Spiroplasma chrysopicola
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Mycoplasmopsis synoviae
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Trypanosoma cruzi
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Leishmania donovani
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Dictyostelium discoideum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Entamoeba histolytica
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Paramecium tetraurelia
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Plasmodium falciparum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Saccharomyces cerevisiae
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Schizosaccharomyces pombe
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Schizosaccharomyces japonicus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Aspergillus niger
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Colletotrichum gloeosporioides
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Phaeodactylum tricornutum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Thalassiosira pseudonana
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Ectocarpus siliculosus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Chlorella variabilis
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Chlamydomonas reinhardtii
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Genlisea aurea
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Selaginella moellendorffii
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Physcomitrium patens
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Solanum tuberosum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Populus trichocarpa
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Oryza sativa
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Triticum aestivum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Zea mays
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Arabidopsis thaliana
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Brassica rapa
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Toxoplasma gondii
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Hydra vulgaris
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Xenopus laevis
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Drosophila melanogaster
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Ascaris suum
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Caenorhabditis elegans
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Echinops telfairi
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Tupaia chinensis
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Mus musculus
4.2.1.130 evolution evolution of glyoxalase III enzymes across prokaryotes and eukaryotes, with special emphasis on plants. GLYIII proteins are characterized by the presence of DJ-1_PfpI domains thereby, belonging to the DJ-1_PfpI protein superfamily. The analysis delineates evolution of double DJ-1_PfpI domains in plant GLYIII. Based on sequence and structural characteristics, plant GLYIII enzymes can be categorized into three different clusters, which followed different evolutionary trajectories. Glyoxalase III proteins from monocots and dicots group separately in each cluster and the each of the two domains of these proteins also cluster differentially. Glyoxalase III proteins have undergone significant evolutionary changes in plants, which is likely to confer diversity and flexibility in their functions Homo sapiens
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Natronobacterium gregoryi
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Vulcanisaeta distributa
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Methanobacterium sp.
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Natronococcus occultus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Natrinema pellirubrum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Mobiluncus mulieris
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Schaalia georgiae
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Acetobacter pasteurianus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Rhizobium sp.
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Hydrogenobaculum sp.
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Prevotella denticola
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Ralstonia solanacearum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Coraliomargarita akajimensis
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Verrucomicrobiia bacterium
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Pseudanabaena biceps
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Synechococcus sp.
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Caldithrix abyssi
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Denitrovibrio acetiphilus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Alkalidesulfovibrio alkalitolerans
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Campylobacter jejuni
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Helicobacter bilis
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Fibrobacter succinogenes
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Gemella haemolysans
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Bacillus cereus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Cetobacterium somerae
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Leptotrichia wadei
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Escherichia coli
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Pseudomonas sp.
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Winmispira thermophila
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Spiroplasma chrysopicola
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Mycoplasmopsis synoviae
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Trypanosoma cruzi
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Leishmania donovani
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Dictyostelium discoideum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Entamoeba histolytica
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Paramecium tetraurelia
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Plasmodium falciparum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Saccharomyces cerevisiae
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Schizosaccharomyces pombe
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Schizosaccharomyces japonicus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Aspergillus niger
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Colletotrichum gloeosporioides
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Phaeodactylum tricornutum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Thalassiosira pseudonana
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Ectocarpus siliculosus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Chlorella variabilis
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Chlamydomonas reinhardtii
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Genlisea aurea
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Selaginella moellendorffii
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Physcomitrium patens
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Solanum tuberosum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Populus trichocarpa
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Oryza sativa
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Triticum aestivum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Zea mays
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Arabidopsis thaliana
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Brassica rapa
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Toxoplasma gondii
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Hydra vulgaris
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Xenopus laevis
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Drosophila melanogaster
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Ascaris suum
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Caenorhabditis elegans
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Echinops telfairi
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Tupaia chinensis
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Mus musculus
4.2.1.130 physiological function glyoxalase III proteins in different systems demonstrate diverse functional capacities and play a vital role in oxidative stress response Homo sapiens