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Literature summary extracted from

  • Miranda, H.; Antelmann, H.; Hepowit, N.; Chavarria, N.; Krause, D.; Pritz, J.; Bäsell, K.; Becher, D.; Humbard, M.; Brocchieri, L.; Maupin-Furlow, J.
    Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism (2014), Mol. Cell. Proteomics, 13, 220-239 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.2.1.55 DMSO levels of samp3ylated proteins and samp3 transcripts are increased by the addition of dimethyl sulfoxide to aerobically growing cells Haloferax volcanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.55 Mg2+ required Haloferax volcanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.100 ATP + [SAMP3]-Gly-Gly Haloferax volcanii
-
 diphosphate + [SAMP3]-Gly-Gly-AMP
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine Haloferax volcanii
-
 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2
-
 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 additional information Haloferax volcanii the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase ?
-
 ?
6.2.1.55 additional information Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.100 Haloferax volcanii
-
-
-
6.2.1.55 Haloferax volcanii D4GSF3
-
-
6.2.1.55 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 D4GSF3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.100 ATP + [SAMP3]-Gly-Gly
-
 Haloferax volcanii diphosphate + [SAMP3]-Gly-Gly-AMP
-
 ?
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
-
 Haloferax volcanii AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 from Haloferax volcanii strain H26 Haloferax volcanii AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine
-
 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine SAMP3 from Haloferax volcanii strain H26 Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine]
-
 r
6.2.1.55 additional information the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase Haloferax volcanii ?
-
 ?
6.2.1.55 additional information phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview Haloferax volcanii ?
-
 ?
6.2.1.55 additional information the molybdopterin (MPT) synthase large subunit homologue MoaE is samp3ylated at conserved active site lysine residues determined by MS/MS analysis, immunoprecipitation, and tandem affinity purifications. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 ?
-
 ?
6.2.1.55 additional information phylogenetic and sequence analysis and comparison of SAMP3 substrate, overview Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.100 UbaA
-
 Haloferax volcanii
6.2.1.55 E1 enzyme homologue
-
 Haloferax volcanii
6.2.1.55 UbaA
-
 Haloferax volcanii

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.55 ATP
-
 Haloferax volcanii

General Information

EC Number General Information Comment Organism
6.2.1.55 physiological function the novel small archaeal modifier protein (SAMP3) with a beta-grasp fold and C-terminal diglycine motif characteristic of ubiquitin is functional in protein conjugation in Haloferax volcanii. Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism. SAMP3 conjugates are dependent on the ubiquitin-activating E1 enzyme homologue of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1. Samp3ylation is covalent and reversible and controls the activity of enzymes such as MPT synthase. Sampylation of MPT synthase may govern the levels of molybdenum cofactor available and thus facilitate the scavenging of oxygen prior to the transition to respiration with molybdenum-cofactor-containing terminal reductases that use alternative electron acceptors such as dimethyl sulfoxide Haloferax volcanii