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Information on EC 1.1.1.202 - 1,3-propanediol dehydrogenase

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UNIPROT: Q9X022 not found.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
1,3-propanediol oxidoreductase, 1,3-propanediol dehydrogenase, 1,3-pd oxidoreductase, lr_1734, 1,3-pd dehydrogenase, lr_0030, 1,3-propanediol-oxidoreductase, nadh-dependent 1,3-propanediol oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,3-PD:NAD+ oxidoreductase
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1,3-propanediol dehydrogenase
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1,3-propanediol oxidoreductase
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1,3-propanediol:NAD oxidoreductase
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3-hydroxypropionaldehyde reductase
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dehydrogenase, 1,3-propanediol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
propane-1,3-diol:NAD+ 1-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
81611-70-3
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene TM0920, strain MSB8
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9X022_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
359
0
39943
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged protein in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, by nandroplet vapour diffusion method, cyrstallization buffer contains 20% PEG 300, 5% w/v PEG 8000, 10% glycerol, and 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis at 1.3 A resolution, modeling of 2 enzyme molecules, residues 1-359, complexed with 2 molecules of NADP+, 2 ions of Fe2+, 2 molecules of Tris, and 895 water molecules
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged selenomethionine-labeled enzyme from Escherichia coli by nickel affinity, ion exchange, and gel filtration chromatography and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TM0920, expression of soluble N-terminally MGSDKIHHHHHH-tagged selenomethionine-labeled enzyme in Escherichia coli methionine auxotrophic strain DL41
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwarzenbacher, R.; von Delft, F.; Canaves, J.M.; Brinen, L.S.; Dai, X.; Deacon, A.M.; Elsliger, M.A.; Eshaghi, S.; Floyd, R.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Guda, C.; Jaroszewski, L.; Karlak, C.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; McMullan, D.; McPhillips, T.M.; Miller, M.A.; Miller, M.D.; Morse, A.; Moy, K.; Ouyang, J.; Page, R.; Robb, A.; Rodrigues, K.; Selby, T.L.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Velasquez, J.; Vincent, J.; Wang, X.; West, B.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Wilson, I.A.
Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolution
Proteins
54
174-177
2003
Thermotoga maritima (Q9X022), Thermotoga maritima
Manually annotated by BRENDA team