A1A835 (FRMA_ECOK1) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 45.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: S-(hydroxymethyl)glutathione dehydrogenase EC=1.1.1.284 | ||||||
| Gene names |
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| Organism | Escherichia coli O1:K1 / APEC [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 405955 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 369 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent By similarity. |
| Catalytic activity | S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H. An alcohol + NAD+ = an aldehyde or ketone + NADH. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ethanol oxidation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | S-(hydroxymethyl)glutathione dehydrogenase activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activityInferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 369 | 369 | S-(hydroxymethyl)glutathione dehydrogenase | PRO_0000341288 | |||||
Sites | |||||||||
| Metal binding | 40 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 62 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 92 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 95 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 98 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 106 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 169 | 1 | Zinc 1; catalytic By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes." Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K. J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000468 Genomic DNA. Translation: ABI99824.1. |
| RefSeq | YP_851539.1. NC_008563.1. |
3D structure databases | |
| ProteinModelPortal | A1A835. |
| SMR | A1A835. Positions 1-368. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A1A835. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000039135; EBESCP00000037652; EBESCG00000038185. |
| GeneID | 4494461. |
| GenomeReviews | Gene locus Ecok1_03310 in contig CP000468_GR. |
| KEGG | ecv:APECO1_1645. |
| PATRIC | 18212106. VBIEscCol127180_0357. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1062. |
| GeneTree | EBGT00050000008796. |
| HOGENOM | HBG753318. |
| OMA | VDHTFEC. |
| ProtClustDB | CLSK2393163. |
Enzyme and pathway databases | |
| BioCyc | ECOL405955:APECO1_1645-MONOMER. |
Family and domain databases | |
| InterPro | IPR014183. ADH_3. IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00121. |
| PANTHER | PTHR11695. ADH_Sf_Zn. 1 hit. |
| Pfam | PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view] |
| SUPFAM | SSF50129. GroES_like. 2 hits. |
| TIGRFAMs | TIGR02818. Adh_III_F_hyde. 1 hit. |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FRMA_ECOK1 | ||||||||
| Accession | Primary (citable) accession number: A1A835 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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