B1LIP1 (FRMA_ECOSM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 34.
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 (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 439855 [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_0000341284 | |||||
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] | "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5." Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R. J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SMS-3-5 / SECEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000970 Genomic DNA. Translation: ACB18273.1. |
| RefSeq | YP_001742490.1. NC_010498.1. |
3D structure databases | |
| ProteinModelPortal | B1LIP1. |
| SMR | B1LIP1. Positions 1-368. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B1LIP1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000065086; EBESCP00000062728; EBESCG00000064133. |
| GeneID | 6143543. |
| GenomeReviews | Gene locus EcSMS35_0387 in contig CP000970_GR. |
| KEGG | ecm:EcSMS35_0387. |
| PATRIC | 18429617. VBIEscCol6161_0560. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000008796. |
| HOGENOM | HBG753318. |
| OMA | VDHTFEC. |
| ProtClustDB | CLSK2393163. |
Enzyme and pathway databases | |
| BioCyc | ECOL439855:ECSMS35_0387-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_ECOSM | ||||||||
| Accession | Primary (citable) accession number: B1LIP1 | ||||||||
| 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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