Reviewed,
UniProtKB/Swiss-Prot P0AET9 (HDHA_ECO57)
Last modified
June 16, 2009.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 7-alpha-hydroxysteroid dehydrogenase Short name=7-alpha-HSDH EC=1.1.1.159 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 255 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | 7-alpha-dehydroxylation of cholic acid, yielding deoxycholic acid and lithocholic acid, respectively. Highest affinity with taurochenodeoxycholic acid By similarity. |
| Catalytic activity | 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD+ = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Bile acid catabolism Lipid metabolism Steroid metabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | bile acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 7-alpha-hydroxysteroid dehydrogenase activity Inferred from electronic annotation. Source: EC 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 – 255 | 255 | 7-alpha-hydroxysteroid dehydrogenase | PRO_0000054709 | |||||
Regions | |||||||||
| Nucleotide binding | 18 – 42 | 25 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 159 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 146 | 1 | Substrate By similarity | ||||||
| Binding site | 163 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG56608.1. BA000007 Genomic DNA. Translation: BAB35750.1. | |
| PIR | D85768. G90919. |
| RefSeq | NP_288055.1. NP_310354.1. |
3D structure databases | |
| SMR | P0AET9. Positions 1-255. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 912528. 961569. |
| GenomeReviews | Gene locus Z2624 in contig AE005174_GR. Gene locus ECs2327 in contig BA000007_GR. |
| KEGG | ece:Z2624. ecs:ECs2327. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0AET9. |
| OMA | P0AET9. WRCDITS. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS2327-MON. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HDHA_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AET9 Secondary accession number(s): P25529 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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