Reviewed,
UniProtKB/Swiss-Prot P58220 (GHRB_ECO57)
Last modified
January 19, 2010.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glyoxylate/hydroxypyruvate reductase B EC=1.1.1.79 EC=1.1.1.81 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 324 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively By similarity. HAMAP MF_01667 |
| Catalytic activity | Glycolate + NADP+ = glyoxylate + NADPH. HAMAP MF_01667 D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H. HAMAP MF_01667 |
| Subunit structure | Homodimer Probable. HAMAP MF_01667 |
| Subcellular location | Cytoplasm Probable HAMAP MF_01667. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: HAMAP |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyoxylate reductase (NADP) activityInferred from electronic annotation. Source: HAMAP hydroxypyruvate reductase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 324 | 324 | Glyoxylate/hydroxypyruvate reductase B HAMAP MF_01667 | PRO_0000076030 | |||||
Sites | |||||||||
| Active site | 237 | 1 | By similarity | ||||||
| Active site | 266 | 1 | By similarity | ||||||
| Active site | 285 | 1 | Proton donor 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 | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG58702.1. Different initiation. BA000007 Genomic DNA. Translation: BAB37861.1. Different initiation. |
| PIR | B86030. F91183. |
| RefSeq | NP_290138.2. NP_312465.2. |
3D structure databases | |
| SMR | P58220. Positions 1-323. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 915671. 961060. |
| GenomeReviews | Gene locus Z4978 in contig AE005174_GR. Gene locus ECs4438 in contig BA000007_GR. |
| KEGG | ece:Z4978. ecs:ECs4438. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG731446. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4438-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01667. 2-Hacid_dh_C_GhrB. [Tree] |
| InterPro | IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. False negative. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GHRB_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P58220 | ||||||||
| 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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