Reviewed,
UniProtKB/Swiss-Prot Q0VQC3 (PDXB_ALCBS)
Last modified
June 16, 2009.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Erythronate-4-phosphate dehydrogenase EC=1.1.1.290 | ||||
| Gene names |
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| Organism | Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 393595 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax |
Protein attributes
| Sequence length | 371 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate By similarity. |
| Catalytic activity | 4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. HAMAP MF_01825 |
| Pathway | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5. HAMAP MF_01825 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridoxine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4-phosphoerythronate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD or NADH 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 – 371 | 371 | Erythronate-4-phosphate dehydrogenase HAMAP MF_01825 | PRO_0000297432 | |||||
Sites | |||||||||
| Active site | 208 | 1 | By similarity | ||||||
| Active site | 237 | 1 | By similarity | ||||||
| Active site | 254 | 1 | Proton donor By similarity | ||||||
| Binding site | 44 | 1 | Substrate By similarity | ||||||
| Binding site | 65 | 1 | Substrate By similarity | ||||||
| Binding site | 145 | 1 | NAD By similarity | ||||||
| Binding site | 232 | 1 | NAD By similarity | ||||||
| Binding site | 257 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 258 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. Golyshin P.N.Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM286690 Genomic DNA. Translation: CAL16625.1. Different initiation. | |
| RefSeq | YP_692897.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4212449. |
| GenomeReviews | Gene locus ABO_1177 in contig AM286690_GR. |
| KEGG | abo:ABO_1177. |
| NMPDR | fig|393595.12.peg.1189. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q0VQC3. |
Enzyme and pathway databases | |
| BioCyc | ABOR393595:ABO_1177-MON. |
Family and domain databases | |
| HAMAP | MF_01825. [Tree] |
| InterPro | IPR006139. D-isomer_2_OHA_DH. IPR006140. D-isomer_2_OHA_DH_NAD-bd. [Graphical view] |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PDXB_ALCBS | ||||||||
| Accession | Primary (citable) accession number: Q0VQC3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


