A4XTK4 (PDXB_PSEMY) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 37.
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: Erythronate-4-phosphate dehydrogenase EC=1.1.1.290 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas mendocina (strain ymp) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 399739 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 376 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01825 |
| 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. HAMAP MF_01825 |
| Subcellular location | Cytoplasm Potential HAMAP MF_01825. |
| 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 | pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4-phosphoerythronate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD bindingInferred from electronic annotation. Source: InterPro protein dimerization activityInferred 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 – 376 | 376 | Erythronate-4-phosphate dehydrogenase HAMAP MF_01825 | PRO_1000070404 | |||||
Regions | |||||||||
| Nucleotide binding | 126 – 127 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 201 – 203 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 203 | 1 | By similarity | ||||||
| Active site | 232 | 1 | By similarity | ||||||
| Active site | 249 | 1 | Proton donor By similarity | ||||||
| Binding site | 45 | 1 | Substrate By similarity | ||||||
| Binding site | 66 | 1 | Substrate By similarity | ||||||
| Binding site | 146 | 1 | NAD By similarity | ||||||
| Binding site | 174 | 1 | NAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 227 | 1 | NAD By similarity | ||||||
| Binding site | 252 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 253 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Pseudomonas mendocina ymp." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. Richardson P.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ymp. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000680 Genomic DNA. Translation: ABP84670.1. |
| RefSeq | YP_001187402.1. NC_009439.1. |
3D structure databases | |
| ProteinModelPortal | A4XTK4. |
| SMR | A4XTK4. Positions 1-373. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A4XTK4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5110036. |
| GenomeReviews | Gene locus Pmen_1908 in contig CP000680_GR. |
| KEGG | pmy:Pmen_1908. |
| PATRIC | 19910317. VBIPseMen131592_1932. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0111. |
| HOGENOM | HBG289972. |
| OMA | SAPGCNA. |
| PhylomeDB | A4XTK4. |
| ProtClustDB | PRK00257. |
Enzyme and pathway databases | |
| BioCyc | PMEN399739:PMEN_1908-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01825. PdxB. [Tree] |
| InterPro | IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR020921. Erythronate-4-P_DHase. IPR024531. Erythronate-4-P_DHase_dimer. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. |
| KO | K03473. |
| PANTHER | PTHR10996:SF4. Erythronate-4-P_DHase. 1 hit. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. PF11890. DUF3410. 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 | PDXB_PSEMY | ||||||||
| Accession | Primary (citable) accession number: A4XTK4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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