B7LVS5 (PDXA_ESCF3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
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: 4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 Alternative name(s): 4-(phosphohydroxy)-L-threonine dehydrogenase | ||||
| Gene names |
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| Organism | Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585054 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP-Rule MF_00536 |
| Catalytic activity | 4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule MF_00536 |
| Cofactor | Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity. |
| Pathway | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP-Rule MF_00536 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is located at the dimer interface By similarity. HAMAP-Rule MF_00536 |
| Sequence similarities | Belongs to the PdxA family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridoxine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Cobalt Magnesium Metal-binding NAD NADP Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP NAD bindingInferred from electronic annotation. Source: InterPro cobalt ion bindingInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred 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 – 329 | 329 | 4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536 | PRO_1000128249 | |||||
Sites | |||||||||
| Metal binding | 166 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Metal binding | 211 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Metal binding | 266 | 1 | Divalent metal cation; shared with dimeric partner By similarity | ||||||
| Binding site | 136 | 1 | Substrate By similarity | ||||||
| Binding site | 137 | 1 | Substrate By similarity | ||||||
| Binding site | 274 | 1 | Substrate By similarity | ||||||
| Binding site | 283 | 1 | Substrate By similarity | ||||||
| Binding site | 292 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928158 Genomic DNA. Translation: CAQ87649.1. |
| RefSeq | YP_002381293.1. NC_011740.1. |
3D structure databases | |
| ProteinModelPortal | B7LVS5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 585054.EFER_0063. |
Proteomic databases | |
| PRIDE | B7LVS5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAQ87649; CAQ87649; EFER_0063. |
| GeneID | 7120816. |
| KEGG | efe:EFER_0063. |
| PATRIC | 32124553. VBIEscFer122920_0065. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1995. |
| HOGENOM | HOG000221592. |
| KO | K00097. |
| ProtClustDB | PRK00232. |
Enzyme and pathway databases | |
| BioCyc | EFER585054:GJJM-64-MONOMER. |
| UniPathway | UPA00244; UER00312. |
Family and domain databases | |
| Gene3D | 3.40.718.10. 1 hit. |
| HAMAP | MF_00536. PdxA. |
| InterPro | IPR024084. IsoPropMal-DH-like_dom. IPR005255. PyrdxlP_synth_PdxA. [Graphical view] |
| Pfam | PF04166. PdxA. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00557. pdxA. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PDXA_ESCF3 | ||||||||
| Accession | Primary (citable) accession number: B7LVS5 | ||||||||
| 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 |

Clusters with
