Q87QA3 (SERC_VIBPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 75.
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: Phosphoserine aminotransferase EC=2.6.1.52 Alternative name(s): Phosphohydroxythreonine aminotransferase Short name=PSAT | ||||
| Gene names |
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| Organism | Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 223926 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › ![]() |
Protein attributes
| Sequence length | 364 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP-Rule MF_00160 |
| Catalytic activity | O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule MF_00160 |
| Cofactor | Binds 1 pyridoxal phosphate per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP-Rule MF_00160 Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule MF_00160 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. |
| Sequence caution | The sequence BAC59510.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Pyridoxine biosynthesis Serine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Aminotransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | L-serine 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 | O-phospho-L-serine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate 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 – 364 | 364 | Phosphoserine aminotransferase HAMAP-Rule MF_00160 | PRO_0000150216 | |||||
Regions | |||||||||
| Region | 80 – 81 | 2 | Pyridoxal phosphate binding By similarity | ||||||
| Region | 241 – 242 | 2 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 46 | 1 | L-glutamate By similarity | ||||||
| Binding site | 106 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 157 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 176 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 199 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 200 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000031 Genomic DNA. Translation: BAC59510.1. Different initiation. |
| RefSeq | NP_797626.1. NC_004603.1. |
3D structure databases | |
| ProteinModelPortal | Q87QA3. |
| SMR | Q87QA3. Positions 8-364. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 223926.VP1247. |
Proteomic databases | |
| PRIDE | Q87QA3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAC59510; BAC59510; BAC59510. |
| GeneID | 1188752. |
| KEGG | vpa:VP1247. |
| PATRIC | 20140698. VBIVibPar50997_1186. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1932. |
| HOGENOM | HOG000088965. |
| KO | K00831. |
| OMA | MSIMEMS. |
| ProtClustDB | PRK05355. |
Enzyme and pathway databases | |
| UniPathway | UPA00135; UER00197. UPA00244; UER00311. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| HAMAP | MF_00160. SerC_aminotrans_5. |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR022278. Pser_aminoTfrase. IPR003248. Pser_aminoTfrase_subgr. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| PANTHER | PTHR21152:SF1. PTHR21152:SF1. 1 hit. |
| Pfam | PF00266. Aminotran_5. 1 hit. [Graphical view] |
| PIRSF | PIRSF000525. SerC. 1 hit. |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR01364. serC_1. 1 hit. |
| PROSITE | PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERC_VIBPA | ||||||||
| Accession | Primary (citable) accession number: Q87QA3 | ||||||||
| 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
