Q2L2T1 (SERC_BORA1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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 | Bordetella avium (strain 197N) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360910 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 376 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 MF_00160 |
| Catalytic activity | O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP MF_00160 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP MF_00160 |
| Cofactor | Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP MF_00160 |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP MF_00160 Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP MF_00160 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00160 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00160. |
| Sequence similarities | Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. |
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: UniProtKB-KW pyridoxine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| 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: EC pyridoxal phosphate 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 – 376 | 376 | Phosphoserine aminotransferase HAMAP MF_00160 | PRO_1000058201 | |||||
Regions | |||||||||
| Region | 253 – 254 | 2 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 42 | 1 | L-glutamate By similarity | ||||||
| Binding site | 104 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 163 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 188 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 211 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 212 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 197N. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM167904 Genomic DNA. Translation: CAJ48957.1. |
| RefSeq | YP_785870.1. NC_010645.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2C0R based on UniProtKB Q59196. |
| ProteinModelPortal | Q2L2T1. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2L2T1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6267140. |
| GenomeReviews | Gene locus BAV1348 in contig AM167904_GR. |
| KEGG | bav:BAV1348. |
| NMPDR | fig|521.1.peg.520. |
| PATRIC | 21128888. VBIBorAvi43433_1367. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG289982. |
| OMA | VPENYKV. |
| ProtClustDB | PRK05355. |
Enzyme and pathway databases | |
| BioCyc | ABAU360910:BAV1348-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00160. SerC_aminotrans_5. [Tree] |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. IPR022278. Pser_aminoTfrase. IPR003248. Pser_aminoTfrase_subgr. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| KO | K00831. |
| 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_BORA1 | ||||||||
| Accession | Primary (citable) accession number: Q2L2T1 | ||||||||
| 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