Reviewed,
UniProtKB/Swiss-Prot Q7W5Z9 (SERC_BORPA)
Last modified
February 9, 2010.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (2) |
 Third-party data |
 Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Phosphoserine aminotransferase EC=2.6.1.52 Alternative name(s): Phosphohydroxythreonine aminotransferase Short name=PSAT | ||||
| Gene names |
| ||||
| Organism | Bordetella parapertussis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 519 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella |
Protein attributes
| Sequence length | 377 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: HAMAP 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: 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 – 377 | 377 | Phosphoserine aminotransferase HAMAP MF_00160 | PRO_0000150156 | |||||
Regions | |||||||||
| Region | 254 – 255 | 2 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 43 | 1 | L-glutamate By similarity | ||||||
| Binding site | 105 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 164 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 189 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 212 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 213 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.  Maskell D.J.Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12822 / ATCC BAA-587 / NCTC 13253. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX640432 Genomic DNA. Translation: CAE38418.1. |
| RefSeq | NP_885308.1. |
3D structure databases | |
| SMR | Q7W5Z9. Positions 5-377. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1666661. |
| KEGG | bpa:BPP3133. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG289982. |
| OMA | TFAWYLA. |
| PhylomeDB | Q7W5Z9. |
Enzyme and pathway databases | |
| BioCyc | BPAR257311:BPP3133-MONOMER. |
| BRENDA | 2.6.1.52. 263123. |
Family and domain databases | |
| HAMAP | MF_00160. SerC_aminotrans_5. [Tree] |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR003248. Pser_amintransf. 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. |
| Pfam | PF00266. Aminotran_5. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01364. serC_1. 1 hit. |
| PROSITE | PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERC_BORPA | ||||||||
| Accession | Primary (citable) accession number: Q7W5Z9 | ||||||||
| Entry history |
| ||||||||
| 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 |
