Reviewed,
UniProtKB/Swiss-Prot A8FKB5 (SERC_CAMJ8)
Last modified
June 16, 2009.
Version 14.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 | Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 407148 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 358 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: 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. |
| Subcellular location | Cytoplasm By similarity. |
| 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 – 358 | 358 | Phosphoserine aminotransferase HAMAP MF_00160 | PRO_1000071542 | |||||
Regions | |||||||||
| Region | 75 – 76 | 2 | Pyridoxal phosphate binding By similarity | ||||||
| Region | 233 – 234 | 2 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 41 | 1 | L-glutamate By similarity | ||||||
| Binding site | 100 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 148 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 167 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 190 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 191 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)." Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M. J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000814 Genomic DNA. Translation: ABV51902.1. | |
| RefSeq | YP_001481879.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5618480. |
| GenomeReviews | Gene locus C8J_0303 in contig CP000814_GR. |
| KEGG | cju:C8J_0303. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A8FKB5. SMYNTPP. |
Family and domain databases | |
| HAMAP | MF_00160. [Tree] |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR003248. Pser_amintransf. 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] |
| ProDom | PD001544. Pser_amintransf. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01364. serC_1. 1 hit. |
| PROSITE | PS00595. AA_TRANSFER_CLASS_5. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERC_CAMJ8 | ||||||||
| Accession | Primary (citable) accession number: A8FKB5 | ||||||||
| Entry history |
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| 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 |

Clusters with


