Reviewed,
UniProtKB/Swiss-Prot B6J1E0 (SERC_COXB2)
Last modified
October 13, 2009.
Version 9.
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 | Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 434923 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella |
Protein attributes
| Sequence length | 360 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-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. |
| 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 – 360 | 360 | Phosphoserine aminotransferase HAMAP MF_00160 | PRO_1000097211 | |||||
Regions | |||||||||
| Region | 237 – 238 | 2 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 42 | 1 | L-glutamate By similarity | ||||||
| Binding site | 102 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 152 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 171 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 194 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 195 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella." Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A. Infect. Immun. 77:642-656(2009) [PubMed: 19047403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP001019 Genomic DNA. Translation: ACJ18768.1. | |
| RefSeq | YP_002303913.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 7013885. |
| GenomeReviews | Gene locus CbuG_1469 in contig CP001019_GR. |
| KEGG | cbg:CbuG_1469. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_00160. [Tree] |
| InterPro | IPR000192. Aminotrans_V/Cys_dSase. IPR020578. Aminotrans_V_PyrdxlP_BS. 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] |
| TIGRFAMs | TIGR01364. serC_1. 1 hit. |
| PROSITE | PS00595. AA_TRANSFER_CLASS_5. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERC_COXB2 | ||||||||
| Accession | Primary (citable) accession number: B6J1E0 | ||||||||
| 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


