Reviewed,
UniProtKB/Swiss-Prot P44336 (SERC_HAEIN)
Last modified
June 16, 2009.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (3) |
 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 |
| ||||
| Organism | Haemophilus influenzae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 727 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 362 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 – 362 | 362 | Phosphoserine aminotransferase HAMAP MF_00160 | PRO_0000150174 | |||||
Regions | |||||||||
| Region | 76 – 77 | 2 | Pyridoxal phosphate binding By similarity | ||||||
| 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 | 172 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 195 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 196 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I.  Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| L42023 Genomic DNA. Translation: AAC22822.1. | |
| PIR | E64187. |
| RefSeq | NP_439325.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BJN based on UniProtKB P23721. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 949636. |
| GenomeReviews | Gene locus HI1167 in contig L42023_GR. |
| KEGG | hin:HI1167. |
| NMPDR | fig|71421.1.peg.1120. |
| TIGR | HI1167. |
Phylogenomic databases | |
| HOGENOM | P44336. |
| OMA | P44336. SMYNTPP. |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_1167-MON. |
| BRENDA | 2.6.1.52. 109. |
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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SERC_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P44336 | ||||||||
| 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
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
