Tag | Content |
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CPLM ID | CPLM-005215 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoserine aminotransferase |
Protein Synonyms/Alias | Phosphohydroxythreonine aminotransferase; PSAT |
Gene Name | serC |
Gene Synonyms/Alias | pdxC; pdxF; b0907; JW0890 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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20 | MLPAEVLKQAQQELR | acetylation | [1] | 44 | MEVSHRGKEFIQVAE | acetylation | [2] | 55 | QVAEEAEKDFRDLLN | acetylation | [2] | 68 | LNVPSNYKVLFCHGG | acetylation | [2] | 91 | PLNILGDKTTADYVD | acetylation | [2] | 108 | YWAASAIKEAKKYCT | acetylation | [1, 2] | 111 | ASAIKEAKKYCTPNV | acetylation | [2] | 122 | TPNVFDAKVTVDGLR | acetylation | [2] | 257 | GLVFKWLKANGGVAE | acetylation | [2] | 267 | GGVAEMDKINQQKAE | acetylation | [2] | 292 | FYRNDVAKANRSRMN | acetylation | [2] | 311 | LADSALDKLFLEESF | acetylation | [2] | 326 | AAGLHALKGHRVVGG | acetylation | [1, 2] |
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Reference | [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis. |
Sequence Annotation | REGION 76 77 Pyridoxal phosphate binding. REGION 239 240 Pyridoxal phosphate binding. BINDING 9 9 L-glutamate. BINDING 42 42 L-glutamate. BINDING 102 102 Pyridoxal phosphate. BINDING 153 153 Pyridoxal phosphate. BINDING 174 174 Pyridoxal phosphate. BINDING 197 197 Pyridoxal phosphate. MOD_RES 198 198 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Pyridoxal phosphate; Pyridoxine biosynthesis; Reference proteome; Serine biosynthesis; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 362 AA |
Protein Sequence | MAQIFNFSSG PAMLPAEVLK QAQQELRDWN GLGTSVMEVS HRGKEFIQVA EEAEKDFRDL 60 LNVPSNYKVL FCHGGGRGQF AAVPLNILGD KTTADYVDAG YWAASAIKEA KKYCTPNVFD 120 AKVTVDGLRA VKPMREWQLS DNAAYMHYCP NETIDGIAID ETPDFGADVV VAADFSSTIL 180 SRPIDVSRYG VIYAGAQKNI GPAGLTIVIV REDLLGKANI ACPSILDYSI LNDNGSMFNT 240 PPTFAWYLSG LVFKWLKANG GVAEMDKINQ QKAELLYGVI DNSDFYRNDV AKANRSRMNV 300 PFQLADSALD KLFLEESFAA GLHALKGHRV VGGMRASIYN AMPLEGVKAL TDFMVEFERR 360 HG 362 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IDA:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP. GO:0006564; P:L-serine biosynthetic process; IMP:EcoCyc. GO:0042823; P:pyridoxal phosphate biosynthetic process; IMP:EcoCyc. GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP. |
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