Tag | Content |
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CPLM ID | CPLM-026634 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoserine aminotransferase |
Protein Synonyms/Alias | |
Gene Name | serC |
Gene Synonyms/Alias | RPA4309 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
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67 | LEVPADYKIGIVPAS | acetylation | [1] | 113 | GDITKELKLPNVTKL | acetylation | [1] | 330 | EAQADFAKKLVAAVE | acetylation | [1] |
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Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine (By similarity). |
Sequence Annotation | |
Keyword | Amino-acid biosynthesis; Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; Serine biosynthesis; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 390 AA |
Protein Sequence | MTVAKPASRP NAPQFSSGPC AKRPGWTPEN LKDAPLGRSH RAKVGKAKLK LAIDLTRDVL 60 EVPADYKIGI VPASDTGAVE MALWSLLGPR PVTTLAWESF GDGWVGDITK ELKLPNVTKL 120 KAGYGEIPDL SKVDCNTDVV FTWNGTTSGV RVPNADWIKA DREGLTICDA TSAAFAQPLD 180 WAKLDVVTFS WQKALGGEAA HGMLILSPRA VARLESYTPT WPMPKIFRLT KGGKLMEGIF 240 QGETINTPSM LCVEDYIDAL QWAKSVGGLK GLIARADANT KVLTDWQAKT PWVDFLAKDP 300 AIRSNTSVCL KVVDPAITAL SPEAQADFAK KLVAAVEKEG AGFDLGAYRD APPGLRIWCG 360 ATVEAADVAA LTQWLDWAFE TTKASLTQAA 390 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:EC. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |