CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
20MLPAEVLKQAQQELRacetylation[1]
44MEVSHRGKEFIQVAEacetylation[2]
55QVAEEAEKDFRDLLNacetylation[2]
68LNVPSNYKVLFCHGGacetylation[2]
91PLNILGDKTTADYVDacetylation[2]
108YWAASAIKEAKKYCTacetylation[1, 2]
111ASAIKEAKKYCTPNVacetylation[2]
122TPNVFDAKVTVDGLRacetylation[2]
257GLVFKWLKANGGVAEacetylation[2]
267GGVAEMDKINQQKAEacetylation[2]
292FYRNDVAKANRSRMNacetylation[2]
311LADSALDKLFLEESFacetylation[2]
326AAGLHALKGHRVVGGacetylation[1, 2]
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. 
Interpro
 IPR000192; Aminotrans_V/Cys_dSase.
 IPR020578; Aminotrans_V_PyrdxlP_BS.
 IPR022278; Pser_aminoTfrase.
 IPR003248; Pser_aminoTfrase_subgr.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00266; Aminotran_5 
SMART
  
PROSITE
 PS00595; AA_TRANSFER_CLASS_5 
PRINTS