ID SERC_SALPC Reviewed; 362 AA.
AC C0PXU3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; OrderedLocusNames=SPC_0976;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T.,
RA Peng Y.-H., Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R.,
RA Liu S.-L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella
RT choleraesuis and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine (By similarity).
CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC phosphonooxypyruvate + L-glutamate.
CC -!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC -!- COFACTOR: Binds 1 pyridoxal phosphate per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC from 3-phospho-D-glycerate: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000857; ACN45143.1; -; Genomic_DNA.
DR RefSeq; YP_002636584.1; NC_012125.1.
DR ProteinModelPortal; C0PXU3; -.
DR SMR; C0PXU3; 3-362.
DR STRING; 476213.SPC_0976; -.
DR PRIDE; C0PXU3; -.
DR EnsemblBacteria; ACN45143; ACN45143; SPC_0976.
DR GeneID; 7553476; -.
DR KEGG; sei:SPC_0976; -.
DR PATRIC; 32360780; VBISalEnt12305_1031.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
DR BioCyc; SENT476213:GH8J-994-MONOMER; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:HAMAP.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1; -.
DR InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR003248; Pser_aminoTfrase_subgr.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR21152:SF1; PTHR21152:SF1; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW Serine biosynthesis; Transferase.
FT CHAIN 1 362 Phosphoserine aminotransferase.
FT /FTId=PRO_1000203558.
FT REGION 76 77 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 239 240 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 9 9 L-glutamate (By similarity).
FT BINDING 42 42 L-glutamate (By similarity).
FT BINDING 102 102 Pyridoxal phosphate (By similarity).
FT BINDING 153 153 Pyridoxal phosphate (By similarity).
FT BINDING 174 174 Pyridoxal phosphate (By similarity).
FT BINDING 197 197 Pyridoxal phosphate (By similarity).
FT MOD_RES 198 198 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 362 AA; 39885 MW; 8A9BC4A74D312FB7 CRC64;
MAQVFNFSSG PAMLPAEVLK LAQQELRDWH GLGTSVMEIS HRGKEFIQVA EEAEQDFRDL
LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG YWAASAIKEA KKYCAPQIID
AKITVDGKRA VKPMREWQLS DNAAYLHYCP NETIDGIAID ETPDFGPEVV VTADFSSTIL
SAPLDVSRYG VIYAGAQKNI GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT
PPTFAWYLSG LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV
PFQLADNTLD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL TDFMIDFERR
HG
//
