ID Q48FM8_PSE14 Unreviewed; 380 AA.
AC Q48FM8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 29-MAY-2013, entry version 69.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; OrderedLocusNames=PSPPH_3666;
OS Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J.,
RA Creasy T., Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H., Feldblyum T., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D.J., Mansfield J.,
RA Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT phaseolicola 1448A reveals divergence among pathovars in genes
RT involved in virulence and transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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: 4-phosphonooxy-L-threonine + 2-oxoglutarate =
CC (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.
CC -!- CATALYTIC ACTIVITY: O-phospho-L-serine + 2-oxoglutarate = 3-
CC phosphonooxypyruvate + 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.
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DR EMBL; CP000058; AAZ36896.1; -; Genomic_DNA.
DR RefSeq; YP_275808.1; NC_005773.3.
DR ProteinModelPortal; Q48FM8; -.
DR SMR; Q48FM8; 23-380.
DR STRING; 264730.PSPPH_3666; -.
DR World-2DPAGE; 0008:Q48FM8; -.
DR EnsemblBacteria; AAZ36896; AAZ36896; PSPPH_3666.
DR GeneID; 3559526; -.
DR KEGG; psp:PSPPH_3666; -.
DR PATRIC; 19976758; VBIPseSyr78478_3843.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
DR BioCyc; PSAV264730:GKDE-3669-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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW Serine biosynthesis; Transferase.
FT REGION 96 97 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 257 258 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 62 62 L-glutamate (By similarity).
FT BINDING 122 122 Pyridoxal phosphate (By similarity).
FT BINDING 172 172 Pyridoxal phosphate (By similarity).
FT BINDING 192 192 Pyridoxal phosphate (By similarity).
FT BINDING 215 215 Pyridoxal phosphate (By similarity).
FT MOD_RES 216 216 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 380 AA; 41970 MW; 21F0C5D2849FCF9F CRC64;
MASNQKQART DPTYLTRVDM SKRAFNFCAG PAALPEAVLL RAQAELLDWH GKGLSVMEMS
HRSDEFVSIA TKAEQDLRDL LSIPSNYKVL FLQGGASQQF AQIALNLLPE NGKADYIDTG
IWSQKAIDEA SRYGTVNVAA SAKPYDYFAI PGQNEWKLSK DAAYVHYAPN ETIGGLEFNW
IPETGDVPLV ADMSSDILSR PVDISRFGMI YAGAQKNIGP SGIVVVIIRE DLLGRARSLC
PTMLDYKVAA DNGSMYNTPP TLAWYLSGLV FEWLKEQGGV EAIGKRNDIK QRTLYDFIDA
SELYSNPINK PDRSWMNVPF RLADDRLDKP FLAGADANGL LNLKGHRSVG GMRASIYNAV
DINAVNALVA YMKDFEKEHG
//
