ID B0KTX7_PSEPG Unreviewed; 335 AA.
AC B0KTX7;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; OrderedLocusNames=PputGB1_1359;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABY97266.1; -; Genomic_DNA.
DR RefSeq; YP_001667602.1; NC_010322.1.
DR ProteinModelPortal; B0KTX7; -.
DR SMR; B0KTX7; 1-335.
DR STRING; 76869.PputGB1_1359; -.
DR EnsemblBacteria; ABY97266; ABY97266; PputGB1_1359.
DR GeneID; 5869123; -.
DR KEGG; ppg:PputGB1_1359; -.
DR PATRIC; 19929699; VBIPsePut76638_1365.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
DR BioCyc; PPUT76869:GIXB-1394-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 51 52 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 212 213 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 17 17 L-glutamate (By similarity).
FT BINDING 77 77 Pyridoxal phosphate (By similarity).
FT BINDING 127 127 Pyridoxal phosphate (By similarity).
FT BINDING 147 147 Pyridoxal phosphate (By similarity).
FT BINDING 170 170 Pyridoxal phosphate (By similarity).
FT MOD_RES 171 171 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 335 AA; 37091 MW; 070060C7AADD4827 CRC64;
MLDWRGKGLS VMEMSHRSDD YVAIAEKAEQ DLRDLLSVPS NYKVLFLQGG ASQQFAEIPL
NLLPENGTAD YIETGIWSKK AIEEARRFGN VNVAASAKPY DYLAIPGQNE WSLTKNAAYV
HYASNETIGG LQFDWVPETG DVPLVVDMSS DILSRPIDVS QYGLIYAGAQ KNIGPSGLVV
VIVREDLLGR ARSSCPTMLD YKVSADNGSM YNTPATYSWY LSGLVFEWLK EQGGVDAMEQ
RNRAKKERLY GFIDNSDFYT NPISVNARSW MNVPFRLADE RLDKAFLAGA DARGLLNLKG
HRSVGGMRAS IYNALGLEAV DALVGYMAEF EKEHG
//
