ID   SERC_BURCM              Reviewed;         360 AA.
AC   Q0BH96;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
DE            Short=PSAT;
GN   Name=serC; OrderedLocusNames=Bamb_0918;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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: 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-glyceric acid: 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; CP000440; ABI86477.1; -; Genomic_DNA.
DR   RefSeq; YP_772811.1; -.
DR   GeneID; 4310385; -.
DR   GenomeReviews; CP000440_GR; Bamb_0918.
DR   KEGG; bam:Bamb_0918; -.
DR   NMPDR; fig|339670.3.peg.2003; -.
DR   OMA; Q0BH96; SMYNTPP.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotran...; 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:UniProtKB-KW.
DR   HAMAP; MF_00160; -; 1.
DR   InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR   InterPro; IPR003248; Pser_amintransf.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   ProDom; PD001544; Pser_amintransf; 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    360       Phosphoserine aminotransferase.
FT                                /FTId=PRO_1000058204.
FT   REGION      237    238       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      41     41       L-glutamate (By similarity).
FT   BINDING     101    101       Pyridoxal phosphate (By similarity).
FT   BINDING     152    152       Pyridoxal phosphate (By similarity).
FT   BINDING     172    172       Pyridoxal phosphate (By similarity).
FT   BINDING     195    195       Pyridoxal phosphate (By similarity).
FT   MOD_RES     196    196       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   360 AA;  39354 MW;  8CC21EA73E31CB0F CRC64;
     MRVFNFSAGP AALPEEVLRQ AADEMLDWHG SGMSVMEMSH RGKEFMSIHE AALADLRELL
     DVPASHRILF LQGGGIAENA IVPMNLLGSR QTADFVVTGS WSQKSFNEAK KYGTPHLAAS
     GKTADGFTRA PARAEWQLSD DPAYVHLCTN ETIDGVETFE IPDLGDIPLV ADVSSHILSR
     PMDVAKYGVL FGGAQKNIGM AGVTVVIVRE DLLDRALSIC PSAFEWKTVA ANNSLYNTPP
     TYAIYIAGLV FQWLKRQGGL EAIEARNIEK AKLLYDTIDA SGFYLNKVEP AVRSRMNVPF
     FLADETRNED FLAGAKARGL LQLKGHKSVG GMRASIYNAV PLEGVKALVE YMKDFEQRGA
//