ID D5TRB2_BACT1 Unreviewed; 417 AA.
AC D5TRB2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 01-MAY-2013, entry version 24.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; OrderedLocusNames=BMB171_C2920;
OS Bacillus thuringiensis (strain BMB171).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=714359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BMB171;
RX PubMed=20525827; DOI=10.1128/JB.00562-10;
RA He J., Shao X., Zheng H., Li M., Wang J., Zhang Q., Li L., Liu Z.,
RA Sun M., Wang S., Yu Z.;
RT "Complete genome sequence of Bacillus thuringiensis mutant strain
RT BMB171.";
RL J. Bacteriol. 192:4074-4075(2010).
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 -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC from 3-phospho-D-glycerate: step 2/3.
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; CP001903; ADH07730.1; -; Genomic_DNA.
DR RefSeq; YP_003665450.1; NC_014171.1.
DR EnsemblBacteria; ADH07730; ADH07730; BMB171_C2920.
DR GeneID; 9193961; -.
DR KEGG; btb:BMB171_C2920; -.
DR PATRIC; 38132719; VBIBacThu148000_3144.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR BioCyc; BTHU714359:GJBQ-3035-MONOMER; -.
DR UniPathway; UPA00135; UER00197.
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 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; Serine biosynthesis; Transferase.
FT REGION 133 134 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 294 295 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 99 99 L-glutamate (By similarity).
FT BINDING 159 159 Pyridoxal phosphate (By similarity).
FT BINDING 209 209 Pyridoxal phosphate (By similarity).
FT BINDING 229 229 Pyridoxal phosphate (By similarity).
FT BINDING 252 252 Pyridoxal phosphate (By similarity).
FT MOD_RES 253 253 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 417 AA; 46969 MW; F3F325900BC15B7C CRC64;
MYLTLFYMSI KKSALASDSI ASCALIIENK LTTYYILGYN SESLKNNPMR NREVMRVMER
VYNFSAGPSI LPLPVLEKVQ KELLNYNGTG MSIMEMSHRS SYFQSIIEEA SNLLRELMSI
PDEYEVLFLQ GGASLQFSMI PLNLMNTYKK AGYVLTGSWS KKALQEAEKV GEVQVIASSE
QEKFTKIPKL DGLLSDEKLD YVHITTNNTI EGTKYVGIPH VERVPLVADM SSNILSEQYD
VSKFGLIYAG AQKNLGPAGL TIAIIKRDLI GGADRSCPTM LNYETYSKNN SLYNTPPSFS
IYVTKLVLEW LKEQGGVSAI EEQNRMKSSL IYHFLDESKL FTSPVDPAYR SLMNIPFTTP
SEELNNEFLQ KAKERGLVTL KGHRSVGGMR ASIYNAMPVQ GVQQLVNYMK EFELENR
//
