ID SERC_LACH4 Reviewed; 373 AA.
AC A8YW78;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 01-MAY-2013, entry version 39.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
DE Short=PSAT;
GN Name=serC; OrderedLocusNames=lhv_0048;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/JB.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism
RT distinguished by selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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 -!- 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; CP000517; ABX26333.1; -; Genomic_DNA.
DR RefSeq; YP_001576620.1; NC_010080.1.
DR ProteinModelPortal; A8YW78; -.
DR STRING; 405566.lhv_0048; -.
DR EnsemblBacteria; ABX26333; ABX26333; lhv_0048.
DR GeneID; 5772750; -.
DR KEGG; lhe:lhv_0048; -.
DR PATRIC; 22232068; VBILacHel91643_0051.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
DR BioCyc; LHEL405566:GJEN-42-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; 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; FALSE_NEG.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Cytoplasm; Pyridoxal phosphate; Serine biosynthesis; Transferase.
FT CHAIN 1 373 Phosphoserine aminotransferase.
FT /FTId=PRO_1000071543.
FT REGION 75 76 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 236 237 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 373 AA; 41162 MW; 9090F84548F80786 CRC64;
MTVYNFAAGP ATLPDPVIKQ IQEELPSLQG SGMSILEISH RSQMFDKIID TAKQDIKDLM
HVPDNYHILF FQGGGTGQFA AVPMNLATKH KRIALLDSGH WATRAGDEAA NLGVTVDVLD
STKDKHYQEL PHMPHAISAS DYDYLHITTN NTIEGTAYHT LPEHGDVTLV GDLSSNFMAE
EYQVSDFGLI FGGVQKNLGP AGVTVVIVRD DLVNHVDHIP SILNYELFVK KNSMFNTPPV
FAIYATGLVL KWLKQQGGIA GIEALNKKKS ALLYDFLDQS TLFHNDIKKT DRSLTNIPFK
TTDPVLDKQV IAEADQAGLK NLKGHRSVGG LRASLYNAMP LAGVQALVDF LYNFEKQHKN
NTMGKRYVSS KNI
//
