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Database: UniProt/SWISS-PROT
Entry: SERC_LACH4
LinkDB: SERC_LACH4
Original site: SERC_LACH4 
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   19-FEB-2014, entry version 42.
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; NNTIFGT; -.
DR   OrthoDB; EOG60CWP3; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-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; SSF53383; 1.
DR   TIGRFAMs; TIGR01364; serC_1; 1.
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
//
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