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Database: UniProt/TrEMBL
Entry: E1VIG6_9GAMM
LinkDB: E1VIG6_9GAMM
Original site: E1VIG6_9GAMM 
ID   E1VIG6_9GAMM            Unreviewed;       360 AA.
AC   E1VIG6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   09-JUL-2014, entry version 23.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
GN   Name=serC; ORFNames=HDN1F_10250;
OS   gamma proteobacterium HdN1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria.
OX   NCBI_TaxID=83406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F.,
RA   Ehrenreich P., Behrends A., Wilkes H., Kube M., Reinhardt R.,
RA   Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with
RT   possible involvement of the electron acceptor in substrate
RT   activation.";
RL   Environ. Microbiol. 0:0-0(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   -!- 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; FP929140; CBL44608.1; -; Genomic_DNA.
DR   RefSeq; YP_003810265.1; NC_014366.1.
DR   EnsemblBacteria; CBL44608; CBL44608; HDN1F_10250.
DR   GeneID; 9702867; -.
DR   KEGG; gpb:HDN1F_10250; -.
DR   PATRIC; 42344907; VBIGamPro61291_1115.
DR   HOGENOM; HOG000088965; -.
DR   KO; K00831; -.
DR   BioCyc; GPRO83406:GIWA-1051-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: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   GO; GO:0008615; P:pyridoxine 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; 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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01364; serC_1; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW   Serine biosynthesis; Transferase.
FT   REGION      237    238       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      42     42       L-glutamate (By similarity){EA3}.
FT   BINDING     102    102       Pyridoxal phosphate (By similarity){EA3}.
FT   BINDING     152    152       Pyridoxal phosphate (By similarity){EA3}.
FT   BINDING     172    172       Pyridoxal phosphate (By similarity){EA3}.
FT   BINDING     195    195       Pyridoxal phosphate (By similarity){EA3}.
FT   MOD_RES     196    196       N6-(pyridoxal phosphate)lysine (By
FT                                similarity){EA3}.
SQ   SEQUENCE   360 AA;  39576 MW;  DC9F41AF83DBAA5F CRC64;
     MARAFNFCAG PAALPEEVLT QASAEMLDYQ GRGLSVMEMS HRSAEFVAIA EQAEKDLREL
     LQIPANYKVL FLSGGAHLQF AMVPLNLLAG KTDADYVNTG QWSKRAISEA QRYCAVNVVA
     SDEVNRFTGV PDVSSWRRNP DAAYLHYVAN ETIGGVEFDF VPDAEGVPLV VDMSSNILSR
     PIDVNQYGLI YAGAQKNIGP AGLTVAIVRE DLLGNAHPST PTMLDYKTHA DNGSMYNTPP
     TYAWYLAGLV FQWIQRQGGL GAIEKLNRAK AEKLYRFIDN SGFYKNPVAV ANRSLMNVPF
     TLADASLDKS FLQEAEQRHL LNLKGHRSVG GMRASIYNAV PMAAVDALID FMTDFQKRRG
//
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