ID E1VIG6_9GAMM Unreviewed; 360 AA.
AC E1VIG6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 03-APR-2013, entry version 16.
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-1026-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: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: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; Cytoplasm;
KW Pyridoxal phosphate; Pyridoxine biosynthesis; Serine biosynthesis;
KW Transferase.
FT REGION 237 238 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 42 42 L-glutamate (By similarity).
FT BINDING 102 102 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; 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
//
