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Database: UniProt/TrEMBL
Entry: E0RNC6_SPITD
LinkDB: E0RNC6_SPITD
Original site: E0RNC6_SPITD 
ID   E0RNC6_SPITD            Unreviewed;       393 AA.
AC   E0RNC6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   19-FEB-2014, entry version 26.
DE   RecName: Full=Phosphoserine aminotransferase;
DE            EC=2.6.1.52;
DE   AltName: Full=Phosphohydroxythreonine aminotransferase;
GN   Name=serC; OrderedLocusNames=STHERM_c01500;
OS   Spirochaeta thermophila (strain ATCC 49972 / DSM 6192 / RI 19.B1).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Spirochaeta.
OX   NCBI_TaxID=665571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 6192;
RA   Angelov A., Mientus M., Wittenberg S., Lehmann R., Liesegang H.,
RA   Daniel R., Liebl W.;
RT   "The genome sequence of Spirochaeta thermophila DSM6192.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49972 / DSM 6192 / RI 19.B1;
RX   PubMed=20935097; DOI=10.1128/JB.01023-10;
RA   Angelov A., Liebl S., Ballschmiter M., Bomeke M., Lehmann R.,
RA   Liesegang H., Daniel R., Liebl W.;
RT   "Genome sequence of the polysaccharide-degrading, thermophilic
RT   anaerobe Spirochaeta thermophila DSM 6192.";
RL   J. Bacteriol. 192:6492-6493(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; CP001698; ADN01126.1; -; Genomic_DNA.
DR   RefSeq; YP_003873399.1; NC_014484.1.
DR   EnsemblBacteria; ADN01126; ADN01126; STHERM_c01500.
DR   GeneID; 9755404; -.
DR   KEGG; sta:STHERM_c01500; -.
DR   PATRIC; 42519497; VBISpiThe146732_0152.
DR   HOGENOM; HOG000088965; -.
DR   KO; K00831; -.
DR   OMA; NNTIFGT; -.
DR   BioCyc; STHE665571:GI3Y-150-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   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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW   Serine biosynthesis; Transferase.
FT   REGION      108    109       Pyridoxal phosphate binding (By
FT                                similarity).
FT   REGION      267    268       Pyridoxal phosphate binding (By
FT                                similarity).
FT   BINDING      74     74       L-glutamate (By similarity).
FT   BINDING     134    134       Pyridoxal phosphate (By similarity).
FT   BINDING     182    182       Pyridoxal phosphate (By similarity).
FT   BINDING     202    202       Pyridoxal phosphate (By similarity).
FT   BINDING     225    225       Pyridoxal phosphate (By similarity).
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   393 AA;  43827 MW;  ED5C1B99E2C7A310 CRC64;
     MGACHIAARR DARALRPPYG GRPSHERSTP MRLERVYNFS AGPSVLPEEV LKKAADEMLV
     YRDAGMSVME MSHRSKAFER IIGGTEERLR RLLDIPDDYA VLFLQGGASL QFAMVPMNLM
     GRTGKGGYVD TGHWSSRAIK EAGLFGEVEV VASSADRGYT TIPEIPPLPE GLSYLHITTN
     NTIYGTRYTS LPATGDAPLV ADASSHILSE PVDIRSFGIY YAGAQKNLGP AGVTVVIIRK
     DLVGGHLPHT PTMLRYDIHV EKRSLYNTPP CYAIYMVGLV LEWVERQGGV QAMYERNLEK
     AELLYRFLDE SDLFTTKVEP AYRSLMNVPF FLPTEELTAT FLEEAEERGL VNLKGHRSVG
     GLRASIYNAM PKEGVEALVA FMKDFERRYG RRR
//
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