ID E0RNC6_SPITD Unreviewed; 393 AA.
AC E0RNC6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 23.
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; MSIMEMS; -.
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; 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
//
