ID D3S9K9_THISK Unreviewed; 361 AA.
AC D3S9K9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 01-MAY-2013, entry version 27.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; OrderedLocusNames=TK90_1205;
OS Thioalkalivibrio sp. (strain K90mix).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K90mix;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001905; ADC71714.1; -; Genomic_DNA.
DR RefSeq; YP_003460450.1; NC_013889.1.
DR EnsemblBacteria; ADC71714; ADC71714; TK90_1205.
DR GeneID; 8806967; -.
DR KEGG; tkm:TK90_1205; -.
DR PATRIC; 32525978; VBIThiSp13812_1197.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
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 76 77 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 238 239 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 361 AA; 39335 MW; 9966D24DE4D97A89 CRC64;
MSRVHNFSAG PAALPQAVLE RAREELIDFH GAGMSVMEMS HRGKPFMQVA EKAEQDLRKL
MNIPDNYSVL FLQGGATGQF AAIPMNLHSG GKPMDYIDTG AWSGKAIKEA QKFGPVNIVA
SSQASGYASI PARDSWNLDP NAAYVHYTPN ETIGGVEFHE VPDVGGKPLV ADMSSTILSR
PIDVSKFGVI YAGAQKNIGP AGLTVVIVRN DLLDKESNPN LPAVVDWTLQ AKNDSMYNTP
PTFGWYLAGL VFEWLLEQGG LDKMAEINQR KAEKLYHFVD NSAFYRNPVE PDARSWMNVP
FILADDSLDG TFLNEADAAG LSSLKGHRSV GGMRASIYNA VPESAVDALI EFMADFENRH
A
//
