ID A4SM12_AERS4 Unreviewed; 362 AA.
AC A4SM12;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=Phosphoserine aminotransferase;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=serC; OrderedLocusNames=ASA_1858;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA Nash J.H., Johnson S.C., Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT into the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO89934.1; -; Genomic_DNA.
DR RefSeq; YP_001141682.1; NC_009348.1.
DR ProteinModelPortal; A4SM12; -.
DR SMR; A4SM12; 4-362.
DR STRING; 382245.ASA_1858; -.
DR EnsemblBacteria; ABO89934; ABO89934; ASA_1858.
DR GeneID; 4997368; -.
DR KEGG; asa:ASA_1858; -.
DR PATRIC; 20790090; VBIAerSal2987_1841.
DR eggNOG; COG1932; -.
DR HOGENOM; HOG000088965; -.
DR KO; K00831; -.
DR OMA; MSIMEMS; -.
DR ProtClustDB; PRK05355; -.
DR BioCyc; ASAL382245:GJJN-1849-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; Complete proteome;
KW Cytoplasm; Pyridoxal phosphate; Pyridoxine biosynthesis;
KW Serine biosynthesis; Transferase.
FT REGION 77 78 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 239 240 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 43 43 L-glutamate (By similarity).
FT BINDING 104 104 Pyridoxal phosphate (By similarity).
FT BINDING 154 154 Pyridoxal phosphate (By similarity).
FT BINDING 174 174 Pyridoxal phosphate (By similarity).
FT BINDING 197 197 Pyridoxal phosphate (By similarity).
FT MOD_RES 198 198 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 362 AA; 39535 MW; 63022D0EEC26ED5D CRC64;
MSKQIYNFCA GPAMLPVEVM ERAQREFCNF QGLGASVMEL SHRGKPYMAV AEKAEADLRD
LLAVPDNYKV LFMHGGGRGQ FSAVPMNLLG GANKKADFLL TGVWSQSAVD EARKYGDIQT
VQGVAKNEQG ISHLLQSPAF RADAAYVHYC PNETIDGIEM FDIPATGDVP LVADLSSTIL
SRPMDVSRFG VIYAGAQKNI GPSGLAIAIV RDDLLNQARA DVPSIFDYQL TAKNDSMFNT
PPTYAWYLAG LVFEWLKEQG GLEAMAARNK AKADFLYGYL DDSSFYGNKV DVSCRSRMNI
PFQLKNDALD KQFLAESEAA GLLALKGHRI VGGMRASLYN AMPLEGVKAL VSFMDGFAKR
HG
//
