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SERC_SHEPC
ID   SERC_SHEPC              Reviewed;         363 AA.
AC   A4Y757;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE            EC=2.6.1.52 {ECO:0000255|HAMAP-Rule:MF_00160};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000255|HAMAP-Rule:MF_00160};
DE            Short=PSAT {ECO:0000255|HAMAP-Rule:MF_00160};
GN   Name=serC {ECO:0000255|HAMAP-Rule:MF_00160};
GN   OrderedLocusNames=Sputcn32_2069;
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) 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. {ECO:0000255|HAMAP-
CC       Rule:MF_00160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC         L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC         oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC         ChEBI:CHEBI:58538; EC=2.6.1.52; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00160};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00160};
CC       Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00160};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC       pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC       {ECO:0000255|HAMAP-Rule:MF_00160}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00160}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00160}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00160}.
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DR   EMBL; CP000681; ABP75790.1; -; Genomic_DNA.
DR   RefSeq; WP_011919355.1; NC_009438.1.
DR   AlphaFoldDB; A4Y757; -.
DR   SMR; A4Y757; -.
DR   STRING; 319224.Sputcn32_2069; -.
DR   GeneID; 45042529; -.
DR   KEGG; spc:Sputcn32_2069; -.
DR   eggNOG; COG1932; Bacteria.
DR   HOGENOM; CLU_034866_0_2_6; -.
DR   OMA; GYRASMY; -.
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-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR022278; Pser_aminoTfrase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43247; PTHR43247; 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; Cytoplasm; Pyridoxal phosphate;
KW   Pyridoxine biosynthesis; Serine biosynthesis; Transferase.
FT   CHAIN           1..363
FT                   /note="Phosphoserine aminotransferase"
FT                   /id="PRO_1000203570"
FT   BINDING         42
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         76..77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         102
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         156
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         175
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         198
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   BINDING         240..241
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00160"
SQ   SEQUENCE   363 AA;  40064 MW;  F48FB4378D2810C1 CRC64;
     MSAIYNFCAG PAMLPTAVMK KAQQELLDWN GQGVSVMEIS HRSKEFIALT KQAEADLREL
     MHIPANYHVL FMHGGGRGQF SAVVNNFLGN NGRALYLVSG QWSSSALAEA QKLAGDAQID
     SLNIVEKHNG LNAVVLPDLH KIDADYRYVH YCPNETVDGI EIFDELDSPW PIVADLSSTI
     MSREIDVSRY GLIYAGAQKN IGPSGLSIVI VRDDMLKLPS LVQSSIMDYR LAVEHDSMFN
     TPPTFAWYLA AEVFAWLKSI GGIASIAKIN QQKAQMLYQC IDCNTFYRNG VVASNRSQMN
     VTFQLADETL DGEFLKQAQV AGLVALKGHR IVGGMRASLY NAMPLEGVIA LVKFMNEFAA
     KYR
 
 
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