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Database: UniProt
Entry: A0A1F7IFE8_9BACT
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ID   A0A1F7IFE8_9BACT        Unreviewed;       359 AA.
AC   A0A1F7IFE8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|ARBA:ARBA00021164};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
DE   AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
GN   ORFNames=A3A74_04990 {ECO:0000313|EMBL:OGK42096.1};
OS   Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_35_13.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802055 {ECO:0000313|EMBL:OGK42096.1, ECO:0000313|Proteomes:UP000179270};
RN   [1] {ECO:0000313|EMBL:OGK42096.1, ECO:0000313|Proteomes:UP000179270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001607};
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:0000256|ARBA:ARBA00001871};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGK42096.1}.
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DR   EMBL; MGAF01000011; OGK42096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7IFE8; -.
DR   STRING; 1802055.A3A74_04990; -.
DR   UniPathway; UPA00135; UER00197.
DR   Proteomes; UP000179270; Unassembled WGS sequence.
DR   GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
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; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          31..326
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   359 AA;  40827 MW;  7888D9DE4077B9AC CRC64;
     MKYTYFTCGP SQLYPGVFRH LQIAFDKDIP SLSHRSKIFQ QIYKSTQDNL RKLLSIPKSH
     KIFFVSSSLE SMEKIIQNCV EKNSFHFVNG AFSRKFYQFA EILKKQPIKY EVPEGEGYLP
     EKVMIPPDTE LICVMQNETS TGVAIPVQSI NRLYTQNPKS LIAVDIVSSA PYVELNFNKI
     DLTFFSVQKG FGLPAGMGVL IINEEALAKA QFLRKKGINV GSYHSFSSLL EKDQIFQTPE
     TPNVLLIYLL GQVCKDILKK GMNMIREETE AKAKLVYDFF DKHPRCKPFV KNSNYRSKTT
     IAIDVMGDTN KIVKKLKSKG IVVSSGYGKF KESHIRIANF PAHSAKDFTN LVRYLNIIS
//
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