ID A0A0G4IUM5_PLABS Unreviewed; 382 AA.
AC A0A0G4IUM5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
GN ORFNames=PBRA_006910 {ECO:0000313|EMBL:CEO98796.1}, PLBR_LOCUS7794
GN {ECO:0000313|EMBL:SPR00579.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPR00579.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO98796.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEO98796.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEO98796.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPR00579.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CDSF01000087; CEO98796.1; -; Genomic_DNA.
DR EMBL; OVEO01000014; SPR00579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IUM5; -.
DR STRING; 37360.A0A0G4IUM5; -.
DR EnsemblProtists; CEO98796; CEO98796; PBRA_006910.
DR OMA; AFVYFCD; -.
DR OrthoDB; 1404347at2759; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 HAMAP; MF_00160; SerC_aminotrans_5; 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 Mitochondrion {ECO:0000313|EMBL:SPR00579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 15..369
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 382 AA; 40821 MW; DF00B3CB6CC62A26 CRC64;
MGMGDAGAKA RRVANFQAGP AQLPVPVLGQ AARAMTDVTP DGAGVSIAEL GHRTEQFERI
MDQTCADIRR LLQLPDTHSI LFMPGGGSAQ FSAVPLNLLG ATGKDTADYI VTGSWSEKAA
TEAKKYCNVN VVYSGKAQGY TDCPQQGQAL SFSPDPAYVY YCANETVNGV EYPGVPDCPN
GVPLVGDFSS TFMSRPFAAD DYAKFAVVFA GAQKNVGPPG ITIVIVQNDM IGKALGITPL
MLDYRTFSAH KSLYNTPPTI SVYMVGLMMQ WIESMGGVDA LGKINDAKAS ALYDAIDGSR
LFKCSVSRNC RSRMNVVFTI NGDCSGELLR SFLSEAESNG MVGLAGHRSV GGVRASLYNA
VSKDNVDQLI QFMKDFESRH LP
//