ID Q2YQI1_BRUA2 Unreviewed; 391 AA.
AC Q2YQI1;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|ARBA:ARBA00031421};
GN Name=serC {ECO:0000313|EMBL:CAJ11655.1};
GN OrderedLocusNames=BAB1_1699 {ECO:0000313|EMBL:CAJ11655.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11655.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ11655.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ11655.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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}.
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DR EMBL; AM040264; CAJ11655.1; -; Genomic_DNA.
DR RefSeq; WP_002964776.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YQI1; -.
DR STRING; 359391.BAB1_1699; -.
DR GeneID; 58775301; -.
DR KEGG; bmf:BAB1_1699; -.
DR PATRIC; fig|359391.11.peg.214; -.
DR HOGENOM; CLU_040283_0_0_5; -.
DR PhylomeDB; Q2YQI1; -.
DR UniPathway; UPA00135; UER00197.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01494; AAT_I; 1.
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; IPR006271; Pser_aminoTfrase_methanosarc.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01365; serC_2; 1.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 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 ECO:0000313|EMBL:CAJ11655.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW Sugar transport {ECO:0000313|EMBL:CAJ11655.1};
KW Transferase {ECO:0000313|EMBL:CAJ11655.1};
KW Transport {ECO:0000313|EMBL:CAJ11655.1}.
FT DOMAIN 140..325
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42381 MW; E8C23EC777CBE6C7 CRC64;
MTTIAKPAVR PANPNFSSGP CAKRPGWSLD ALADAPLGRS HRAKIGKNKL KEAIDLTREV
LQVPADYRIG IVPASDTGAV EMALWSMLGA RGVDMVAWES FGSGWVTDVV KQLKLEDVRT
FEAPYGEIVD FSKVDFDRDV VFTWNGTTSG VRVPNAGFIP ADRKGLTFCD ATSAAFAQRL
DFAKLDVVTF SWQKVLGGEG AHGILILSPR AVERLESYKP AWPLPKIFRM TKGGKLIEGI
FVGETINTPS MLCVEDYLDA LKWAKSLGGL DALIARADRN FSVLNDFVEK TPWIANLAMK
PETRSNTSVC LTIVDPEITA LSADEQAAFA KGIVTTLDKE GVAYDIGAYR DAPSGLRIWA
GATVEASDLE ALTHWLNWAF ATQKAALKAA A
//
