ID G0EY81_CUPNN Unreviewed; 385 AA.
AC G0EY81;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE EC=2.6.1.52 {ECO:0000256|HAMAP-Rule:MF_00160};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000256|HAMAP-Rule:MF_00160};
DE Short=PSAT {ECO:0000256|HAMAP-Rule:MF_00160};
GN Name=serC {ECO:0000256|HAMAP-Rule:MF_00160,
GN ECO:0000313|EMBL:AEI76165.1};
GN OrderedLocusNames=CNE_1c08030 {ECO:0000313|EMBL:AEI76165.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI76165.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI76165.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine. {ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001607, ECO:0000256|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:0000256|ARBA:ARBA00001871, ECO:0000256|HAMAP-
CC Rule:MF_00160};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00160};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00005099,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00160}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily.
CC {ECO:0000256|ARBA:ARBA00006904, ECO:0000256|HAMAP-Rule:MF_00160}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00160}.
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DR EMBL; CP002877; AEI76165.1; -; Genomic_DNA.
DR RefSeq; WP_013955843.1; NC_015726.1.
DR AlphaFoldDB; G0EY81; -.
DR KEGG; cnc:CNE_1c08030; -.
DR HOGENOM; CLU_034866_0_2_4; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000006798; Chromosome 1.
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; 3.90.1150.10; 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 NCBIfam; TIGR01364; serC_1; 1.
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, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00160}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00160};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299, ECO:0000256|HAMAP-
KW Rule:MF_00160};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00160, ECO:0000313|EMBL:AEI76165.1}.
FT DOMAIN 21..373
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 59
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 123
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 173
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 220
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT BINDING 262..263
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00160"
SQ SEQUENCE 385 AA; 42607 MW; 59F9F11622880F2D CRC64;
MNDPQNPALA GMMQRALAER VYNFSPGPAV LPAEVLQQAA EEMLSWRGTG VSVMEMSHRS
REFEGIQAEA IADLRELLHI PSNFHVLFLQ GGAIGENGIV PLNLMRLRSA DAPKADFVVT
GTWSVKTEQE ARRYGAVNIA ATSEAQKFHR IPDVADWKLS DDAGYVHLCT NETIVGVEFQ
NIPDIGQVKG DRIVVADASS HILSRPIDWS RVQVVYGGAQ KNIGPAGVTI VIVRDDLIGH
AHPLCPSAFN WRLVAEHNSM YNTPPTYAIY IAGLVFKWLK RQGGVPAIEQ RNIAKASALY
NYLDQSDFYR NEIHPSCRSR MNVPFFLGDE SRNEAFLQQA RANGLVQLKG HKTVGGMRAS
IYNAMSLEGV MALVDFMREF ERTSA
//
