PDXA_SYNR3
ID PDXA_SYNR3 Reviewed; 328 AA.
AC A5GPX7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
DE EC=1.1.1.262 {ECO:0000255|HAMAP-Rule:MF_00536};
DE AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00536};
GN Name=pdxA {ECO:0000255|HAMAP-Rule:MF_00536};
GN OrderedLocusNames=SynRCC307_0033;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-
CC threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which
CC spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate
CC (AHAP). {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(phosphooxy)-L-threonine + NAD(+) = 3-amino-2-oxopropyl
CC phosphate + CO2 + NADH; Xref=Rhea:RHEA:32275, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57279, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58452; EC=1.1.1.262; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00536};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00536};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00536};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5.
CC {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- MISCELLANEOUS: The active site is located at the dimer interface.
CC {ECO:0000255|HAMAP-Rule:MF_00536}.
CC -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000255|HAMAP-
CC Rule:MF_00536}.
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DR EMBL; CT978603; CAK26936.1; -; Genomic_DNA.
DR RefSeq; WP_011934451.1; NC_009482.1.
DR AlphaFoldDB; A5GPX7; -.
DR SMR; A5GPX7; -.
DR STRING; 316278.SynRCC307_0033; -.
DR EnsemblBacteria; CAK26936; CAK26936; SynRCC307_0033.
DR KEGG; syr:SynRCC307_0033; -.
DR eggNOG; COG1995; Bacteria.
DR HOGENOM; CLU_040168_0_0_3; -.
DR OMA; TAQVVMM; -.
DR OrthoDB; 1414545at2; -.
DR UniPathway; UPA00244; UER00312.
DR Proteomes; UP000001115; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00536; PdxA; 1.
DR InterPro; IPR037510; PdxA.
DR InterPro; IPR005255; PdxA_fam.
DR PANTHER; PTHR30004; PTHR30004; 1.
DR Pfam; PF04166; PdxA; 1.
DR TIGRFAMs; TIGR00557; pdxA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase;
KW Pyridoxine biosynthesis; Reference proteome.
FT CHAIN 1..328
FT /note="4-hydroxythreonine-4-phosphate dehydrogenase"
FT /id="PRO_1000051523"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 160
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 203
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00536"
SQ SEQUENCE 328 AA; 35324 MW; DB8197D66D80824B CRC64;
MTRLAIALGD PAGIGAEVVL KALAHRPSLN PLLVGCRQWL QASYEQLLPC CHEPLADPSQ
LEILDEPLTE AITPGSISAA AGAASFGWLT RATEAVLDGR AQALVTAPIA KTAWHQAGHH
YPGQTERLAE LCGCDDAAML FTARSPQSGW RFNTLLATTH IPLSSVPAAL TPERLERRLG
QLEDFCRRFR QRPRLRVAGL NPHAGEAGQL GTEEQRWITA CLQAYQQRHN NLQLEGPVPP
DTCWLGAAQA WNDSQHVEEG CDGYLALYHD QGLIPVKVLA FDQAVNTTLG LPFLRTSPDH
GTGFDRAGQG SARGASMLAA IDTAVELG
