PDXA2_CLOB6
ID PDXA2_CLOB6 Reviewed; 334 AA.
AC C3KYY3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Putative D-threonate 4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P58718};
DE EC=1.1.1.408 {ECO:0000250|UniProtKB:P58718};
GN Name=pdxA; OrderedLocusNames=CLJ_B2416;
OS Clostridium botulinum (strain 657 / Type Ba4).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=515621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=657 / Type Ba4;
RA Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent
CC decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone
CC phosphate (DHAP). {ECO:0000250|UniProtKB:P58718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-phospho-D-threonate + NAD(+) = CO2 + dihydroxyacetone
CC phosphate + NADH; Xref=Rhea:RHEA:52396, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:136590; EC=1.1.1.408;
CC Evidence={ECO:0000250|UniProtKB:P58718};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P19624};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P19624};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P58718}.
CC -!- SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001083; ACQ54394.1; -; Genomic_DNA.
DR RefSeq; WP_012721219.1; NC_012658.1.
DR AlphaFoldDB; C3KYY3; -.
DR SMR; C3KYY3; -.
DR EnsemblBacteria; ACQ54394; ACQ54394; CLJ_B2416.
DR KEGG; cbi:CLJ_B2416; -.
DR HOGENOM; CLU_040168_0_1_9; -.
DR OMA; TAQVVMM; -.
DR Proteomes; UP000002333; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..334
FT /note="Putative D-threonate 4-phosphate dehydrogenase"
FT /id="PRO_1000211910"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 215
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 270
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19624"
SQ SEQUENCE 334 AA; 36314 MW; 6E373CC452F25B1A CRC64;
MINNKPIIGI PIGDPAGVGP EIVVKSLTQA EIYEKCNPIL IGDAKVIKQA MGFCNVNLNI
NSIKKVDEGK FTLGTIDLID LNNIDIDELK IGKVQGIAGK AAFEYIKKSV EMAKEGELDA
IATTPINKES LREGNVNYIG HTEILADLTD TEDPLTMFEV RGMRVFFLTR HVSLRKACDL
VTKERVLDYI IRCSEALEKL GVKDGKMAVA GLNPHSGEHG LFGDEEMKAV VPAIEEAQKM
GYKVEGPIGA DSVFHLALKG RYNSVLSLYH DQGHIATKTL DFERTIAVTN GMPILRTSVD
HGTAFDIAGT GQASSVSMVE AIILAAKYSP KFKK