ID   PDXA2_CLOBL             Reviewed;         334 AA.
AC   A7GFE5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=CLI_2255;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) 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}.
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DR   EMBL; CP000728; ABS39431.1; -; Genomic_DNA.
DR   RefSeq; WP_004451569.1; NC_009699.1.
DR   AlphaFoldDB; A7GFE5; -.
DR   SMR; A7GFE5; -.
DR   EnsemblBacteria; ABS39431; ABS39431; CLI_2255.
DR   KEGG; cbf:CLI_2255; -.
DR   HOGENOM; CLU_040168_0_1_9; -.
DR   OMA; TAQVVMM; -.
DR   Proteomes; UP000002410; 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_1000051499"
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;  36259 MW;  D48D3A43F3A457F6 CRC64;
     MINNKPIIGI PIGDPAGVGP EIVVKSLTEA EVYEKCNPIL IGDAKVIKQA MGFCNVNLNI
     NSIKKADEGK 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 AIVLAAKYSP KFKK