ID   PDXA2_CLOBH             Reviewed;         334 AA.
AC   A5I3X9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Putative D-threonate 4-phosphate dehydrogenase {ECO:0000250|UniProtKB:P58718};
DE            EC=1.1.1.408 {ECO:0000250|UniProtKB:P58718};
GN   OrderedLocusNames=CBO2208;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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; AM412317; CAL83749.1; -; Genomic_DNA.
DR   RefSeq; YP_001254702.1; NC_009495.1.
DR   AlphaFoldDB; A5I3X9; -.
DR   SMR; A5I3X9; -.
DR   KEGG; cbo:CBO2208; -.
DR   PATRIC; fig|413999.7.peg.2176; -.
DR   HOGENOM; CLU_040168_0_1_9; -.
DR   OMA; TAQVVMM; -.
DR   Proteomes; UP000001986; 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;
KW   Reference proteome.
FT   CHAIN           1..334
FT                   /note="Putative D-threonate 4-phosphate dehydrogenase"
FT                   /id="PRO_1000051498"
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;  36273 MW;  D48D3A5B50A457F6 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 AIILAAKYSP KFKK