PDXA2_CLOB1
ID PDXA2_CLOB1 Reviewed; 334 AA.
AC A7FVM3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=CLB_2147;
OS Clostridium botulinum (strain ATCC 19397 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441770;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19397 / Type A;
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(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}.
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DR EMBL; CP000726; ABS35267.1; -; Genomic_DNA.
DR RefSeq; WP_012047748.1; NC_009697.1.
DR AlphaFoldDB; A7FVM3; -.
DR SMR; A7FVM3; -.
DR GeneID; 5186463; -.
DR KEGG; cba:CLB_2147; -.
DR HOGENOM; CLU_040168_0_1_9; -.
DR OMA; TAQVVMM; -.
DR OrthoDB; 1414545at2; -.
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_1000051497"
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