ID   PDXA2_ALKHC             Reviewed;         334 AA.
AC   Q9RC88;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=BH0804;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10484179; DOI=10.1007/s007920050120;
RA   Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R.,
RA   Hirama C., Fuji F., Masui N.;
RT   "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-
RT   125.";
RL   Extremophiles 3:227-233(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; AB024550; BAA83911.1; -; Genomic_DNA.
DR   EMBL; BA000004; BAB04523.1; -; Genomic_DNA.
DR   PIR; D83750; D83750.
DR   RefSeq; WP_010896977.1; NC_002570.2.
DR   AlphaFoldDB; Q9RC88; -.
DR   SMR; Q9RC88; -.
DR   STRING; 272558.10173418; -.
DR   EnsemblBacteria; BAB04523; BAB04523; BAB04523.
DR   KEGG; bha:BH0804; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_0_1_9; -.
DR   OMA; TAQVVMM; -.
DR   OrthoDB; 1414545at2; -.
DR   Proteomes; UP000001258; 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_0000188797"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         170
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         214
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         269
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         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   334 AA;  36632 MW;  24436A1866079820 CRC64;
     MNKKPIIAIP MGDPAGIGPE ITVGALNKKE LYDVANPVVI GHGDMLEKML PVMKADLTIN
     RITTVDEAMF EYGTIDVIHL DNLNVAEVKM GTVQAQCGKA AFEYIRHAVQ LANDKKVDAL
     ATTPINKESL KAAEVPYIGH TEMLADLTKT EDPLTMFEVH SMRIFFLTRH LSLKDAIDQM
     TKERVHDYLL RCDKALEKLG VKERRFAVAG LNPHSGENGL FGREEMDEIT PGIELAKKDG
     INAVGPVPAD SVFHHALNGR YDAVLSLYHD QGHIAAKMTD FERTISITNG LPFLRTSVDH
     GTAFDIAGKG IASTVSMEEC IKLAAKYAPH FVTA