ID   PDXA2_SYMTH             Reviewed;         335 AA.
AC   Q3V818;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=STH2300;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41285.1; -; Genomic_DNA.
DR   RefSeq; WP_011196423.1; NC_006177.1.
DR   AlphaFoldDB; Q3V818; -.
DR   SMR; Q3V818; -.
DR   STRING; 292459.STH2300; -.
DR   EnsemblBacteria; BAD41285; BAD41285; STH2300.
DR   KEGG; sth:STH2300; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_0_1_9; -.
DR   OMA; TAQVVMM; -.
DR   OrthoDB; 1414545at2; -.
DR   Proteomes; UP000000417; 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..335
FT                   /note="Putative D-threonate 4-phosphate dehydrogenase"
FT                   /id="PRO_1000211916"
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   335 AA;  36102 MW;  C6B4D45E97B0DEDE CRC64;
     MDTRPLIGIT MGDPASIGPE IAAKALANPE IYALCRPLLI GDSRVMARAF ETTGVKLNLN
     PVATPAEGKY AHGTVDLIDL PVVDMGTLQW GQVQAQAGAA AFAYIKRSIE LALEGAVDAV
     TTGPINKEAL KAARIDFIGH TEIFGELTGS HDPLTMFETK GLRIFFLTRH VSLAQACRMI
     TRDRVLDYIR RCTAALEQLG LVRPKLAVAG LNPHCGEHGL FGDEEVREIE PAVQQAQAEG
     YNVSGPHPAD SVFWHAAQGR FDAVLSLYHD QGHIAAKMYD FERTVSITAG LPFLRSSVDH
     GTAFDIAGTG RASAVSLEEA IRVGAKYAAA FRRTR