ID   PDXA2_FUSNN             Reviewed;         332 AA.
AC   Q8RGR0;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=FN0226;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94432.1; -; Genomic_DNA.
DR   RefSeq; NP_603133.1; NC_003454.1.
DR   AlphaFoldDB; Q8RGR0; -.
DR   SMR; Q8RGR0; -.
DR   STRING; 190304.FN0226; -.
DR   EnsemblBacteria; AAL94432; AAL94432; FN0226.
DR   KEGG; fnu:FN0226; -.
DR   PATRIC; fig|190304.8.peg.807; -.
DR   eggNOG; COG1995; Bacteria.
DR   HOGENOM; CLU_040168_0_1_0; -.
DR   InParanoid; Q8RGR0; -.
DR   OMA; TAQVVMM; -.
DR   BioCyc; FNUC190304:G1FZS-828-MON; -.
DR   Proteomes; UP000002521; 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..332
FT                   /note="Putative D-threonate 4-phosphate dehydrogenase"
FT                   /id="PRO_0000188808"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         168
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         211
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         266
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         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P19624"
SQ   SEQUENCE   332 AA;  36547 MW;  A9032E3F6E7081FC CRC64;
     MRTKIAIPMG DPAGVGPEIV VKTAVSKEIL DLCDLVVIGD KKVLEKATKI CQVDLKIHTI
     KNIEEGKYEK GILNVIDLEN VDMNTLEYGQ VQGMCGKAAF EYIKKCVELA MEYKVDAIAT
     TPINKESLRA GNVNYIGHTE ILGDLSNSRD PLTMFEVDNM RVFFLTRHMS LRKACDAITK
     ERVLEYIERC TKALKQLGVT GKMAVAGLNP HSGEHGLFGN EEVKEITPAI EEAQKLGYDV
     VGPIGADSVF HQALQGRYVA VLSLYHDQGH IATKTYDFER TIAITLDMPF LRTSVDHGTA
     FDIAGKGIVS AISMIEAVKL AAKYAPNFKN IK