ID   GAD_THETE               Reviewed;         497 AA.
AC   Q704D2;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=D-gluconate dehydratase;
DE            EC=4.2.1.39;
GN   Name=gad;
OS   Thermoproteus tenax.
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=2271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA   Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA   Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT   "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT   tenax using genomic and biochemical data.";
RL   J. Bacteriol. 186:2179-2194(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=15869466; DOI=10.1042/bj20041711;
RA   Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J.,
RA   Siebers B.;
RT   "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic
RT   archaea: a re-evaluation.";
RL   Biochem. J. 390:529-540(2005).
CC   -!- FUNCTION: Involved in the degradation of glucose via the Entner-
CC       Doudoroff pathway. Catalyzes the dehydration of gluconate to produce 2-
CC       keto-3-deoxygluconate (KDG). It is not able to use D-galactonate as
CC       substrate. {ECO:0000269|PubMed:15028704, ECO:0000269|PubMed:15869466}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC         Xref=Rhea:RHEA:21612, ChEBI:CHEBI:15377, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:57990; EC=4.2.1.39;
CC         Evidence={ECO:0000269|PubMed:15869466};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GaD subfamily. {ECO:0000305}.
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DR   EMBL; AJ621281; CAF18462.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q704D2; -.
DR   SMR; Q704D2; -.
DR   UniPathway; UPA00792; -.
DR   GO; GO:0047929; F:gluconate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034599; Gluconate_dehydratase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; PTHR48080; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00008; gluconate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..497
FT                   /note="D-gluconate dehydratase"
FT                   /id="PRO_0000422652"
FT   ACT_SITE        305
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         355
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            378
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000250"
FT   SITE            430
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  55119 MW;  AF258660483589CE CRC64;
     MASAMASSAL REATCTMTRL AADVAASVSS IFSCKDSAGP RPVVPATKTT STPLDVMFFT
     WFAKSSGSSL PPLKVVMTGA TISIDSTRGA LKKLARKGIK GWLNQYMATI KEIEPIVLYE
     QETDARWASY SILVRVVTSD GRVSYGEAVP TLRILPVVSA VRQTARAFLG RDPHEISAAF
     YEWYRQDFFL SRSFESATAL SAIDMALWDL KARELGAPLY ELLGGKLRDR VKVYANGWYG
     GCRDPQCFAE KAKEVVARGY DALKFDPFGP SFNSITSEEL RRAEEAVAAV RDAVGDDVDI
     LIEHHGRFNA NAAVEIAKRF EPYRPYFMEE PLHHEDIEGY RKYRSLTSAR IAMGERLISA
     KEALQYLVEG LVDVIQPDAC NIGGVTGSMK VAALAEAFSV EVSYHNAYGP VQFALEVQLS
     AVTPTLYRLE SFYDYWPQWK RDLIGDPFRL SQSSVEVPRG PGIGVAVNER VLEKYRAEPS
     EIPVGEEPVW VVRGTWR