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IOLD_CLOPE
ID   IOLD_CLOPE              Reviewed;         639 AA.
AC   Q8XP76;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000255|HAMAP-Rule:MF_01669};
DE            Short=THcHDO hydrolase {ECO:0000255|HAMAP-Rule:MF_01669};
DE            EC=3.7.1.22 {ECO:0000255|HAMAP-Rule:MF_01669};
GN   Name=iolD {ECO:0000255|HAMAP-Rule:MF_01669}; OrderedLocusNames=CPE0089;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-
CC       trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate
CC       (5DG). {ECO:0000255|HAMAP-Rule:MF_01669}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-
CC         glucuronate + H(+); Xref=Rhea:RHEA:25836, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28446, ChEBI:CHEBI:58852; EC=3.7.1.22;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01669};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01669};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 3/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01669}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000255|HAMAP-
CC       Rule:MF_01669}.
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DR   EMBL; BA000016; BAB79795.1; -; Genomic_DNA.
DR   RefSeq; WP_003470047.1; NC_003366.1.
DR   AlphaFoldDB; Q8XP76; -.
DR   SMR; Q8XP76; -.
DR   STRING; 195102.gene:10489333; -.
DR   EnsemblBacteria; BAB79795; BAB79795; BAB79795.
DR   KEGG; cpe:CPE0089; -.
DR   HOGENOM; CLU_013748_6_0_9; -.
DR   OMA; PNTYHLE; -.
DR   UniPathway; UPA00076; UER00145.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01669; IolD; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
DR   InterPro; IPR023757; THcHDO_hydrolase_firmi.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 1.
DR   PANTHER; PTHR18968:SF9; PTHR18968:SF9; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; NAD; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..639
FT                   /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT                   hydrolase"
FT                   /id="PRO_0000352539"
FT   REGION          438..518
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         62
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         516
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ   SEQUENCE   639 AA;  70398 MW;  8455C9A40CE0AD7A CRC64;
     MRMTTGQALV KFLDNQYVSF DGKEEKFVDG IFTIFGHGIV VGLGEALYEN PGELKVYQGR
     NEQGMAHVST AFAKQNNRRK IIACSSSVGP GAANMVTAAA TATVNNIPLL LLPGDSFATR
     QPDPVLQQIE QSYNLGITTN DAFKPVCKYW DRINRPEQLM SAMINAMRVL TDPAETGAVC
     IALPQDVQGE AYDFPEYFFK KRVHRITRPL AVQEEFEEAL DIIMNKKKPI IICGGGVRYS
     EAGEALVDFA EEFNIPICET QAGKSAIKSS HPLNLGGIGV TGNLAANMIA KDTDLVIGVG
     TRFSDFTTSS KSLFKNPEVD FITVNVSKFH GGKMDAHKII GDAKVCIEEL QAMLEANNYE
     SSYEDEIVNA KKAWKEEMKR LTNIKYDENF EALIKPKREG CIEEFSVLTG GLITQTAALG
     VIRETIDDDA IVVGAAGSLP GDLQRMWETD ARDSYHMEYG YSCMGYEIAA TLGAKLAEPE
     REVYSMVGDG SYLMLHSEMV TAMQEQKKIN ILLFDNCGFG CINNLQMSNG IGSLATEFRY
     RDENGKLEGG LIPIDFAKVA SGYGLKTYSV KTLAQLKEAL EDAKKQKVST LIDIKVLPKT
     MTDGYDAWWH VGIAGESEID GVNKAFENKE KNLKAARRY
 
 
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