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 02-SEP-2026, entry version 117. 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}; GN OrderedLocusNames=CPE0089; OS Clostridium perfringens (strain 13 / Type A). OC Bacteria; Bacillati; Bacillota; 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; cpe:CPE0089; -. DR HOGENOM; CLU_013748_6_0_9; -. DR UniPathway; UPA00076; UER00145. DR GO; GO:0005948; C:acetolactate synthase complex; IEA:TreeGrafter. DR GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:TreeGrafter. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter. 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 GO; GO:0009099; P:L-valine biosynthetic process; IEA:TreeGrafter. DR CDD; cd02003; TPP_IolD; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. 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_TPP-bd. DR NCBIfam; TIGR04377; myo_inos_iolD; 1. DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1. DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Hydrolase; Magnesium; Metal-binding; NAD; 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 //