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 27-MAR-2024, entry version 112.
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; 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;
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 KEGG; cpe:CPE0089; -.
DR HOGENOM; CLU_013748_6_0_9; -.
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 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; 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
//
