ID   IOLD_BACC0              Reviewed;         644 AA.
AC   B7JPM3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=BCAH820_2530;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK90007.1; -; Genomic_DNA.
DR   RefSeq; WP_001195353.1; NC_011773.1.
DR   AlphaFoldDB; B7JPM3; -.
DR   SMR; B7JPM3; -.
DR   EnsemblBacteria; ACK90007; ACK90007; BCAH820_2530.
DR   KEGG; bcu:BCAH820_2530; -.
DR   HOGENOM; CLU_013748_6_0_9; -.
DR   OMA; PNTYHLE; -.
DR   UniPathway; UPA00076; UER00145.
DR   Proteomes; UP000001363; 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; Thiamine pyrophosphate.
FT   CHAIN           1..644
FT                   /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT                   hydrolase"
FT                   /id="PRO_1000187309"
FT   REGION          442..522
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         65
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         520
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ   SEQUENCE   644 AA;  71015 MW;  D4C66C1BEB7392D3 CRC64;
     MQTVRMTTAQ ALVKFLNQQY VEFDGKQQKF VKGIFTIFGH GNVVGLGQAL EEDAGELEVY
     QGRNEQGMAN AAMAFAKQKH RKQIMACTSS VGPGSANMIT SAATASANNI PVLLLPGDVF
     ATRQPDPVLQ QIEQTHDLSI STNDAFRAVS KYWDRINRPE QLMTAMIQAM RVLTNPADTG
     AVTICLPQDV QGEAWDFPSY FFQKRVHRIE RRLPTKASLA DAVEMIKRKK KPVMICGGGV
     RYAEAAEELK QFAETFHIPF GETQAGKSAI ESSHPYNLGG IGVTGNVAAN TIAKEADLVI
     GIGTRFTDFT TASKQLFQNE EVEFLNINIS EFHANKLDAL KVIADAKEAL LALIDELQEI
     DYQSSYTVEI ADAKDAWETE LSRLHNIRFT CQDFTPEVEG HFDENLNEYV DALGTQLTQT
     AVIGQINTLL DEDAIIVGAA GSLPGDLQRM WASRKPNTYH MEYGYSCMGY EVAGALGAKL
     AEPSKEVYAM VGDGSYQMLH SELVTSLQEN KKINVLLFDN SGFGCINNLQ MGNGMGSFGT
     EFRYRNQETR KLDGAIMKID FAASAAGYGV KTYHVTSLEQ LQEALIDAKK QTVSTLIDIK
     VLPKTMTNGY ESWWHVGVAE VSKNQSVQAA YESKVSNLQQ ARSY