ID   IOLD_BACAC              Reviewed;         644 AA.
AC   C3LHY1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=BAMEG_2087;
OS   Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=568206;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 684 / NRRL 3495;
RA   Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA   Sutton G., Sims D.;
RT   "Genome sequence of Bacillus anthracis str. CDC 684.";
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; CP001215; ACP13968.1; -; Genomic_DNA.
DR   RefSeq; WP_001195355.1; NC_012581.1.
DR   AlphaFoldDB; C3LHY1; -.
DR   SMR; C3LHY1; -.
DR   GeneID; 45022377; -.
DR   KEGG; bah:BAMEG_2087; -.
DR   HOGENOM; CLU_013748_6_0_9; -.
DR   OMA; PNTYHLE; -.
DR   UniPathway; UPA00076; UER00145.
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_1000187308"
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;  71013 MW;  94239E0062C6B52B 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 HFNENLNEYV DALGTQLTQT
     AVIGQINTLL DKDAIIVGAA GSLPGDLQRM WASRKPNTYH MEYGYSCMGY EVAGALGAKL
     AEPSKEVYAM VGDGSYQMLH SELVTSLQEN KKINVLLFDN SGFGCINNLQ MGNGMGSFGT
     EFRYRNQETR KLDGAIMKID FAASAAGYGV KTYHVTSLEQ LQEALIDAKK QTVSTLIDIK
     VLPKTMTNGY ESWWHVGVAE VSKNQSVQAA YESKVSNLQQ ARSY