ID   IOLD_LACCA              Reviewed;         642 AA.
AC   A5YBJ6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 58.
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};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BL23;
RX   PubMed=17449687; DOI=10.1128/aem.00243-07;
RA   Yebra M.J., Zuniga M., Beaufils S., Perez-Martinez G., Deutscher J.,
RA   Monedero V.;
RT   "Identification of a gene cluster allowing Lactobacillus casei BL23 the
RT   utilization of myo-inositol.";
RL   Appl. Environ. Microbiol. 73:3850-3858(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP57765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EF382358; ABP57765.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5YBJ6; -.
DR   SMR; A5YBJ6; -.
DR   STRING; 543734.LCABL_02200; -.
DR   eggNOG; COG3962; Bacteria.
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..642
FT                   /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT                   hydrolase"
FT                   /id="PRO_0000352544"
FT   REGION          446..526
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         71
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT   BINDING         524
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ   SEQUENCE   642 AA;  70086 MW;  520559671F0022C5 CRC64;
     MAADAKKETI RLTTAQALVR FLNQQYIDVD GQVTSFVEGL FAIFGHGNVL GLGEALQEDP
     GHLKVYQGHN EQGMASTAIA YSRQLYRHKI FAVTASAGPG SANFVTAAGN AYVNSIPILF
     LPADTFATRQ PDPVLQQIEV DYSADTTTND VLKPVSKYWD RIERPEQLMS ALLKAFEVLT
     NPATAGPVTI ALPQDVEGQA YDYPLSFFKK RVHVVKRVQP SSAELAGAVE LIQASQTPVL
     IVGGGAKFSD AGAAIETFSE RFNIPIVETP TGKSAISSDF PNNMGGTGIL GTAAANAVIT
     KADLIIGAGT RYTDFTTASK TAIHPGKTQL ININLNRMQS YKFDAFPIVA DVRDTLSQLT
     ESLSDYRSQF TDLATIKEAW QKERQRLAHT NYDAPAYVPE VKNQFDAKTM AAYAEKLQTH
     LTQTEAVIAV NNTIDPTSII VAAAGSLPGD VQRIWDPVVP NTYHMEYGYS MMGYEVPAAL
     GIKLAQPDQE SYALVGDGSF MMLHSELVTA LQYHKKINIL VFDNSGFASI NNLQMAQGSN
     SYLTEFRTSD NDIMKTDFAK IAEGYGAKAY RANDRKSLIA AIEDAKKQTV STLIDIKVLP
     KTMTQGYGQS WWRVGVSEIS NNPKVQKAYQ DIQTGIDKAF KY