ID A0A1H1ZE38_9BACL Unreviewed; 637 AA.
AC A0A1H1ZE38;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000256|HAMAP-Rule:MF_01669};
DE Short=THcHDO hydrolase {ECO:0000256|HAMAP-Rule:MF_01669};
DE EC=3.7.1.22 {ECO:0000256|HAMAP-Rule:MF_01669};
GN Name=iolD {ECO:0000256|HAMAP-Rule:MF_01669};
GN ORFNames=SAMN05444162_3806 {ECO:0000313|EMBL:SDT31807.1};
OS Paenibacillaceae bacterium GAS479.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX NCBI_TaxID=1882832 {ECO:0000313|EMBL:SDT31807.1, ECO:0000313|Proteomes:UP000198637};
RN [1] {ECO:0000313|EMBL:SDT31807.1, ECO:0000313|Proteomes:UP000198637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS479 {ECO:0000313|EMBL:SDT31807.1,
RC ECO:0000313|Proteomes:UP000198637};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01669};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01669};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01669}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|HAMAP-Rule:MF_01669}.
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DR EMBL; LT629764; SDT31807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ZE38; -.
DR STRING; 1882832.SAMN05444162_3806; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000198637; Chromosome i.
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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01669};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01669};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01669};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01669};
KW Reference proteome {ECO:0000313|Proteomes:UP000198637};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01669}.
FT DOMAIN 8..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 440..592
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
SQ SEQUENCE 637 AA; 69666 MW; 93E3BFBFBEC0C95A CRC64;
MAGTIRLTTS QALIKFLNQQ YIHVDGEESP FVEGIFTVFG HGNVLGIGQA LEQDSGHLKV
FQGKNEQGMA HAAIAFSKEK RRRKIMAVST SAGPGSANVV TAAATALANQ LPVLFLPGDT
FATRQPDPVL QQLEQEYSIA VTTNDALKPV SRYWDRITRP EQLMSSLLRA FEVLTDPARC
GPVTICICQD TEGEAFDYDE AFFRKRVHYM DRLAPSEREL LAATELIRRS RRPLIIAGGG
VRYSGAREEL MAFSTAYNIP IVETQAGKSA VESTFANNLG GMGLTGTSSA NKAAQEADLI
IGIGTRYSDF TTSSKTAFNF ENTAFLNINV SRLHAYKLDA LQVVADAKTA LSGLHAMLEG
YRSQFGERIG QLKREWDGER ERLAGIVFAR EDFDPEVKGH FTQEQLNEYA DALGTELPQS
SALLAINEAL APDSIIVGAA GSLPGDLQRA WSASVPDTYH VEYGYSCMGY EISGALGVKL
AKPDHEVYSI VGDGSFLMLH SELITALQYN HKINILLFDN SGFGCINNLQ MGNGGGSYFC
EFRNDEKQIM NIDYAKVAEG YGAKVYRANT LEQLREALAD AKGQSRSTLI DIKVLPKTMT
DGYGGWWNVG VAEVSESESI RQAHESRMSK LQGAKSY
//
