IOLD_LISMF
ID IOLD_LISMF Reviewed; 638 AA.
AC Q723S8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=LMOf2365_0398;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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=AAT03183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017262; AAT03183.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_074384934.1; NC_002973.6.
DR AlphaFoldDB; Q723S8; -.
DR SMR; Q723S8; -.
DR KEGG; lmf:LMOf2365_0398; -.
DR HOGENOM; CLU_013748_6_0_9; -.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; NAD; Thiamine pyrophosphate.
FT CHAIN 1..638
FT /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT hydrolase"
FT /id="PRO_0000352547"
FT REGION 442..523
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 67
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 494
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ SEQUENCE 638 AA; 70443 MW; 3071AEFAE67A682B CRC64;
MTEKTIRLTT AQALVKFLNQ QYIEVDGEMA PFVDGIFTLF GHGNVVGIGQ ALEEAPGHLK
VYQGKNEQGM AHAAIAYAKQ KNRQRIYACS TSAGPGSANL ITAAGTALAN NLPVLFLPAD
TFATRQPDPV LQQLEHESST AITTNDGFQA VSRYFDRVQR PEQLMSALIR AFEVMTNPAS
AGPATICIAQ DTEGEAFDYP VEFFQKRIHY LNRQIPTKRE LTEAARLIKA SKTPVIIVGG
GARYSRAREE LIALSEQTNI PLVETHAGKS TLEFDFKNNL GGTGILGTLA ANKAIRDADL
VIGIGTRYTD FTTSSKTAFD PTTKFININV SRMQTYKLDA FQVVGDAKAT LAELAPLLKG
YQTQFGNKIA AYKTEWLDER ARLQTTKFNR ETFTPEIKDQ FDQAILNEYA DRLQTEFTQT
EALITINDNV APDSIVVCSA GSLPGDLQRL WNPAVPDTYH LEYGYSCMGY EINGALGAKM
AAAKKQEVYA IVGDGSFCMS HSELLTSLQY GKKINIMLFD NSGFGCINNL QMANGSDSFF
CEFRDSDNQI MQVDYAKIAE GYGAKVYRAN TKEDLISALE DAKTQSKTTL IEMKVLPKTM
SEGYLNWWNV GVSEVSNKES IKQAYEEKQA NLKNARLY
