(data stored in ACNUC10821 zone)

SWISSPROT: 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   08-MAY-2019, entry version 81.
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.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome 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-
CC       (3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-
CC       glucuronate (5DG). {ECO:0000255|HAMAP-Rule:MF_01669}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-
CC         D-glucuronate + H(+); Xref=Rhea:RHEA:25836, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28446, ChEBI:CHEBI:58852;
CC         EC=3.7.1.22; 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-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_01669};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; 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};
DR   EMBL; AE017262; AAT03183.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_074384934.1; NC_002973.6.
DR   EnsemblBacteria; AAT03183; AAT03183; LMOf2365_0398.
DR   KEGG; lmf:LMOf2365_0398; -.
DR   HOGENOM; HOG000239708; -.
DR   KO; K03336; -.
DR   BioCyc; LMON265669:G1G0V-417-MONOMER; -.
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; IPR011766; TPP_enzyme-bd_C.
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;
DR   PRODOM; Q723S8.
DR   SWISS-2DPAGE; Q723S8.
KW   Hydrolase; Magnesium; Metal-binding; NAD; Thiamine pyrophosphate.
FT   CHAIN         1    638       3D-(3,5/4)-trihydroxycyclohexane-1,2-
FT                                dione hydrolase.
FT                                /FTId=PRO_0000352547.
FT   REGION      442    523       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01669}.
FT   METAL       494    494       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01669}.
FT   METAL       521    521       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01669}.
FT   BINDING      67     67       Thiamine pyrophosphate.
FT                                {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
//

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