ID   IOLE_YERE8              Reviewed;         298 AA.
AC   A1JSK6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Inosose dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE            EC=4.2.1.44 {ECO:0000255|HAMAP-Rule:MF_01672};
DE   AltName: Full=2-keto-myo-inositol dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE            Short=2KMI dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
GN   Name=iolE {ECO:0000255|HAMAP-Rule:MF_01672}; OrderedLocusNames=YE4025;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Catalyzes the dehydration of inosose (2-keto-myo-inositol,
CC       2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-
CC       trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
CC       {ECO:0000255|HAMAP-Rule:MF_01672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=scyllo-inosose = 3D-3,5/4-trihydroxycyclohexane-1,2-dione +
CC         H2O; Xref=Rhea:RHEA:14065, ChEBI:CHEBI:15377, ChEBI:CHEBI:17811,
CC         ChEBI:CHEBI:28446; EC=4.2.1.44; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01672};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC   -!- SIMILARITY: Belongs to the IolE/MocC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01672}.
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; AM286415; CAL14043.1; -; Genomic_DNA.
DR   RefSeq; WP_011817366.1; NC_008800.1.
DR   RefSeq; YP_001008389.1; NC_008800.1.
DR   AlphaFoldDB; A1JSK6; -.
DR   SMR; A1JSK6; -.
DR   STRING; 393305.YE4025; -.
DR   EnsemblBacteria; CAL14043; CAL14043; YE4025.
DR   KEGG; yen:YE4025; -.
DR   PATRIC; fig|393305.7.peg.4285; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_059523_0_0_6; -.
DR   OMA; YDSRPEL; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050114; F:myo-inosose-2 dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01672; IolE; 1.
DR   InterPro; IPR023952; IolE.
DR   InterPro; IPR030823; IolE/MocC.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR04379; myo_inos_iolE; 1.
PE   3: Inferred from homology;
KW   Cobalt; Lyase; Manganese.
FT   CHAIN           1..298
FT                   /note="Inosose dehydratase"
FT                   /id="PRO_0000352381"
SQ   SEQUENCE   298 AA;  33627 MW;  7450D50DCB54E56A CRC64;
     MNKDRVKLAI APIGWTNDDM PDLGKENTFQ QCISEMALAG FIGSEVGSKY PRDPNVLKPM
     LELRGMQICN AWFSTFFADG QRARTIDEFT NHMNFLHAMG AKVIGCSEQS KSIQGTTKAI
     FEEKPYFTDT EWQRVAEGYN ELAKIAATKG MQVCLHHHMG TGIQTTEEID RYMSMVNDDV
     YLLFDTGHAY YSEGSQEAML AILEKYLPRI NHVHLKDVRD EVVAEVKAKK LSFLDGVKKG
     TFTVPGDGVI DFRPVFKLLD EKGYQGWMVV EAEQDPAIAN PFEYAVKARR YIKETAGI