ID   IOLE_CLOP1              Reviewed;         297 AA.
AC   Q0TUZ0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=CPF_0086;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 2/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01672}.
CC   -!- SIMILARITY: Belongs to the IolE/MocC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01672}.
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DR   EMBL; CP000246; ABG83745.1; -; Genomic_DNA.
DR   RefSeq; WP_003459953.1; NC_008261.1.
DR   AlphaFoldDB; Q0TUZ0; -.
DR   SMR; Q0TUZ0; -.
DR   STRING; 195103.CPF_0086; -.
DR   EnsemblBacteria; ABG83745; ABG83745; CPF_0086.
DR   GeneID; 29570825; -.
DR   KEGG; cpf:CPF_0086; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_059523_0_0_9; -.
DR   OMA; VHCKDIR; -.
DR   OrthoDB; 1194699at2; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000001823; 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..297
FT                   /note="Inosose dehydratase"
FT                   /id="PRO_0000352365"
SQ   SEQUENCE   297 AA;  33753 MW;  AE38F1CA3BDD05E9 CRC64;
     MFNSNVKLGI APIAWTNDDM PDLGKENTFE QCISEMALAG FKGSEVGNKY PRDVKVLKKA
     LELRDMEIAS AWFSAFLTTK PYEETEKAFI EHRDFLNAMG AKVIVVSEQG HSIQGQMETP
     IFDGKYVLNE EEWKTLAEGL NKLGALAKEK GMKLVYHHHM GTVVQTTEEI DKLMDLTDEN
     LVYLLFDSGH LVYSGEDALE VLKKYVNRVK HVHLKDIRKE KVEEVKRDKL SFLQGVRKGA
     FTVPGDGDID FEPIFKVLDD NNYEGYLLVE AEQDPAIANP LEYAIKARKY IKEKTNL