ID   IOLE1_BACCZ             Reviewed;         298 AA.
AC   Q63B72;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Inosose dehydratase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01672};
DE            Short=2KMI dehydratase 1 {ECO:0000255|HAMAP-Rule:MF_01672};
GN   Name=iolE1 {ECO:0000255|HAMAP-Rule:MF_01672}; OrderedLocusNames=BCE33L2255;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(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; CP000001; AAU18002.1; -; Genomic_DNA.
DR   RefSeq; WP_000471994.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q63B72; -.
DR   SMR; Q63B72; -.
DR   EnsemblBacteria; AAU18002; AAU18002; BCE33L2255.
DR   KEGG; bcz:BCE33L2255; -.
DR   PATRIC; fig|288681.22.peg.3244; -.
DR   OMA; VHIKQMD; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000002612; 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 1"
FT                   /id="PRO_0000352354"
SQ   SEQUENCE   298 AA;  33409 MW;  AF88AA0FD8609053 CRC64;
     MFKENTVKLG IAPIAWTNDD MPELGAGNTF EQCISEMALA GFNGSEVGNK YPRNTVVLKK
     SLALRNLEIA SAWFSTFLTT KPLEETVEEF IKHRDFLHDM GAKVIVVSEQ GHSIQGLMDV
     PLFKNKPVFT EEEWNKLADG LHHLGKLAQE KGLHIVYHHH MGTGVQTTAE IEKLMDMTNP
     ALVSLLFDTG HLVFSGEEPL YILKKYLPRI KHVHLKDIRQ EVVDTVKENE LSFLQAVKNG
     AFTVPGDGVI GFDEVFTILA NSDYQGWFVV EAEQDPALAN PFEYALKARK FIQEKAGL