ID   IOLE2_BACCZ             Reviewed;         298 AA.
AC   Q4V1F4;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Inosose dehydratase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01672};
DE            Short=2KMI dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_01672};
GN   Name=iolE2 {ECO:0000255|HAMAP-Rule:MF_01672};
GN   OrderedLocusNames=pE33L466_0303;
OS   Bacillus cereus (strain ZK / E33L).
OG   Plasmid pE33L466.
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; CP000040; AAY60453.1; -; Genomic_DNA.
DR   RefSeq; WP_000471974.1; NZ_CP009967.1.
DR   AlphaFoldDB; Q4V1F4; -.
DR   SMR; Q4V1F4; -.
DR   EnsemblBacteria; AAY60453; AAY60453; pE33L466_0303.
DR   KEGG; bcz:pE33L466_0303; -.
DR   PATRIC; fig|288681.22.peg.5503; -.
DR   OMA; VHCKDIR; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000002612; Plasmid pE33L466.
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; Plasmid.
FT   CHAIN           1..298
FT                   /note="Inosose dehydratase 2"
FT                   /id="PRO_0000352355"
SQ   SEQUENCE   298 AA;  33499 MW;  8837F2AF66CFAF04 CRC64;
     MFKENTIKLG IAPIAWTNDD MPELGAENTF EQCISEMALA GFNGSEVGNK YPRNTVVLKK
     SLELRNLEIA SAWFSAFLTT KPLEETVQAF IKHRDFLHDM GAKVIVVSEQ GHSIQGLMDV
     PLFKNKPVFT EEEWEKLADG LHHLGKLAQE KGLHIVYHHH MGTGVQTTAE IEKLMDMTDP
     ELVSLLFDTG HLVFSGEEPL YILKKYLSRI KHVHLKDIRQ EVVDAVKESD LSFLQAVKNG
     AFTVPGDGVI VFDEVFTILA NSDYKGWFVV EAEQDPALAN PFEYALKARK FIQEKAGL