ID   IOLE_CLOB8              Reviewed;         298 AA.
AC   A6M225;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Cbei_4546;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000721; ABR36655.1; -; Genomic_DNA.
DR   RefSeq; WP_012060702.1; NC_009617.1.
DR   AlphaFoldDB; A6M225; -.
DR   SMR; A6M225; -.
DR   STRING; 290402.Cbei_4546; -.
DR   EnsemblBacteria; ABR36655; ABR36655; Cbei_4546.
DR   KEGG; cbe:Cbei_4546; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_059523_0_0_9; -.
DR   OMA; VHCKDIR; -.
DR   OrthoDB; 1194699at2; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000000565; 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_0000352361"
SQ   SEQUENCE   298 AA;  33887 MW;  67AD26CF429AE788 CRC64;
     MLNTEKVKLG ICPIGWTNDD MPDLGKENTF EQAVSEMALA GFKGTEVGNK YPKDVNVLKK
     ALDLRNLQIA SAWFSSFLTT KPYEETEKEF IAHRDFLHEM GAKVIVVSEQ GHSIQGEMDT
     PICEGKYYFN EEEWKLLADG LNKLGRLAED KGMKIVYHHH MGTGVQTTDE IDKLMSMTDE
     SLVYLLFDTG HLVYSGENPI AILNKYANRI KHVHLKDIRA DVLEKVKKEK MSFLMGVREG
     SFTVPGDGCI DFEPIFKILD ENNYEGWILV EAEQDPAIAN PFEYAMKARK YIKEKTGF