IOLE_BACSU
ID IOLE_BACSU Reviewed; 297 AA.
AC P42416;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Inosose dehydratase;
DE EC=4.2.1.44;
DE AltName: Full=2-keto-myo-inositol dehydratase;
DE Short=2KMI dehydratase;
GN Name=iolE; Synonyms=yxdE; OrderedLocusNames=BSU39720; ORFNames=E83E;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7952181; DOI=10.1099/13500872-140-9-2289;
RA Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y.;
RT "Cloning and nucleotide sequencing of a 15 kb region of the Bacillus
RT subtilis genome containing the iol operon.";
RL Microbiology 140:2289-2298(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RX PubMed=14993306; DOI=10.1099/mic.0.26768-0;
RA Yoshida K., Yamaguchi M., Ikeda H., Omae K., Tsurusaki K., Fujita Y.;
RT "The fifth gene of the iol operon of Bacillus subtilis, iolE, encodes 2-
RT keto-myo-inositol dehydratase.";
RL Microbiology 150:571-580(2004).
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:0000269|PubMed:14993306}.
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;
CC Evidence={ECO:0000269|PubMed:14993306};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:14993306};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:14993306};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14993306};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.65 mM for inosose (at pH 8) {ECO:0000269|PubMed:14993306};
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:14993306};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 2/7.
CC -!- INDUCTION: By inositol. {ECO:0000269|PubMed:14993306}.
CC -!- SIMILARITY: Belongs to the IolE/MocC family. {ECO:0000305}.
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DR EMBL; D14399; BAA03294.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16008.1; -; Genomic_DNA.
DR PIR; E69645; E69645.
DR RefSeq; NP_391851.1; NC_000964.3.
DR RefSeq; WP_003227062.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42416; -.
DR SMR; P42416; -.
DR STRING; 224308.BSU39720; -.
DR PaxDb; P42416; -.
DR PRIDE; P42416; -.
DR EnsemblBacteria; CAB16008; CAB16008; BSU_39720.
DR GeneID; 936212; -.
DR KEGG; bsu:BSU39720; -.
DR PATRIC; fig|224308.179.peg.4297; -.
DR eggNOG; COG1082; Bacteria.
DR InParanoid; P42416; -.
DR OMA; YDSRPEL; -.
DR PhylomeDB; P42416; -.
DR BioCyc; BSUB:BSU39720-MON; -.
DR BioCyc; MetaCyc:BSU39720-MON; -.
DR UniPathway; UPA00076; UER00144.
DR PRO; PR:P42416; -.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Cobalt; Lyase; Manganese; Reference proteome.
FT CHAIN 1..297
FT /note="Inosose dehydratase"
FT /id="PRO_0000084213"
SQ SEQUENCE 297 AA; 33588 MW; 38E44632D6022E94 CRC64;
MGKNEILWGI APIGWRNDDM PEIGAGNTLQ HLLSDIVVAR FQGTEVGGFF PEPAILNKEL
KLRNLRIAGK WFSSFILRDG LGEAAKTFTL HCEYLQQVNA DVAVVSEQTY SVQSLEKNVF
TEKPHFTDDE WERLCEGLNH LGEIAAQHGL KLVYHHHLGT GVQTAEEVDR LMAGTDPAHV
HLLYDTGHAY ISDGDYMGML EKHIGRIKHV HFKDARLNVM EQCRLEGQSF RQSFLKGMFT
VPGDGCIDFR EVYQLLLKHS YSGWIVIEAE QDPDVANPLE YALIARNYID QQLLDLA
