ID   IOLG_BACSU              Reviewed;         344 AA.
AC   P26935; Q6B6R7;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 66.
DE   RecName: Full=Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase;
DE            EC=1.1.1.18;
DE            EC=1.1.1.n6;
DE   AltName: Full=Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase;
DE            Short=MI 2-dehydrogenase/DCI 3-dehydrogenase;
GN   Name=iolG; Synonyms=idh; OrderedLocusNames=BSU39700; ORFNames=E83G;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=168 / 60015;
RX   MEDLINE=92104493; PubMed=1761221; DOI=10.1016/0378-1119(91)90496-X;
RA   Fujita Y., Shindo K., Miwa Y., Yoshida K.;
RT   "Bacillus subtilis inositol dehydrogenase-encoding gene (idh):
RT   sequence and expression in Escherichia coli.";
RL   Gene 108:121-125(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   MEDLINE=95039891; PubMed=7952181;
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Daniellou R., Phenix C.P., Tam P.H., Laliberte M.C., Palmer D.R.J.;
RT   "Probing the active site of Bacillus subtilis myo-inositol
RT   dehydrogenase.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=168 / 60015;
RX   MEDLINE=79239346; PubMed=112095;
RA   Ramaley R., Fujita Y., Freese E.;
RT   "Purification and properties of Bacillus subtilis inositol
RT   dehydrogenase.";
RL   J. Biol. Chem. 254:7684-7690(1979).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=168 / 60015;
RX   PubMed=16461681; DOI=10.1128/AEM.72.2.1310-1315.2006;
RA   Yoshida K., Yamaguchi M., Morinaga T., Ikeuchi M., Kinehara M.,
RA   Ashida H.;
RT   "Genetic modification of Bacillus subtilis for production of D-chiro-
RT   inositol, an investigational drug candidate for treatment of type 2
RT   diabetes and polycystic ovary syndrome.";
RL   Appl. Environ. Microbiol. 72:1310-1315(2006).
CC   -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) and D-
CC       chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose)
CC       and 1-keto-D-chiro-inositol (1KDCI), respectively. Can also use D-
CC       glucose and D-xylose, and shows a trace of activity with D-ribose
CC       and D-fructose.
CC   -!- CATALYTIC ACTIVITY: Myo-inositol + NAD(+) = 2,4,6/3,5-
CC       pentahydroxycyclohexanone + NADH.
CC   -!- CATALYTIC ACTIVITY: D-chiro-inositol + NAD(+) = 2,3,5/4,6-
CC       pentahydroxycyclohexanone + NADH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.036 mM for NADH (in the presence of 5 mM 2-inosose at 25
CC         degrees Celsius and pH 7);
CC         KM=0.23 mM for NAD (in the presence of 40 mM myo-inositol at 25
CC         degrees Celsius and pH 9);
CC         KM=1.61 mM for 2-inosose (in the presence of 0.1 mM NADH at 25
CC         degrees Celsius and pH 7);
CC         KM=18.2 mM for myo-inositol (in the presence of 0.5 mM NAD at 25
CC         degrees Celsius and pH 9);
CC         KM=55.6 mM for alpha-D-glucose (in the presence of 0.5 mM NAD at
CC         25 degrees Celsius and pH 9);
CC         KM=167 mM for D-glucose (in the presence of 0.5 mM NAD at 25
CC         degrees Celsius and pH 9);
CC         KM=190 mM for D-xylose (in the presence of 0.5 mM NAD at 25
CC         degrees Celsius and pH 9);
CC         Vmax=42 umol/min/mg enzyme for 2-inosose reduction reaction (at
CC         25 degrees Celsius and pH 7);
CC         Vmax=21 umol/min/mg enzyme for myo-inositol oxidation reaction
CC         (at 25 degrees Celsius and pH 9);
CC         Vmax=13.5 umol/min/mg enzyme with for alpha-D-glucose oxidation
CC         reaction (at 25 degrees Celsius and pH 9);
CC         Vmax=7.3 umol/min/mg enzyme for D-glucose oxidation reaction (at
CC         25 degrees Celsius and pH 9);
CC         Vmax=6.7 umol/min/mg enzyme for D-xylose oxidation reaction (at
CC         25 degrees Celsius and pH 9);
CC       pH dependence:
CC         Optimum pH is 9.5 for inositol 2-dehydrogenase activity;
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; acetyl-CoA from myo-inositol: step 1/7.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INDUCTION: By inositol. Subjected to catabolite repression.
CC   -!- SIMILARITY: Belongs to the gfo/idh/mocA family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M76431; AAA22543.1; -; Genomic_DNA.
DR   EMBL; D14399; BAA03296.1; -; Genomic_DNA.
DR   EMBL; AY676876; AAT78431.1; -; Genomic_DNA.
DR   EMBL; Z99124; CAB16006.1; -; Genomic_DNA.
DR   PIR; JH0511; JH0511.
DR   RefSeq; NP_391849.1; -.
DR   GeneID; 937615; -.
DR   GenomeReviews; AL009126_GR; BSU39700.
DR   KEGG; bsu:BSU39700; -.
DR   NMPDR; fig|224308.1.peg.3975; -.
DR   SubtiList; BG10669; iolG.
DR   HOGENOM; P26935; -.
DR   BioCyc; BSUB224308:BSU3966-MON; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01671; -; 1.
DR   InterPro; IPR000683; GFO/IDH/MocA_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR004104; OxRdtase_C.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    344       Inositol 2-dehydrogenase/D-chiro-inositol
FT                                3-dehydrogenase.
FT                                /FTId=PRO_0000091774.
FT   CONFLICT    145    145       N -> I (in Ref. 3; AAT78431).
SQ   SEQUENCE   344 AA;  38352 MW;  2FCE908D4E2C332F CRC64;
     MSLRIGVIGT GAIGKEHINR ITNKLSGAEI VAVTDVNQEA AQKVVEQYQL NATVYPNDDS
     LLADENVDAV LVTSWGPAHE SSVLKAIKAQ KYVFCEKPLA TTAEGCMRIV EEEIKVGKRL
     VQVGFMRRYD SGYVQLKEAL DNHVNGEPLM IHCAHRNPTV GDNYTTDMAV VDTLVHEIDV
     LHWLVNDDYE SVQVIYPKKS KNALPHLKDP QIVVIETKGG IVINAEIYVN CKYGYDIQCE
     IVGEDGIIKL PEPSSISLRK EGRFSTDILM DWQRRFVAAY DVEIQDFIDS IQKKGEVSGP
     TAWDGYIAAV TTDACVKAQE SGQKEKVELK EKPEFYQSFT TVQN
//