IOLG_BACSU
ID IOLG_BACSU Reviewed; 344 AA.
AC P26935; Q6B6R7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase;
DE EC=1.1.1.18;
DE EC=1.1.1.369;
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 (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=168 / 60015;
RX 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): sequence and
RT expression in Escherichia coli.";
RL Gene 108:121-125(1991).
RN [2]
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 [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 dehydrogenase.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SEQUENCE REVISION TO 145.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=168 / 60015;
RX PubMed=112095; DOI=10.1016/s0021-9258(18)36000-9;
RA Ramaley R., Fujita Y., Freese E.;
RT "Purification and properties of Bacillus subtilis inositol dehydrogenase.";
RL J. Biol. Chem. 254:7684-7690(1979).
RN [7]
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., 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-chiro-
CC inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-
CC chiro-inositol (1KDCI), respectively. Can also use D-glucose and D-
CC xylose, and shows a trace of activity with D-ribose and D-fructose.
CC {ECO:0000269|PubMed:112095, ECO:0000269|PubMed:16461681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose;
CC Xref=Rhea:RHEA:16949, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:17811, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.18;
CC Evidence={ECO:0000269|PubMed:16461681};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-chiro-inositol + NAD(+) = H(+) + NADH + scyllo-inosine;
CC Xref=Rhea:RHEA:25832, ChEBI:CHEBI:15378, ChEBI:CHEBI:27372,
CC ChEBI:CHEBI:50920, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.369; Evidence={ECO:0000269|PubMed:16461681};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.036 mM for NADH (in the presence of 5 mM 2-inosose at 25 degrees
CC Celsius and pH 7) {ECO:0000269|PubMed:112095};
CC KM=0.23 mM for NAD (in the presence of 40 mM myo-inositol at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC KM=1.61 mM for 2-inosose (in the presence of 0.1 mM NADH at 25
CC degrees Celsius and pH 7) {ECO:0000269|PubMed:112095};
CC KM=18.2 mM for myo-inositol (in the presence of 0.5 mM NAD at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC KM=55.6 mM for alpha-D-glucose (in the presence of 0.5 mM NAD at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC KM=167 mM for D-glucose (in the presence of 0.5 mM NAD at 25 degrees
CC Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC KM=190 mM for D-xylose (in the presence of 0.5 mM NAD at 25 degrees
CC Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC Vmax=42 umol/min/mg enzyme for 2-inosose reduction reaction (at 25
CC degrees Celsius and pH 7) {ECO:0000269|PubMed:112095};
CC Vmax=21 umol/min/mg enzyme for myo-inositol oxidation reaction (at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC Vmax=13.5 umol/min/mg enzyme with for alpha-D-glucose oxidation
CC reaction (at 25 degrees Celsius and pH 9)
CC {ECO:0000269|PubMed:112095};
CC Vmax=7.3 umol/min/mg enzyme for D-glucose oxidation reaction (at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC Vmax=6.7 umol/min/mg enzyme for D-xylose oxidation reaction (at 25
CC degrees Celsius and pH 9) {ECO:0000269|PubMed:112095};
CC pH dependence:
CC Optimum pH is 9.5 for inositol 2-dehydrogenase activity.
CC {ECO:0000269|PubMed:112095};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 1/7.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:112095}.
CC -!- INDUCTION: By inositol. Subjected to catabolite repression.
CC {ECO:0000269|PubMed:1761221}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; M76431; AAA22543.1; -; Genomic_DNA.
DR EMBL; D14399; BAA03296.1; -; Genomic_DNA.
DR EMBL; AY676876; AAT78431.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16006.2; -; Genomic_DNA.
DR PIR; JH0511; JH0511.
DR RefSeq; NP_391849.2; NC_000964.3.
DR RefSeq; WP_003244482.1; NZ_JNCM01000034.1.
DR PDB; 3MZ0; X-ray; 1.54 A; A=1-344.
DR PDB; 3NT2; X-ray; 2.30 A; A/B=1-344.
DR PDB; 3NT4; X-ray; 2.50 A; A/B=1-344.
DR PDB; 3NT5; X-ray; 2.90 A; A/B=1-344.
DR PDB; 3NTO; X-ray; 1.91 A; A=1-344.
DR PDB; 3NTQ; X-ray; 2.60 A; A/B=1-344.
DR PDB; 3NTR; X-ray; 2.65 A; A/B=1-344.
DR PDB; 4L8V; X-ray; 2.09 A; A/B/C/D=1-337.
DR PDB; 4L9R; X-ray; 1.95 A; A=1-337.
DR PDBsum; 3MZ0; -.
DR PDBsum; 3NT2; -.
DR PDBsum; 3NT4; -.
DR PDBsum; 3NT5; -.
DR PDBsum; 3NTO; -.
DR PDBsum; 3NTQ; -.
DR PDBsum; 3NTR; -.
DR PDBsum; 4L8V; -.
DR PDBsum; 4L9R; -.
DR AlphaFoldDB; P26935; -.
DR SMR; P26935; -.
DR STRING; 224308.BSU39700; -.
DR PaxDb; P26935; -.
DR PRIDE; P26935; -.
DR EnsemblBacteria; CAB16006; CAB16006; BSU_39700.
DR GeneID; 937615; -.
DR KEGG; bsu:BSU39700; -.
DR PATRIC; fig|224308.179.peg.4295; -.
DR eggNOG; COG0673; Bacteria.
DR InParanoid; P26935; -.
DR OMA; VNCKYGY; -.
DR PhylomeDB; P26935; -.
DR BioCyc; BSUB:BSU39700-MON; -.
DR BioCyc; MetaCyc:BSU39700-MON; -.
DR BRENDA; 1.1.1.18; 658.
DR BRENDA; 1.1.1.369; 658.
DR SABIO-RK; P26935; -.
DR UniPathway; UPA00076; UER00143.
DR EvolutionaryTrace; P26935; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01671; IolG; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR023794; MI/DCI_dehydrogenase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..344
FT /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT dehydrogenase"
FT /id="PRO_0000091774"
FT CONFLICT 145
FT /note="I -> N (in Ref. 1; AAA22543 and 2; BAA03296)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:3MZ0"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3MZ0"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3NTR"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:3MZ0"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:3MZ0"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3NT2"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3MZ0"
SQ SEQUENCE 344 AA; 38351 MW; 92464EDEC3A735F6 CRC64;
MSLRIGVIGT GAIGKEHINR ITNKLSGAEI VAVTDVNQEA AQKVVEQYQL NATVYPNDDS
LLADENVDAV LVTSWGPAHE SSVLKAIKAQ KYVFCEKPLA TTAEGCMRIV EEEIKVGKRL
VQVGFMRRYD SGYVQLKEAL DNHVIGEPLM IHCAHRNPTV GDNYTTDMAV VDTLVHEIDV
LHWLVNDDYE SVQVIYPKKS KNALPHLKDP QIVVIETKGG IVINAEIYVN CKYGYDIQCE
IVGEDGIIKL PEPSSISLRK EGRFSTDILM DWQRRFVAAY DVEIQDFIDS IQKKGEVSGP
TAWDGYIAAV TTDACVKAQE SGQKEKVELK EKPEFYQSFT TVQN
