IOLX_BACSU
ID IOLX_BACSU Reviewed; 342 AA.
AC P40332; O07924;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=scyllo-inositol 2-dehydrogenase (NAD(+));
DE EC=1.1.1.370 {ECO:0000269|PubMed:20133360};
GN Name=iolX {ECO:0000303|PubMed:20133360}; Synonyms=yisS, yucG, yuxD;
GN OrderedLocusNames=BSU10850;
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;
RX PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT position encoding 11 membrane proteins.";
RL Microbiology 143:3309-3312(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Oudega B., Koningstein G., Duesterhoeft A.;
RT "Bacillus subtilis genome project, DNA sequence from yucA to yucH.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92.
RC STRAIN=168 / DB104;
RX PubMed=8407808; DOI=10.1128/jb.175.19.6348-6353.1993;
RA Bussey L.B., Switzer R.L.;
RT "The degA gene product accelerates degradation of Bacillus subtilis
RT phosphoribosylpyrophosphate amidotransferase in Escherichia coli.";
RL J. Bacteriol. 175:6348-6353(1993).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RC STRAIN=168 / 60015;
RX PubMed=20133360; DOI=10.1099/mic.0.037499-0;
RA Morinaga T., Ashida H., Yoshida K.;
RT "Identification of two scyllo-inositol dehydrogenases in Bacillus
RT subtilis.";
RL Microbiology 156:1538-1546(2010).
CC -!- FUNCTION: Catalyzes the reversible NAD(+)-dependent oxidation of
CC scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo-
CC inosose or SIS). Is required for SI catabolism that allows B.subtilis
CC to utilize SI as the sole carbon source for growth. Cannot use NADP(+)
CC instead of NAD(+). {ECO:0000269|PubMed:20133360}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + scyllo-inositol = H(+) + NADH + scyllo-inosose;
CC Xref=Rhea:RHEA:17613, ChEBI:CHEBI:10642, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17811, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.370; Evidence={ECO:0000269|PubMed:20133360};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.1 mM for scyllo-inositol {ECO:0000269|PubMed:20133360};
CC KM=2.85 mM for scyllo-inosose {ECO:0000269|PubMed:20133360};
CC KM=0.15 mM for NAD(+) {ECO:0000269|PubMed:20133360};
CC KM=0.019 mM for NADH {ECO:0000269|PubMed:20133360};
CC Vmax=6.43 umol/min/mg enzyme toward scyllo-inositol
CC {ECO:0000269|PubMed:20133360};
CC Vmax=63.8 umol/min/mg enzyme toward scyllo-inosose
CC {ECO:0000269|PubMed:20133360};
CC Vmax=5.85 umol/min/mg enzyme toward NAD(+)
CC {ECO:0000269|PubMed:20133360};
CC Vmax=73.2 umol/min/mg enzyme toward NADH
CC {ECO:0000269|PubMed:20133360};
CC -!- PATHWAY: Polyol metabolism. {ECO:0000269|PubMed:20133360}.
CC -!- INDUCTION: Induced by either myo-inositol (MI) or SI; SI is
CC approximately three times more efficient than MI.
CC {ECO:0000269|PubMed:20133360}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of this gene abolishes growth on SI
CC as the sole carbon source, but does not affect growth on MI or glucose.
CC {ECO:0000269|PubMed:20133360}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; Y09476; CAA70648.1; -; Genomic_DNA.
DR EMBL; Z93940; CAB07962.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12924.1; -; Genomic_DNA.
DR EMBL; L08822; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; B69838; B69838.
DR RefSeq; NP_388965.1; NC_000964.3.
DR RefSeq; WP_003244942.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P40332; -.
DR SMR; P40332; -.
DR STRING; 224308.BSU10850; -.
DR PaxDb; P40332; -.
DR PRIDE; P40332; -.
DR EnsemblBacteria; CAB12924; CAB12924; BSU_10850.
DR GeneID; 939785; -.
DR KEGG; bsu:BSU10850; -.
DR PATRIC; fig|224308.179.peg.1167; -.
DR eggNOG; COG0673; Bacteria.
DR InParanoid; P40332; -.
DR OMA; CEKPVAR; -.
DR PhylomeDB; P40332; -.
DR BioCyc; BSUB:BSU10850-MON; -.
DR BioCyc; MetaCyc:BSU10850-MON; -.
DR BRENDA; 1.1.1.370; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:1902141; P:cellular response to inositol; IDA:UniProtKB.
DR GO; GO:0019310; P:inositol catabolic process; IMP:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..342
FT /note="scyllo-inositol 2-dehydrogenase (NAD(+))"
FT /id="PRO_0000091783"
SQ SEQUENCE 342 AA; 37484 MW; B6DF205F9E4B0103 CRC64;
MEHQVRCAVL GLGRLGYYHA KNLVTSVPGA KLVCVGDPLK GRAEQVAREL GIEKWSEDPY
EVLEDPGIDA VIIVTPTSTH GDMIIKAAEN GKQIFVEKPL TLSLEESKAA SEKVKETGVI
CQVGFMRRFD PAYADAKRRI DAGEIGKPIY YKGFTRDQGA PPAEFIKHSG GIFIDCSIHD
YDIARYLLGA EITSVSGHGR ILNNPFMEQY GDVDQALTYI EFDSGAAGDV EASRTSPYGH
DIRAEVIGTE GSIFIGTLRH QHVTILSAKG SSFDIIPDFQ TRFHEAYCLE LQHFAECVRN
GKTPIVTDID ATINLEVGIA ATNSFRNGMP VQLDVKRAYT GM
