ID   IOLU_BACSU              Reviewed;         328 AA.
AC   O05265;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=scyllo-inositol 2-dehydrogenase (NADP(+)) IolU {ECO:0000303|PubMed:28043209};
DE            EC=1.1.1.371 {ECO:0000269|PubMed:28043209};
DE   AltName: Full=NADP(+)-dependent scyllo-inositol dehydrogenase 2 {ECO:0000303|PubMed:28043209};
DE            Short=NADP(+)-dependent SI dehydrogenase 2 {ECO:0000303|PubMed:28043209};
GN   Name=iolU {ECO:0000303|PubMed:28043209};
GN   Synonyms=yulF {ECO:0000312|EMBL:CAB15095.1}; OrderedLocusNames=BSU31170;
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=9274030; DOI=10.1099/00221287-143-8-2769;
RA   Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA   Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT   "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT   of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL   Microbiology 143:2769-2774(1997).
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   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).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=168;
RX   PubMed=28043209; DOI=10.1080/09168451.2016.1268043;
RA   Kang D.M., Tanaka K., Takenaka S., Ishikawa S., Yoshida K.I.;
RT   "Bacillus subtilis iolU encodes an additional NADP(+)-dependent scyllo-
RT   inositol dehydrogenase.";
RL   Biosci. Biotechnol. Biochem. 81:1026-1032(2017).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of scyllo-inosose
CC       (SIS) to scyllo-inositol (SI) in vitro, but is unable to dehydrogenate
CC       scyllo-inositol and myo-inositol. Is less efficient than the functional
CC       paralog IolW. Under physiological conditions, may primarily function as
CC       an NADPH-dependent oxidoreductase that reduces carbonyl group(s) in its
CC       substrates. Cannot use NADH instead of NADPH.
CC       {ECO:0000269|PubMed:28043209}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + scyllo-inositol = H(+) + NADPH + scyllo-inosose;
CC         Xref=Rhea:RHEA:39063, ChEBI:CHEBI:10642, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17811, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.371; Evidence={ECO:0000269|PubMed:28043209};
CC   -!- INDUCTION: Is not induced in the presence of scyllo-inositol or myo-
CC       inositol. {ECO:0000269|PubMed:20133360}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; Z93938; CAB07947.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15095.1; -; Genomic_DNA.
DR   PIR; H70014; H70014.
DR   RefSeq; NP_390995.1; NC_000964.3.
DR   RefSeq; WP_003228926.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O05265; -.
DR   SMR; O05265; -.
DR   STRING; 224308.BSU31170; -.
DR   jPOST; O05265; -.
DR   PaxDb; O05265; -.
DR   PRIDE; O05265; -.
DR   EnsemblBacteria; CAB15095; CAB15095; BSU_31170.
DR   GeneID; 937153; -.
DR   KEGG; bsu:BSU31170; -.
DR   PATRIC; fig|224308.179.peg.3377; -.
DR   eggNOG; COG0673; Bacteria.
DR   InParanoid; O05265; -.
DR   OMA; FINYCQY; -.
DR   PhylomeDB; O05265; -.
DR   BioCyc; BSUB:BSU31170-MON; -.
DR   BRENDA; 1.1.1.371; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0102497; F:scyllo-inositol dehydrogenase (NADP+) activity; IDA:UniProtKB.
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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="scyllo-inositol 2-dehydrogenase (NADP(+)) IolU"
FT                   /id="PRO_0000091785"
SQ   SEQUENCE   328 AA;  36515 MW;  53134AD13A4B2835 CRC64;
     MIRFAIIGTN WITDRFLESA ADIEDFQLTA VYSRSAERAG EFAAKHNAAH AFSDLQEMAA
     SDCFDAVYIA SPNALHKEQA VLFMNHGKHV LCEKPFASNT KETEEMISAA KANGVVLMEA
     MKTTFLPNFK ELKKHLHKIG TVRRFTASYC QYSSRYDAFR SGTVLNAFQP ELSNGSLMDI
     GVYCIYPAVV LFGAPKDVKA NGYALSSGVD GEGTVILSYD GFEAVLMHSK ISTSYAPAEI
     QGEDGTIVID TIHRPERVEI RYRDGRLENI AIPDPKPAMF YEAEEFVTLI KENKLESEEN
     TFERSLTTAK IMEEARKQMG IVYPADQA