IOLW_BACSU
ID IOLW_BACSU Reviewed; 358 AA.
AC O32223;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=scyllo-inositol 2-dehydrogenase (NADP(+)) IolW {ECO:0000303|PubMed:20133360};
DE EC=1.1.1.371 {ECO:0000269|PubMed:20133360, ECO:0000269|PubMed:28043209};
DE AltName: Full=NADP(+)-dependent scyllo-inositol dehydrogenase 1 {ECO:0000303|PubMed:28043209};
DE Short=NADP(+)-dependent SI dehydrogenase 1 {ECO:0000303|PubMed:28043209};
GN Name=iolW {ECO:0000303|PubMed:20133360}; Synonyms=yvaA;
GN OrderedLocusNames=BSU33530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, AND DISRUPTION PHENOTYPE.
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 [3]
RP INDUCTION.
RX PubMed=22383849; DOI=10.1126/science.1206848;
RA Nicolas P., Maeder U., Dervyn E., Rochat T., Leduc A., Pigeonneau N.,
RA Bidnenko E., Marchadier E., Hoebeke M., Aymerich S., Becher D.,
RA Bisicchia P., Botella E., Delumeau O., Doherty G., Denham E.L., Fogg M.J.,
RA Fromion V., Goelzer A., Hansen A., Haertig E., Harwood C.R., Homuth G.,
RA Jarmer H., Jules M., Klipp E., Le Chat L., Lecointe F., Lewis P.,
RA Liebermeister W., March A., Mars R.A., Nannapaneni P., Noone D., Pohl S.,
RA Rinn B., Ruegheimer F., Sappa P.K., Samson F., Schaffer M., Schwikowski B.,
RA Steil L., Stuelke J., Wiegert T., Devine K.M., Wilkinson A.J.,
RA van Dijl J.M., Hecker M., Voelker U., Bessieres P., Noirot P.;
RT "Condition-dependent transcriptome reveals high-level regulatory
RT architecture in Bacillus subtilis.";
RL Science 335:1103-1106(2012).
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 3-358.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of putative oxidoreductase YvaA from Bacillus subtilis.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible NADPH-dependent reduction of scyllo-
CC inosose (SIS) to scyllo-inositol (SI). Cannot use NADH instead of
CC NADPH. May be involved in reduction of not only SIS but also various
CC oxidized compounds manifested upon stressful conditions.
CC {ECO:0000269|PubMed:20133360, 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:20133360,
CC ECO:0000269|PubMed:28043209};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34.3 mM for scyllo-inositol {ECO:0000269|PubMed:20133360};
CC KM=1.68 mM for scyllo-inosose {ECO:0000269|PubMed:20133360};
CC KM=0.096 mM for NADP(+) {ECO:0000269|PubMed:20133360};
CC KM=0.027 mM for NADPH {ECO:0000269|PubMed:20133360};
CC Vmax=3.46 umol/min/mg enzyme toward scyllo-inositol
CC {ECO:0000269|PubMed:20133360};
CC Vmax=127.1 umol/min/mg enzyme toward scyllo-inosose
CC {ECO:0000269|PubMed:20133360};
CC Vmax=3.43 umol/min/mg enzyme toward NADP(+)
CC {ECO:0000269|PubMed:20133360};
CC Vmax=109.1 umol/min/mg enzyme toward NADPH
CC {ECO:0000269|PubMed:20133360};
CC -!- INDUCTION: Is constitutively expressed, even in the absence of both
CC myo-inositol and scillo-inositol (PubMed:20133360). Is up-regulated
CC under certain stressful conditions (PubMed:22383849).
CC {ECO:0000269|PubMed:20133360, ECO:0000269|PubMed:22383849}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show normal growth on SI
CC as well as on glucose or myo-inositol (MI) as the sole carbon source.
CC {ECO:0000269|PubMed:20133360}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15358.1; -; Genomic_DNA.
DR PIR; G70026; G70026.
DR RefSeq; NP_391233.1; NC_000964.3.
DR RefSeq; WP_009968169.1; NZ_JNCM01000033.1.
DR PDB; 3GDO; X-ray; 2.03 A; A/B=12-358.
DR PDB; 3GFG; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J/K/L=3-358.
DR PDBsum; 3GDO; -.
DR PDBsum; 3GFG; -.
DR AlphaFoldDB; O32223; -.
DR SMR; O32223; -.
DR STRING; 224308.BSU33530; -.
DR PaxDb; O32223; -.
DR PRIDE; O32223; -.
DR DNASU; 936109; -.
DR EnsemblBacteria; CAB15358; CAB15358; BSU_33530.
DR GeneID; 936109; -.
DR KEGG; bsu:BSU33530; -.
DR PATRIC; fig|224308.179.peg.3638; -.
DR eggNOG; COG0673; Bacteria.
DR InParanoid; O32223; -.
DR OMA; RFERWRP; -.
DR PhylomeDB; O32223; -.
DR BioCyc; BSUB:BSU33530-MON; -.
DR BioCyc; MetaCyc:BSU33530-MON; -.
DR BRENDA; 1.1.1.371; 658.
DR EvolutionaryTrace; O32223; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0070401; F:NADP+ binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
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 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..358
FT /note="scyllo-inositol 2-dehydrogenase (NADP(+)) IolW"
FT /id="PRO_0000049934"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3GDO"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:3GFG"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:3GDO"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3GDO"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:3GDO"
FT HELIX 331..350
FT /evidence="ECO:0007829|PDB:3GDO"
SQ SEQUENCE 358 AA; 40112 MW; 532C4DB37CEB1570 CRC64;
MITLLKGRRK VDTIKVGILG YGLSGSVFHG PLLDVLDEYQ ISKIMTSRTE EVKRDFPDAE
VVHELEEITN DPAIELVIVT TPSGLHYEHT MACIQAGKHV VMEKPMTATA EEGETLKRAA
DEKGVLLSVY HNRRWDNDFL TIKKLISEGS LEDINTYQVS YNRYRPEVQA RWREKEGTAT
GTLYDLGSHI IDQTLHLFGM PKAVTANVMA QRENAETVDY FHLTLDYGKL QAILYGGSIV
PANGPRYQIH GKDSSFIKYG IDGQEDALRA GRKPEDDSWG ADVPEFYGKL TTIRGSDKKT
ETIPSVNGSY LTYYRKIAES IREGAALPVT AEEGINVIRI IEAAMESSKE KRTIMLEH
