IOLS_BACSU
ID IOLS_BACSU Reviewed; 310 AA.
AC P46336;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Aldo-keto reductase IolS {ECO:0000303|PubMed:12554958};
DE EC=1.1.1.- {ECO:0000269|PubMed:12554958, ECO:0000269|PubMed:15019785};
DE AltName: Full=AKR11A {ECO:0000303|PubMed:12554958};
DE AltName: Full=Vegetative protein 147 {ECO:0000303|PubMed:9298659};
DE Short=VEG147 {ECO:0000303|PubMed:9298659};
GN Name=iolS {ECO:0000303|PubMed:9226270}; Synonyms=yxbF;
GN OrderedLocusNames=BSU39780; ORFNames=SS92ER;
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 / BGSC1A1;
RX PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT between the gnt and iol operons.";
RL DNA Res. 2:61-69(1995).
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 PROTEIN SEQUENCE OF 1-20.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=168 / BGSC1A1;
RX PubMed=9226270; DOI=10.1128/jb.179.14.4591-4598.1997;
RA Yoshida K.I., Aoyama D., Ishio I., Shibayama T., Fujita Y.;
RT "Organization and transcription of the myo-inositol operon, iol, of
RT Bacillus subtilis.";
RL J. Bacteriol. 179:4591-4598(1997).
RN [5]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=11160890; DOI=10.1093/nar/29.3.683;
RA Yoshida K., Kobayashi K., Miwa Y., Kang C.-M., Matsunaga M., Yamaguchi H.,
RA Tojo S., Yamamoto M., Nishi R., Ogasawara N., Nakayama T., Fujita Y.;
RT "Combined transcriptome and proteome analysis as a powerful approach to
RT study genes under glucose repression in Bacillus subtilis.";
RL Nucleic Acids Res. 29:683-692(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=12554958; DOI=10.1107/s0907444902072001;
RA Ehrensberger A., Wilson D.K.;
RT "Expression, crystallization and activities of the two family 11 aldo-keto
RT reductases from Bacillus subtilis.";
RL Acta Crystallogr. D 59:375-377(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP NADP, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=15019785; DOI=10.1016/j.jmb.2004.01.059;
RA Ehrensberger A.H., Wilson D.K.;
RT "Structural and catalytic diversity in the two family 11 aldo-keto
RT reductases.";
RL J. Mol. Biol. 337:661-673(2004).
CC -!- FUNCTION: In vitro, is able to reduce the standard aldo-keto reductase
CC (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in
CC the presence of NADPH, albeit with poor efficiency. Shows only trace
CC activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo-
CC inositol with either NADP(+) or NAD(+) as a cosubstrate and also does
CC not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and
CC succinyl semialdehyde as a substrate (PubMed:12554958,
CC PubMed:15019785). The physiological function of this enzyme is not
CC clear (PubMed:15019785). Does not seem to be necessary for inositol
CC catabolism (PubMed:9226270). {ECO:0000269|PubMed:12554958,
CC ECO:0000269|PubMed:15019785, ECO:0000269|PubMed:9226270}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=271 mM for DL-glyceraldehyde {ECO:0000269|PubMed:15019785};
CC KM=207 mM for D-erythrose {ECO:0000269|PubMed:15019785};
CC Note=kcat is 2.07 sec(-1) with DL-glyceraldehyde as substrate. kcat
CC is 2.97 sec(-1) with D-erythrose as substrate.
CC {ECO:0000269|PubMed:15019785};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12554958}.
CC -!- INDUCTION: Induced by inositol (PubMed:9226270). Repressed by glucose
CC (PubMed:11160890). Is cotranscribed with iolR, the repressor of the iol
CC operon (PubMed:9226270). {ECO:0000269|PubMed:11160890,
CC ECO:0000269|PubMed:9226270}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene affects neither growth on
CC inositol nor the inducibility and catabolite repression of Idh
CC synthesis. {ECO:0000269|PubMed:9226270}.
CC -!- MISCELLANEOUS: The 3D-structure shows a unique architecture for an AKR
CC active site, which may explain the low catalytic power.
CC {ECO:0000305|PubMed:15019785}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 11 subfamily. {ECO:0000305|PubMed:12554958}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB005554; BAA21607.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16014.1; -; Genomic_DNA.
DR PIR; D69646; D69646.
DR RefSeq; NP_391857.1; NC_000964.3.
DR RefSeq; WP_003243075.1; NZ_JNCM01000034.1.
DR PDB; 1PYF; X-ray; 1.80 A; A=1-310.
DR PDB; 1PZ0; X-ray; 2.35 A; A=1-310.
DR PDBsum; 1PYF; -.
DR PDBsum; 1PZ0; -.
DR AlphaFoldDB; P46336; -.
DR SMR; P46336; -.
DR STRING; 224308.BSU39780; -.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR jPOST; P46336; -.
DR PaxDb; P46336; -.
DR PRIDE; P46336; -.
DR EnsemblBacteria; CAB16014; CAB16014; BSU_39780.
DR GeneID; 937636; -.
DR KEGG; bsu:BSU39780; -.
DR PATRIC; fig|224308.179.peg.4303; -.
DR eggNOG; COG0667; Bacteria.
DR InParanoid; P46336; -.
DR OMA; PPYSLFW; -.
DR PhylomeDB; P46336; -.
DR BioCyc; BSUB:BSU39780-MON; -.
DR SABIO-RK; P46336; -.
DR EvolutionaryTrace; P46336; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..310
FT /note="Aldo-keto reductase IolS"
FT /id="PRO_0000070382"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15019785"
FT BINDING 155..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785"
FT BINDING 203..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15019785"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000305|PubMed:15019785"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1PZ0"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1PYF"
FT TURN 56..61
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1PYF"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1PYF"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1PYF"
FT TURN 205..209
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1PYF"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:1PYF"
SQ SEQUENCE 310 AA; 35168 MW; A870F226F8684867 CRC64;
MKKAKLGKSD LQVFPIGLGT NAVGGHNLYP NLNEETGKEL VREAIRNGVT MLDTAYIYGI
GRSEELIGEV LREFNREDVV IATKAAHRKQ GNDFVFDNSP DFLKKSVDES LKRLNTDYID
LFYIHFPDEH TPKDEAVNAL NEMKKAGKIR SIGVSNFSLE QLKEANKDGL VDVLQGEYNL
LNREAEKTFF PYTKEHNISF IPYFPLVSGL LAGKYTEDTT FPEGDLRNEQ EHFKGERFKE
NIRKVNKLAP IAEKHNVDIP HIVLAWYLAR PEIDILIPGA KRADQLIDNI KTADVTLSQE
DISFIDKLFA
