DHSO_BACSU
ID DHSO_BACSU Reviewed; 353 AA.
AC Q06004; Q45615;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sorbitol dehydrogenase {ECO:0000303|PubMed:1460002};
DE Short=SDH {ECO:0000303|PubMed:1460002};
DE EC=1.1.1.- {ECO:0000269|PubMed:1460002};
DE AltName: Full=Glucitol dehydrogenase {ECO:0000303|PubMed:8195086};
DE AltName: Full=L-iditol 2-dehydrogenase {ECO:0000305|PubMed:1460002};
DE EC=1.1.1.14 {ECO:0000269|PubMed:1460002};
DE AltName: Full=Polyol dehydrogenase {ECO:0000305};
DE AltName: Full=Xylitol dehydrogenase {ECO:0000305|PubMed:1460002};
DE EC=1.1.1.9 {ECO:0000269|PubMed:1460002};
GN Name=gutB {ECO:0000303|PubMed:1460002}; OrderedLocusNames=BSU06150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-32, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND COFACTOR.
RC STRAIN=168;
RX PubMed=1460002; DOI=10.1016/s0021-9258(19)73995-7;
RA Ng K., Ye R., Wu X.-C., Wong S.-L.;
RT "Sorbitol dehydrogenase from Bacillus subtilis. Purification,
RT characterization, and gene cloning.";
RL J. Biol. Chem. 267:24989-24994(1992).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC STRAIN=168;
RX PubMed=8195086; DOI=10.1128/jb.176.11.3314-3320.1994;
RA Ye R., Wong S.-L.;
RT "Transcriptional regulation of the Bacillus subtilis glucitol dehydrogenase
RT gene.";
RL J. Bacteriol. 176:3314-3320(1994).
CC -!- FUNCTION: Polyol dehydrogenase that catalyzes the NAD(+)-dependent
CC oxidation of various sugar alcohols. Is mostly active with D-sorbitol
CC (D-glucitol), xylitol and L-iditol as substrates, leading to the C2-
CC oxidized products D-fructose, D-xylulose and L-sorbose, respectively.
CC {ECO:0000269|PubMed:1460002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + keto-D-fructose + NADH = D-sorbitol + NAD(+);
CC Xref=Rhea:RHEA:33031, ChEBI:CHEBI:15378, ChEBI:CHEBI:17924,
CC ChEBI:CHEBI:48095, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:1460002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + xylitol = D-xylulose + H(+) + NADH;
CC Xref=Rhea:RHEA:20433, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:17151, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.9;
CC Evidence={ECO:0000269|PubMed:1460002};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-iditol + NAD(+) = H(+) + keto-L-sorbose + NADH;
CC Xref=Rhea:RHEA:10160, ChEBI:CHEBI:13172, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18202, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.14;
CC Evidence={ECO:0000269|PubMed:1460002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1460002};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:1460002};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 mM for D-sorbitol {ECO:0000269|PubMed:1460002};
CC KM=14 mM for xylitol {ECO:0000269|PubMed:1460002};
CC KM=18 mM for L-iditol {ECO:0000269|PubMed:1460002};
CC KM=125 mM for ribitol {ECO:0000269|PubMed:1460002};
CC KM=500 mM for galactitol {ECO:0000269|PubMed:1460002};
CC KM=555 mM for D-mannitol {ECO:0000269|PubMed:1460002};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1460002}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M96947; AAA22508.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12434.1; -; Genomic_DNA.
DR EMBL; L16626; AAA20875.1; -; Genomic_DNA.
DR PIR; A45052; A45052.
DR RefSeq; NP_388496.1; NC_000964.3.
DR RefSeq; WP_003244156.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; Q06004; -.
DR SMR; Q06004; -.
DR STRING; 224308.BSU06150; -.
DR jPOST; Q06004; -.
DR PaxDb; Q06004; -.
DR PRIDE; Q06004; -.
DR EnsemblBacteria; CAB12434; CAB12434; BSU_06150.
DR GeneID; 939495; -.
DR KEGG; bsu:BSU06150; -.
DR PATRIC; fig|224308.179.peg.666; -.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; Q06004; -.
DR OMA; QFGVADY; -.
DR PhylomeDB; Q06004; -.
DR BioCyc; BSUB:BSU06150-MON; -.
DR BioCyc; MetaCyc:BSU06150-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046526; F:D-xylulose reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05285; sorbitol_DH; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR045306; SDH-like.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1460002"
FT CHAIN 2..353
FT /note="Sorbitol dehydrogenase"
FT /id="PRO_0000160825"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 296..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q00796"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07846"
SQ SEQUENCE 353 AA; 38390 MW; C87DD26E6DCA74C4 CRC64;
MTHTVPQNMK AAVMHNTREI KIETLPVPDI NHDEVLIKVM AVGICGSDLH YYTNGRIGNY
VVEKPFILGH ECAGEIAAVG SSVDQFKVGD RVAVEPGVTC GRCEACKEGR YNLCPDVQFL
ATPPVDGAFV QYIKMRQDFV FLIPDSLSYE EAALIEPFSV GIHAAARTKL QPGSTIAIMG
MGPVGLMAVA AAKAFGAGTI IVTDLEPLRL EAAKKMGATH IINIREQDAL EEIKTITNDR
GVDVAWETAG NPAALQSALA SVRRGGKLAI VGLPSQNEIP LNVPFIADNE IDIYGIFRYA
NTYPKGIEFL ASGIVDTKHL VTDQYSLEQT QDAMERALQF KNECLKVMVY PNR
