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 16-JUN-2009, entry version 74. DE RecName: Full=Sorbitol dehydrogenase; DE EC=1.1.1.14; DE AltName: Full=L-iditol 2-dehydrogenase; DE AltName: Full=Glucitol dehydrogenase; GN Name=gutB; OrderedLocusNames=BSU06150; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-32. RC STRAIN=168; RX MEDLINE=93094198; PubMed=1460002; 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 MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 MEDLINE=94253000; PubMed=8195086; RA Ye R., Wong S.-L.; RT "Transcriptional regulation of the Bacillus subtilis glucitol RT dehydrogenase gene."; RL J. Bacteriol. 176:3314-3320(1994). CC -!- FUNCTION: Reduces glucitol to fructose. CC -!- CATALYTIC ACTIVITY: L-iditol + NAD(+) = L-sorbose + NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; -. DR HSSP; O96496; 1E3J. DR GeneID; 939495; -. DR GenomeReviews; AL009126_GR; BSU06150. DR KEGG; bsu:BSU06150; -. DR NMPDR; fig|224308.1.peg.615; -. DR SubtiList; BG10177; gutB. DR HOGENOM; Q06004; -. DR OMA; Q06004; GHECAGE. DR BioCyc; BSUB224308:BSU0615-MON; -. DR BRENDA; 1.1.1.14; 150. DR GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR002328; ADH_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Metal-binding; NAD; KW Oxidoreductase; Zinc. FT INIT_MET 1 1 Removed. FT CHAIN 2 353 Sorbitol dehydrogenase. FT /FTId=PRO_0000160825. FT METAL 45 45 Zinc 1; catalytic (By similarity). FT METAL 70 70 Zinc 1; catalytic (By similarity). FT METAL 100 100 Zinc 2 (By similarity). FT METAL 103 103 Zinc 2 (By similarity). FT METAL 106 106 Zinc 2 (By similarity). FT METAL 114 114 Zinc 2 (By similarity). FT METAL 156 156 Zinc 1; catalytic (By similarity). 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 //