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Reviewed, UniProtKB/Swiss-Prot Q06004 (DHSO_BACSU)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Sorbitol dehydrogenase
    EC=1.1.1.14
Alternative name(s):
    L-iditol 2-dehydrogenase
    Glucitol dehydrogenase
Gene names
Name: gutB
Ordered Locus Names: BSU06150
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Reduces glucitol to fructose.

Catalytic activity

L-iditol + NAD+ = L-sorbose + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionL-iditol 2-dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 353352Sorbitol dehydrogenase
PRO_0000160825

Sites

Metal binding451Zinc 1; catalytic By similarity
Metal binding701Zinc 1; catalytic By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1561Zinc 1; catalytic By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q06004-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C87DD26E6DCA74C4

FASTA35338,390
        10         20         30         40         50         60 
MTHTVPQNMK AAVMHNTREI KIETLPVPDI NHDEVLIKVM AVGICGSDLH YYTNGRIGNY 

        70         80         90        100        110        120 
VVEKPFILGH ECAGEIAAVG SSVDQFKVGD RVAVEPGVTC GRCEACKEGR YNLCPDVQFL 

       130        140        150        160        170        180 
ATPPVDGAFV QYIKMRQDFV FLIPDSLSYE EAALIEPFSV GIHAAARTKL QPGSTIAIMG 

       190        200        210        220        230        240 
MGPVGLMAVA AAKAFGAGTI IVTDLEPLRL EAAKKMGATH IINIREQDAL EEIKTITNDR 

       250        260        270        280        290        300 
GVDVAWETAG NPAALQSALA SVRRGGKLAI VGLPSQNEIP LNVPFIADNE IDIYGIFRYA 

       310        320        330        340        350 
NTYPKGIEFL ASGIVDTKHL VTDQYSLEQT QDAMERALQF KNECLKVMVY PNR

« Hide

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References

« Hide 'large scale' references
[1]"Sorbitol dehydrogenase from Bacillus subtilis. Purification, characterization, and gene cloning."
Ng K., Ye R., Wu X.-C., Wong S.-L.
J. Biol. Chem. 267:24989-24994(1992) [PubMed: 1460002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-32.
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Transcriptional regulation of the Bacillus subtilis glucitol dehydrogenase gene."
Ye R., Wong S.-L.
J. Bacteriol. 176:3314-3320(1994) [PubMed: 8195086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
Strain: 168.

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Cross-references

Sequence databases

M96947 Genomic DNA. Translation: AAA22508.1.
AL009126 Genomic DNA. Translation: CAB12434.1.
L16626 Genomic DNA. Translation: AAA20875.1.
PIRA45052.
RefSeqNP_388496.1.

3D structure databases

HSSPHSSP built from PDB template 1E3J based on UniProtKB O96496.
ModBaseSearch...

Genome annotation databases

GeneID939495.
GenomeReviewsGene locus BSU06150 in contig AL009126_GR.
KEGGbsu:BSU06150.
NMPDRfig|224308.1.peg.615.

Organism-specific databases

SubtiListBG10177. gutB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMQ06004.
OMAQ06004. GHECAGE.

Enzyme and pathway databases

BioCycBSUB224308:BSU0615-MON.
BRENDA1.1.1.14. 150.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDHSO_BACSU
AccessionPrimary (citable) accession number: Q06004
Secondary accession number(s): Q45615
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents