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Q06004 (DHSO_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

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

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.

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

Sequences

Sequence LengthMass (Da)Tools
Q06004 [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

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M96947 Genomic DNA. Translation: AAA22508.1.
AL009126 Genomic DNA. Translation: CAB12434.1.
L16626 Genomic DNA. Translation: AAA20875.1.
PIRA45052.
RefSeqNP_388496.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ06004.
SMRQ06004. Positions 7-353.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003937; EBBACP00000003937; EBBACG00000003929.
GeneID939495.
GenomeReviewsGene locus BSU06150 in contig AL009126_GR.
KEGGbsu:BSU06150.
NMPDRfig|224308.1.peg.615.
PATRIC18972866. VBIBacSub10457_0647.

Organism-specific databases

GenoListBSU06150. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000383.
HOGENOMHBG753318.
OMAKTVFRYR.
PhylomeDBQ06004.
ProtClustDBCLSK886804.

Enzyme and pathway databases

BioCycBSUB:BSU06150-MONOMER.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00008.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents