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Reviewed, UniProtKB/Swiss-Prot Q9Z9U1 (DHSO_BACHD)

Last modified November 3, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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: BH0189
OrganismBacillus halodurans [Complete proteome] [HAMAP]
Taxonomic identifier86665 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Reduces glucitol to fructose By similarity.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Sorbitol dehydrogenase
PRO_0000160824

Sites

Metal binding391Zinc 1; catalytic By similarity
Metal binding601Zinc 1; catalytic By similarity
Metal binding911Zinc 2 By similarity
Metal binding941Zinc 2 By similarity
Metal binding971Zinc 2 By similarity
Metal binding1051Zinc 2 By similarity
Metal binding1461Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z9U1-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 20961F7C34676DFA

FASTA34336,889
        10         20         30         40         50         60 
MKALVKTQHG TGHFAVQEKP EPTPGKHQVK IKVKYTGVCG SDIHTYEGHY PVAAPVTLGH 

        70         80         90        100        110        120 
EFSGEIVELG EGVTGFNVGD RVTSETTYSI CGKCSYCTSG DYNLCSHRKG LGNQQDGSFA 

       130        140        150        160        170        180 
KYVIARQESL HHLPAGVDDR SAAMTEPLAC THHAIAKTSI NKGDLVVVTG PGPIGLLAAQ 

       190        200        210        220        230        240 
VAKSHGGTVI ITGLSNDQVR LKKAKEVGID YAIDTQEVDI KELVSELTDG YGADVVLECS 

       250        260        270        280        290        300 
GAVPAAKQGI DLLRKKGQYA QVGLFAQPEI QFNFEKIIQK EISVVGSRSQ KPADWEPALS 

       310        320        330        340 
LLNEKKVNAK TLVTHEYTIS EWDKAYHAIK SGEAIKVLLT PID 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of three lambda clones from the genome of alkaliphilic Bacillus sp. strain C-125."
Takami H., Nakasone K., Ogasawara N., Hirama C., Nakamura Y., Masui N., Fuji F., Takaki Y., Inoue A., Horikoshi K.
Extremophiles 3:29-34(1999) [PubMed: 10086842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.
[2]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases

AB011837 Genomic DNA. Translation: BAA75341.1.
BA000004 Genomic DNA. Translation: BAB03908.1.
PIRE83673.
RefSeqNP_241055.1.

3D structure databases

HSSPHSSP built from PDB template 1JVB based on UniProtKB P39462.
ModBaseSearch...

Genome annotation databases

GeneID891766.
GenomeReviewsGene locus BH0189 in contig BA000004_GR.
KEGGbha:BH0189.
NMPDRfig|272558.1.peg.189.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9Z9U1.
OMATEPLACT.

Enzyme and pathway databases

BioCycBHAL272558:BH0189-MON.
BRENDA1.1.1.14. 191865.

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]
ProDomPD040557. GroES_related. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHSO_BACHD
AccessionPrimary (citable) accession number: Q9Z9U1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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