Skip Header

Contribute Send feedback
Read comments (?) or add your own

P42328 (ADH3_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

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

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase
EC=1.1.1.1
Alternative name(s):
ADH-HT
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thermophilic NAD+-dependent alcohol dehydrogenase. Bears mainly an ethanol-dehydrogenase activity.

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Temperature dependence:

Thermostable.

Ontologies

Keywords
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Alcohol dehydrogenase
PRO_0000160738

Regions

Nucleotide binding172 – 1776NAD By similarity
Nucleotide binding260 – 2623NAD By similarity

Sites

Metal binding381Zinc 1; catalytic By similarity
Metal binding611Zinc 1; catalytic By similarity
Metal binding921Zinc 2 By similarity
Metal binding951Zinc 2 By similarity
Metal binding981Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1481Zinc 1; catalytic By similarity
Binding site1951NAD By similarity
Binding site2001NAD By similarity
Binding site3311NAD By similarity

Secondary structure

1 ................................................................ 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42328 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: AED17E4A34163430

FASTA33936,338
        10         20         30         40         50         60 
MKAAVVEQFK EPLKIKEVEK PTISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG 

        70         80         90        100        110        120 
HEGVGIVEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCEHQK NAGYSVDGGY 

       130        140        150        160        170        180 
AEYCRAAADY VVKIPDNLSF EEAAPIFCAG VTTYKALKVT GAKPGEWVAI YGIGGLGHVA 

       190        200        210        220        230        240 
VQYAKAMGLN VVAVDIGDEK LELAKELGAD LVVNPLKEDA AKFMKEKVGG VHAAVVTAVS 

       250        260        270        280        290        300 
KPAFQSAYNS IRRGGACVLV GLPPEEMPIP IFDTVLNGIK IIGSIVGTRK DLQEALQFAA 

       310        320        330 
EGKVKTIIEV QPLEKINEVF DRMLKGQING RVVLTLEDK

« Hide

References

[1]"A few amino acid substitutions are responsible for the higher thermostability of a novel NAD(+)-dependent bacillar alcohol dehydrogenase."
Cannio R., Rossi M., Bartolucci S.
Eur. J. Biochem. 222:345-352(1994) [PubMed: 8020473] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCIMB 12403 / LLD-R.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z27089 Genomic DNA. Translation: CAA81612.1.
PIRS45605.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RJWX-ray2.35A/B/C/D1-339[»]
3PIIX-ray2.90A/B/C/D1-339[»]
ProteinModelPortalP42328.
SMRP42328. Positions 1-339.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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 nameADH3_GEOSE
AccessionPrimary (citable) accession number: P42328
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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