Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P12311 (ADH1_BACST)

Last modified November 25, 2008. Version 62. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase
    EC=1.1.1.1
Alternative name(s):
    ADH-T
Gene names
Name: adhT
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Hide | Top

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

NAD(+)-dependent alcohol dehydrogenase.

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Substrate inhibition is not observed with any alcohols, and the enzyme-NADH dissociation is not considered to be a rate-limiting step.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Temperature dependence:

Thermostable.

Hide | Top

Ontologies

Keywords

   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: InterPro

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Alcohol dehydrogenase
PRO_0000160736

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

Experimental info

Mutagenesis381C → S: No activity
Mutagenesis401T → A: No activity
Mutagenesis401T → S: Little decrease in activity
Mutagenesis431H → A: No activity
Mutagenesis431H → R: Higher level of activity at pH 9
Sequence conflict221Missing AA sequence Ref.2
Sequence conflict331Missing AA sequence Ref.2
Sequence conflict52 – 532KP → PK AA sequence Ref.3

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P12311-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: B9B35A80EE9B7A86

FASTA33736,100
        10         20         30         40         50         60 
MKAAVVEQFK KPLQVKEVEK PKISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG 

        70         80         90        100        110        120 
HEGVGVIEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCERQQ NAGYSVDGGY 

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

       190        200        210        220        230        240 
VQYAKAMGLN VVAVDLGDEK LELAKQLGAD LVVNPKHDDA AQWIKEKVGG VHATVVTAVS 

       250        260        270        280        290        300 
KAAFESAYKS IRRGGACVLV GLPPEEIPIP IFDTVLNGVK IIGSIVGTRK DLQEALQFAA 

       310        320        330 
EGKVKTIVEV QPLENINDVF DRMLKGQING RVVLKVD

« Hide

Hide | Top

References

[1]"Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and rational shift of the optimum pH."
Sakoda H., Imanaka T.
J. Bacteriol. 174:1397-1402(1992) [PubMed: 1735726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]"Amino acid sequence homology in alcohol dehydrogenase."
Bridgen J., Kolb E., Harris J.I.
FEBS Lett. 33:1-3(1973) [PubMed: 4578954] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-45.
[3]"Identification of the amino acid residue modified in Bacillus stearothermophilus alcohol dehydrogenase by the NAD+ analogue 4-(3-bromoacetylpyridinio)butyldiphosphoadenosine."
Jeck R., Woenckhaus C., Harris J.I., Runswick M.J.
Eur. J. Biochem. 93:57-64(1979) [PubMed: 436831] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-54.
[4]"Gene structure and amino acid sequences of alcohol dehydrogenases of Bacillus stearothermophilus."
Robinson G.A., Bailey C.J., Dowds B.C.A.
Biochim. Biophys. Acta 1218:432-434(1994) [PubMed: 8049268] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-37; 188-197; 247-263 AND 324-336.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.

Hide | Top

Cross-references

Sequence databases

D90421 Genomic DNA. Translation: BAA14411.1.
PIRA42654.

3D structure databases

HSSPHSSP built from PDB template 1JVB based on UniProtKB P39462.
SMRP12311. Positions 1-337.
ModBaseSearch...

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR002328. AlcDHase_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...

Hide | Top

Entry information

Entry nameADH1_BACST
AccessionPrimary (citable) accession number: P12311
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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