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Reviewed, UniProtKB/Swiss-Prot P46364 (XYLB_ACIGB)

Last modified November 4, 2008. Version 41. 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:
    Aryl-alcohol dehydrogenase
    EC=1.1.1.90
Alternative name(s):
    Benzyl alcohol dehydrogenase
      Short name=BADH
OrganismAcinetobacter genomosp. 11
Taxonomic identifier106649 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length42 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Oxidizes primary alcohols with an aromatic or cyclohex-1-ene ring. It is highly specific for benzyl alcohol.

Catalytic activity

An aromatic alcohol + NAD(+) = an aromatic aldehyde + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›42›42Aryl-alcohol dehydrogenase
PRO_0000160828

Experimental info

Non-terminal residue421

Sequences

Sequence LengthMass (Da)Tools
P46364-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 65615B99D4468ACF

FASTA424,508
        10         20         30         40 
SELKDIIAAV TPCKGADFEL QALKIRQPQG DEVLVKXXAT GM 

« Hide

References

[1]"Comparison of benzyl alcohol dehydrogenases and benzaldehyde dehydrogenases from the benzyl alcohol and mandelate pathways in Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid compositions and immunological cross-reactions."
Chalmers R.M., Keen J.N., Fewson C.A.
Biochem. J. 273:99-107(1991) [PubMed: 1989592] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 11171 / NCIB 8250 / CIP 63.46 / B94.

Cross-references

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR002328. AlcDHase_Zn_CS.
[Graphical view]
PROSITEPS00059. ADH_ZINC. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLB_ACIGB
AccessionPrimary (citable) accession number: P46364
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 4, 2008
This is version 41 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