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P46364 (XYLB_ACIGB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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.
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.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaryl-alcohol dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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 [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 11171 / NCIB 8250 / CIP 63.46 / B94.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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: April 3, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families