NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
PLASMID=TOL pWW0;
PubMed=8496150 [NCBI, ExPASy, EBI, Israel, Japan]
Shaw J.P., Rekik M., Schwager F., Harayama S.;
"Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family.";
J. Biol. Chem. 268:10842-10850(1993).

[2]

PROTEIN SEQUENCE OF 1-53.
PLASMID=TOL pWW53;
PubMed=1989592 [NCBI, ExPASy, EBI, Israel, Japan]
Chalmers R.M., Keen J.N., Fewson C.A.;
"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.";
Biochem. J. 273:99-107(1991).

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: Homodimer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D63341; BAA09664.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M94184; AAA26024.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A46704; A46704.

RefSeq

NP_542885.1; -.

3D structure databases

HSSP

P00325; 1DEH. [HSSP ENTRY / PDB]

ModBase

P39849.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-2947; -.
MetaCyc:MON-2967; -.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

BLOCKS

P39849.

Genome annotation databases

GeneID

1218744; -.

Other

ProtoNet

P39849.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 366`	`366`	`Aryl-alcohol dehydrogenase.`	`PRO_0000160827`
`METAL`	`40 40`		`Zinc 1; catalytic (By similarity).`
`METAL`	`61 61`		`Zinc 1; catalytic (By similarity).`
`METAL`	`90 90`		`Zinc 2 (By similarity).`
`METAL`	`93 93`		`Zinc 2 (By similarity).`
`METAL`	`96 96`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 2 (By similarity).`
`METAL`	`169 169`		`Zinc 1; catalytic (By similarity).`
`CONFLICT`	`40 41`		`CH -> PG (in Ref. 2; AA sequence).`
`CONFLICT`	`50 50`		`H -> G (in Ref. 2; AA sequence).`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 38510 Da [This is the MW of the unprocessed precursor]

CRC64: 23A5203C0F96D91B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEIKAAIVRQ KNGPFLLEHV ALNEPAEDQV LVRLVATGLC HTDLVCRDQH YPVPLPMVFG 

        70         80         90        100        110        120 
HEGAGVVERV GSAVKKVQPG DHVVLTFYTC GSCDACLSGD PTSCANSFGP NFMGRSVTGE 

       130        140        150        160        170        180 
CTIHDHQGAE VGASFFGQSS FATYALSYER NTVKVTKDVP LELLGPLGCG IQTGAGSVLN 

       190        200        210        220        230        240 
ALNPPAGSAI AIFGAGAVGL SAVMAAVVAG CTTIIAVDVK ENRLELASEL GATHIINPAA 

       250        260        270        280        290        300 
NDPIEAIKEI FADGVPYVLE TSGLPAVLTQ AILSSAIGGE IGIVGAPPMG ATVPVDINFL 

       310        320        330        340        350        360 
LFNRKLRGIV EGQSISDIFI PRLVELYRQG KFPFDKLIKF YPFDEINRAA EDSEKGVTLK 


PVLRIG

P39849 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools