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Aryl-alcohol dehydrogenase (EC 1.1.1.90) (Benzyl alcohol dehydrogenase) (BADH)

 XYLB_PSEPU              Reviewed;         366 AA.
P39849;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
22-NOV-2017, entry version 100.
RecName: Full=Aryl-alcohol dehydrogenase;
EC=1.1.1.90;
AltName: Full=Benzyl alcohol dehydrogenase;
Short=BADH;
Name=xylB;
Pseudomonas putida (Arthrobacter siderocapsulatus).
Plasmid TOL pWW0, and Plasmid TOL pWW53.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
PLASMID=TOL pWW0;
PubMed=8496150;
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; DOI=10.1042/bj2730099;
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).
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA26024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D63341; BAA09664.1; -; Genomic_DNA.
EMBL; M94184; AAA26024.1; ALT_INIT; Genomic_DNA.
PIR; A46704; A46704.
RefSeq; NP_542885.1; NC_003350.1.
RefSeq; WP_011005928.1; NC_003350.1.
ProteinModelPortal; P39849; -.
SMR; P39849; -.
GeneID; 1218744; -.
BioCyc; MetaCyc:MONOMER-2967; -.
BRENDA; 1.1.1.90; 5092.
GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
1: Evidence at protein level;
Aromatic hydrocarbons catabolism; Direct protein sequencing;
Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.
CHAIN 1 366 Aryl-alcohol dehydrogenase.
/FTId=PRO_0000160827.
METAL 40 40 Zinc 1; catalytic. {ECO:0000250}.
METAL 61 61 Zinc 1; catalytic. {ECO:0000250}.
METAL 90 90 Zinc 2. {ECO:0000250}.
METAL 93 93 Zinc 2. {ECO:0000250}.
METAL 96 96 Zinc 2. {ECO:0000250}.
METAL 104 104 Zinc 2. {ECO:0000250}.
METAL 169 169 Zinc 1; catalytic. {ECO:0000250}.
CONFLICT 40 41 CH -> PG (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 50 50 H -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 366 AA; 38510 MW; 23A5203C0F96D91B CRC64;
MEIKAAIVRQ KNGPFLLEHV ALNEPAEDQV LVRLVATGLC HTDLVCRDQH YPVPLPMVFG
HEGAGVVERV GSAVKKVQPG DHVVLTFYTC GSCDACLSGD PTSCANSFGP NFMGRSVTGE
CTIHDHQGAE VGASFFGQSS FATYALSYER NTVKVTKDVP LELLGPLGCG IQTGAGSVLN
ALNPPAGSAI AIFGAGAVGL SAVMAAVVAG CTTIIAVDVK ENRLELASEL GATHIINPAA
NDPIEAIKEI FADGVPYVLE TSGLPAVLTQ AILSSAIGGE IGIVGAPPMG ATVPVDINFL
LFNRKLRGIV EGQSISDIFI PRLVELYRQG KFPFDKLIKF YPFDEINRAA EDSEKGVTLK
PVLRIG


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