ID   XYLB_ACIGI              Reviewed;          42 AA.
AC   P46364;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   23-FEB-2022, entry version 61.
DE   RecName: Full=Aryl-alcohol dehydrogenase;
DE            EC=1.1.1.90;
DE   AltName: Full=Benzyl alcohol dehydrogenase;
DE            Short=BADH;
DE   Flags: Fragment;
OS   Acinetobacter guillouiae (Acinetobacter genomosp. 11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=106649;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 11171 / DSM 590 / CCUG 2491 / LMG 988 / NCIMB 8250 / CIP 63.46
RC   / B94;
RX   PubMed=1989592; DOI=10.1042/bj2730099;
RA   Chalmers R.M., Keen J.N., Fewson C.A.;
RT   "Comparison of benzyl alcohol dehydrogenases and benzaldehyde
RT   dehydrogenases from the benzyl alcohol and mandelate pathways in
RT   Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene
RT   pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid
RT   compositions and immunological cross-reactions.";
RL   Biochem. J. 273:99-107(1991).
CC   -!- FUNCTION: Oxidizes primary alcohols with an aromatic or cyclohex-1-ene
CC       ring. It is highly specific for benzyl alcohol.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aromatic primary alcohol + NAD(+) = an aromatic aldehyde +
CC         H(+) + NADH; Xref=Rhea:RHEA:12076, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33855, ChEBI:CHEBI:33857, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.90;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   STRING; 106649.GCA_000829655_00508; -.
DR   GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011032; GroES-like_sf.
DR   SUPFAM; SSF50129; SSF50129; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Metal-binding;
KW   NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..>42
FT                   /note="Aryl-alcohol dehydrogenase"
FT                   /id="PRO_0000160828"
FT   NON_TER         42
SQ   SEQUENCE   42 AA;  4508 MW;  65615B99D4468ACF CRC64;
     SELKDIIAAV TPCKGADFEL QALKIRQPQG DEVLVKXXAT GM