XYLB_PSEPU
ID XYLB_PSEPU Reviewed; 366 AA.
AC P39849;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Aryl-alcohol dehydrogenase;
DE EC=1.1.1.90;
DE AltName: Full=Benzyl alcohol dehydrogenase;
DE Short=BADH;
GN Name=xylB;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid TOL pWW0, and Plasmid TOL pWW53.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
RC PLASMID=TOL pWW0;
RX PubMed=8496150; DOI=10.1016/s0021-9258(18)82062-2;
RA Shaw J.P., Rekik M., Schwager F., Harayama S.;
RT "Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid
RT pWWO. A member of the zinc-containing long chain alcohol dehydrogenase
RT family.";
RL J. Biol. Chem. 268:10842-10850(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-53.
RC PLASMID=TOL pWW53;
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.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D63341; BAA09664.1; -; Genomic_DNA.
DR EMBL; M94184; AAA26024.1; ALT_INIT; Genomic_DNA.
DR PIR; A46704; A46704.
DR RefSeq; NP_542885.1; NC_003350.1.
DR RefSeq; WP_011005928.1; NZ_QWEF01000005.1.
DR AlphaFoldDB; P39849; -.
DR SMR; P39849; -.
DR KEGG; ag:BAA09664; -.
DR BioCyc; MetaCyc:MON-2967; -.
DR BRENDA; 1.1.1.90; 5092.
DR GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Metal-binding;
KW NAD; Oxidoreductase; Plasmid; Zinc.
FT CHAIN 1..366
FT /note="Aryl-alcohol dehydrogenase"
FT /id="PRO_0000160827"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 40..41
FT /note="CH -> PG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="H -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
