ID   ALKJ_PSEPU              Reviewed;         552 AA.
AC   Q9WWW2;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Alcohol dehydrogenase [acceptor];
DE            EC=1.1.99.-;
GN   Name=alkJ;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=P1;
RX   PubMed=11390693; DOI=10.1099/00221287-147-6-1621;
RA   Van Beilen J.B., Panke S., Lucchini S., Franchini A.G., Roethlisberger M.,
RA   Witholt B.;
RT   "Analysis of Pseudomonas putida alkane degradation gene clusters and
RT   flanking insertion sequences: evolution and regulation of the alk-genes.";
RL   Microbiology 147:1621-1630(2001).
CC   -!- FUNCTION: Converts aliphatic medium-chain-length alcohols into
CC       aldehydes. May be linked to the electron transfer chain.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a primary alcohol = AH2 + an aldehyde;
CC         Xref=Rhea:RHEA:14685, ChEBI:CHEBI:13193, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:17499;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AJ233397; CAB51051.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WWW2; -.
DR   SMR; Q9WWW2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047645; F:alkan-1-ol dehydrogenase (acceptor) activity; IEA:RHEA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase.
FT   CHAIN           1..552
FT                   /note="Alcohol dehydrogenase [acceptor]"
FT                   /id="PRO_0000205579"
FT   ACT_SITE        469
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         3..32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   552 AA;  60709 MW;  D8419AEEE61D74C3 CRC64;
     MYDYIIVGAG SAGCVLANRL SADPSKRVCL LEAGPRDTNP LIHMPLGIAL LSNSKKLNWA
     FQTAPQQHLN ERSLFWPRGK TLGGSSSINA MVYIRGHEED YQAWEQAGGE YWGWKRAFAL
     FKKLEHNQRF DKSNYHGTDG ELAVSDLKDL NPLSKSFVQA GMEAKISFNG DFNGAHQEGV
     GFYQVTQKHG QRWSSARAFL HDVIDRPNLD IITEAHATKV LFEDRKAVGV SYIQKNMHQQ
     VKTTDSGEVI LSLGAVNTPQ LLMLSGVGAA AELKEHGIAL VHDLPEVGKN LQDHLDITLM
     CAANSRTPIG VAFSFIPRGL VGLFSYIFKR KGFLTSNVAE SGGFVKSSPE RDRPNLQFHF
     LPTYLKDHGR KIAVGYGYTL HICDLLPKSR GRIGLKSANP MDDPLIDPNY LSDPEDIKTM
     IAGIKIGRAI FDAPSMAKHF KREIVPGPAV TSDDEIVADI RSRAETIYHP VGTCRMGKDP
     ASVVDPCLQV RGLRNIRVVD ASIMPNLVAG NTNAPTIMIA ENAAEIIVRK VDMASLDASI
     GFTRQNLEPE LL