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Database: UniProt
Entry: A0A1W6ZHJ8_9BORD
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ID   A0A1W6ZHJ8_9BORD        Unreviewed;       486 AA.
AC   A0A1W6ZHJ8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=CAL15_22115 {ECO:0000313|EMBL:ARP96821.1};
OS   Bordetella genomosp. 13.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP96821.1, ECO:0000313|Proteomes:UP000194161};
RN   [1] {ECO:0000313|EMBL:ARP96821.1, ECO:0000313|Proteomes:UP000194161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU7206 {ECO:0000313|EMBL:ARP96821.1,
RC   ECO:0000313|Proteomes:UP000194161};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty aldehyde + CoA + NADP(+) = a long-chain
CC         fatty acyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:15437,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17176, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83139; EC=1.2.1.50;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009414};
CC   -!- SIMILARITY: Belongs to the LuxC family.
CC       {ECO:0000256|PIRNR:PIRNR009414}.
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DR   EMBL; CP021111; ARP96821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6ZHJ8; -.
DR   STRING; 463040.CAL15_22115; -.
DR   KEGG; bgm:CAL15_22115; -.
DR   OrthoDB; 580775at2; -.
DR   Proteomes; UP000194161; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:InterPro.
DR   CDD; cd07080; ALDH_Acyl-CoA-Red_LuxC; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR008670; CoA_reduct_LuxC.
DR   Pfam; PF05893; LuxC; 1.
DR   PIRSF; PIRSF009414; LuxC; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRNR:PIRNR009414};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009414}.
SQ   SEQUENCE   486 AA;  52211 MW;  47D0347F75B7039E CRC64;
     MNARRIEAGY LPGLAAEEVQ WQVLPFAQDG QRLEVAVPVL SAVQMQALAE RVRRASAKHL
     QAMTVSQIID VIDRATARLL DRDDPYRQQA DALLPIVSGY DAEMVCLGLT GFLKTFRAPQ
     LHRFVAEDFP NPKVLDGFQP AAKGGAVRAY GPRLLVHSWA GNVPALALWS LVCGLLVKAG
     NVGKLPSAEP LFAGWFARLL AEVHPPLADC LAVVWWRGAG GDDAEALYAQ ADAVVAYGGN
     EALQAIQRRL PVTTRFLAHG HKLGFGVVAA QALDAARAPA LARRAAWDVA RYDQQGCYSP
     HVFYVQRGGT VSSRDFAGYL AAELANLHRR YPRRVLELEE SAAVAKWRQS IEWTLPPGAD
     DALMGEPADA WSVAYTDTPK SLAPTALQRC IVVAAVDTLD EVAPAVAGLG AYLQTAGVAA
     PPEDLYRLAG QLGAAGVTRI SALGAMSTPE AGWHHDGRFN LLDLVRMTEI ELSAEAAAEP
     LAPYEP
//
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