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Database: UniProt
Entry: U2S7V7_9ACTN
LinkDB: U2S7V7_9ACTN
Original site: U2S7V7_9ACTN 
ID   U2S7V7_9ACTN            Unreviewed;       456 AA.
AC   U2S7V7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=HMPREF0682_2267 {ECO:0000313|EMBL:ERK61733.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK61733.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK61733.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK61733.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERK61733.1}.
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DR   EMBL; ACVN02000044; ERK61733.1; -; Genomic_DNA.
DR   RefSeq; WP_021796444.1; NZ_ACVN02000044.1.
DR   AlphaFoldDB; U2S7V7; -.
DR   OrthoDB; 580775at2; -.
DR   Proteomes; UP000017052; Unassembled WGS sequence.
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   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   456 AA;  51644 MW;  FA9D1F624B8BF177 CRC64;
     MSAKEFALPI IVNGRLLYPH ELPAEEVLTL RYESGAQLSI PRFTREHLAE MRREAAEIDA
     ELAEIPVRDV ISFLGRVGDR WDRRDLEGRM IVRRHAHQVT KFSELILESD YSTIDHFLAQ
     RFHLYDQIES EFGDQRIFDE WIPVQMGYRR AFPRGLALHY LVGNLPLASC YSLIRSMVSK
     NRTIAKLPSR DPVTPIGLAM AVIEVDPAHP VSRSLSLAYW PRDDEVGLEC MIEADTACVW
     GGDAALAAVK RAISPGVPLA EYGPKWSASV IDLDQVAAQD AAMRVVDDAY FYDQEACFNT
     QRVFVKGNVQ DFLPALQESC ERFVKNVPYL SHNADIMAHR SMTLREAMFM GYQVLQGDDW
     GIVVLPLDSP LRHPLARTIF VHQVDDVADV AKCLDRRNSQ TLSVYPWSLT HEHRDAWARA
     GADRIVELGW SKQPREGFTH DGTLGGLCKT PDFNLR
//
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