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Database: UniProt
Entry: C5E9G4_BIFLI
LinkDB: C5E9G4_BIFLI
Original site: C5E9G4_BIFLI 
ID   C5E9G4_BIFLI            Unreviewed;       499 AA.
AC   C5E9G4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=BLIG_00524 {ECO:0000313|EMBL:EEQ54573.1};
OS   Bifidobacterium longum subsp. infantis CCUG 52486.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=537937 {ECO:0000313|EMBL:EEQ54573.1};
RN   [1] {ECO:0000313|EMBL:EEQ54573.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 52486 {ECO:0000313|EMBL:EEQ54573.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Gougoulias C., Tuohy K.M., Gibson G.R., Ward D., Mehta T., Young S.,
RA   Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA   Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Bifidobacterium longum subsp. infantis CCUG 52486.";
RL   Submitted (AUG-2008) 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; DS990238; EEQ54573.1; -; Genomic_DNA.
DR   RefSeq; WP_007051634.1; NZ_DS990238.1.
DR   AlphaFoldDB; C5E9G4; -.
DR   HOGENOM; CLU_043373_0_0_11; -.
DR   Proteomes; UP000005084; 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   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   499 AA;  54231 MW;  AAE3936B0FD8940B CRC64;
     MPTVDESVSQ AIDVFHLPSG VDVSDYEIYE VATSDGVKRL RYPRLDGSKV TSLAKQLVDV
     RNRTLAAMSV NDILDIVADA AQLWADPDFE LRRQAELLIP AITGYEPDMV RIELKRYMRQ
     FRRRELLRFL DSEIGQPSML DEFRPNKAGG YSKYVGPALT YQVFSSNVPG IPVWSMAMTL
     LVKGAILGKS SFSEPVMPAF FARSIAMVNS DLADAIAVVP WKGGSQQLED SAIDAADAVI
     VYGSSQTTKL IAGKVAGSKP CLGYGAKVGL AFIGREALRP DTYADTVHRV AVDIATYDQQ
     SCLAPQTVFV ETDGALTPRE VAQLLGGELE NQQRKYPRSV LSDAENVAIQ RARTDAEMRA
     LMGGKAAVFA SGHSTAWSVL YRELDGSGAD EDVASLMSPL NRTVNVVAVP DLLDAARRLT
     SCRGWLQSCG VAVDSTRLFG LAGTLAEVGV NRICPLGEMD RAKSGWHHDG GFNLIDLLRA
     VDVERGSDAY SDSFDMDME
//
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