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Database: UniProt
Entry: A0A135WRB7_9BACL
LinkDB: A0A135WRB7_9BACL
Original site: A0A135WRB7_9BACL 
ID   A0A135WRB7_9BACL        Unreviewed;       483 AA.
AC   A0A135WRB7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=AU377_02475 {ECO:0000313|EMBL:KXH87457.1};
OS   Sporosarcina sp. HYO08.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1759557 {ECO:0000313|EMBL:KXH87457.1, ECO:0000313|Proteomes:UP000070230};
RN   [1] {ECO:0000313|EMBL:KXH87457.1, ECO:0000313|Proteomes:UP000070230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYO08 {ECO:0000313|EMBL:KXH87457.1,
RC   ECO:0000313|Proteomes:UP000070230};
RA   Choi I.-G., Park W.;
RT   "Draft genome sequences of microorganisms having biocementation activity.";
RL   Submitted (DEC-2015) 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:KXH87457.1}.
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DR   EMBL; LPUT01000001; KXH87457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135WRB7; -.
DR   STRING; 1759557.AU377_02475; -.
DR   OrthoDB; 580775at2; -.
DR   Proteomes; UP000070230; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070230}.
SQ   SEQUENCE   483 AA;  53850 MW;  321C44BCD276F8CE CRC64;
     MMERAGYFTG LNEEDVKYEI REFQGHGKTL QVEVPVVTTE QLLQIAEGVK TASDHILKSF
     SVSELVRIID EVIARLLDRD NLYRQKAEEL LPIITGFDEE MVRLGLTSQL KTFRKPQLQR
     FLVEDFGNPL LLDDFQPRAK GGHSKAIGPG LMTHIWAGNV PALPLWSIVS SLLVKGGSIG
     KVSSAEPLFA GWVAKMIAEV EPRLRGCLAV VWWPGGDEEK ESALFNASDL VFAYGGNEAL
     TAIKNHVPLT TKFLGHGHKI SFGLVSKESL NAKNAAETAR LAAYDVMRFD QQGCYSPQFF
     FVQSGGQVSP KSFSQYVAHE LAVFEKRFPR RALSKEEGAE LFTWRQKEQM SVFSEQGKEV
     IGPDSGSWAV VYEPLKDFVL PSPLNRVVRI IEIEDFHEIL PLLVPFRHYL QTAGIAASPE
     NLFHLSSLLA KTGVTRISSL GQMTAPEAGW HHDGAWSLLD LVQMVDIEDN AEVYAEKFAS
     YRD
//
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