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Database: UniProt
Entry: W4Q4G5_9BACI
LinkDB: W4Q4G5_9BACI
Original site: W4Q4G5_9BACI 
ID   W4Q4G5_9BACI            Unreviewed;       490 AA.
AC   W4Q4G5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Acyl-CoA reductase {ECO:0000256|PIRNR:PIRNR009414};
DE            EC=1.2.1.50 {ECO:0000256|PIRNR:PIRNR009414};
GN   ORFNames=JCM9140_3066 {ECO:0000313|EMBL:GAE26956.1};
OS   Halalkalibacter wakoensis JCM 9140.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=1236970 {ECO:0000313|EMBL:GAE26956.1, ECO:0000313|Proteomes:UP000018890};
RN   [1] {ECO:0000313|EMBL:GAE26956.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9140 {ECO:0000313|EMBL:GAE26956.1};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains, Bacillus
RT   wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
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:GAE26956.1}.
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DR   EMBL; BAUT01000036; GAE26956.1; -; Genomic_DNA.
DR   RefSeq; WP_052002263.1; NZ_BAZN01000036.1.
DR   AlphaFoldDB; W4Q4G5; -.
DR   STRING; 1236970.JCM9140_3066; -.
DR   OrthoDB; 580775at2; -.
DR   Proteomes; UP000018890; 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:UP000018890}.
SQ   SEQUENCE   490 AA;  55242 MW;  7DEB06DB16BFFC27 CRC64;
     MTFSCYHVPS ECESLISEGS FQTLEFENHG QKIKLTVPTL TVNQLDQVIH KVKRQQRDYV
     RKLQTNEIIT IFDKAVQKWL DPSYEKRQQA EELLPIITGY DREMVRLFIS RYLRQFRKEN
     LQRMIDEDFS NPLILDEFRP RKAGGLYRAF GPNVVTHIFS GNVPALPLWS LAAGILLKSA
     TIGKVSSSEP LFPVLFAKTI AEIDPALGDS LAILWWKGGE SALESTSFSA SNAVIAYGGK
     ETIEQVRQKV PTHVTFHPHG HKVSFGLITK ECLQATKSWE TAKLAASDVS WFDQQGCLSP
     HVFFVERGGT YTPSDFAQML ANEMENFERT HPRASLNNSE KQAILTQRTK VEFESYESTE
     LQLLKSENGT AWSVVYSSLK SEKKAFPISP LNRFVTVIPI NHVSEITEYL SEVKGFVQTV
     GVGCSPQAFS NIINLLGDCG VNRICALGSM PHPQPGWHHD GRFHLADLVT FCDVESTLEM
     QMDLYDVNRD
//
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