ID A0A1K1MHB6_9FLAO Unreviewed; 353 AA.
AC A0A1K1MHB6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=long-chain-fatty-acyl-CoA reductase {ECO:0000256|ARBA:ARBA00013020};
DE EC=1.2.1.50 {ECO:0000256|ARBA:ARBA00013020};
GN ORFNames=SAMN05660313_00626 {ECO:0000313|EMBL:SFW22535.1};
OS Cellulophaga fucicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=76595 {ECO:0000313|EMBL:SFW22535.1, ECO:0000313|Proteomes:UP000183257};
RN [1] {ECO:0000313|EMBL:SFW22535.1, ECO:0000313|Proteomes:UP000183257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24786 {ECO:0000313|EMBL:SFW22535.1,
RC ECO:0000313|Proteomes:UP000183257};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: LuxC is the fatty acid reductase enzyme responsible for
CC synthesis of the aldehyde substrate for the luminescent reaction
CC catalyzed by luciferase. {ECO:0000256|ARBA:ARBA00003277}.
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|ARBA:ARBA00000747};
CC -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC {ECO:0000256|ARBA:ARBA00004908}.
CC -!- SIMILARITY: Belongs to the LuxC family.
CC {ECO:0000256|ARBA:ARBA00010915}.
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DR EMBL; FPIY01000001; SFW22535.1; -; Genomic_DNA.
DR RefSeq; WP_072302291.1; NZ_FPIY01000001.1.
DR AlphaFoldDB; A0A1K1MHB6; -.
DR STRING; 76595.SAMN05660313_00626; -.
DR OrthoDB; 1522941at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000183257; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR008670; CoA_reduct_LuxC.
DR Pfam; PF05893; LuxC; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 353 AA; 40560 MW; 3F0A20B224061950 CRC64;
MAKLEDRIVA FSKLGTLFAD YYEYASSEKQ IETKNKWVSK LHDAVHTASL HNGWFTEENI
LFCLQSWSKL LTQKELNNWF RKYNLNTLKN KRVAIIMAGN IPLVGFHDFL ATILTGNTTL
IKLSSNDKIL LPFVSSFLIE QLPSLADSVV YIEGRLDNFD AVIATGSNNT ARYFEHYFGK
KPNIIRKSRN SVAVLTGSES KEQLENLSED VFRYYGLGCR SVSKLFVPKG YDFDSFFKAM
YPKQDIIHHV KYANNYDYNK AVYLMSEFKI LENGFLMIKE DPSYASPISS VFYEYYDTIE
ELKEKLNTDK EKIQCIVSNG LLDNEVDFGQ TQLPSLTDYA DNVDTVEFLL KTS
//
