ID A0A162P3I0_9FLAO Unreviewed; 352 AA.
AC A0A162P3I0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=FBFR_11975 {ECO:0000313|EMBL:OAB27250.1};
OS Flavobacterium fryxellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB27250.1, ECO:0000313|Proteomes:UP000077164};
RN [1] {ECO:0000313|EMBL:OAB27250.1, ECO:0000313|Proteomes:UP000077164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB27250.1,
RC ECO:0000313|Proteomes:UP000077164};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL Submitted (MAR-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}.
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:OAB27250.1}.
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DR EMBL; LVJE01000019; OAB27250.1; -; Genomic_DNA.
DR RefSeq; WP_066081640.1; NZ_LVJE01000019.1.
DR AlphaFoldDB; A0A162P3I0; -.
DR STRING; 249352.SAMN05444395_104106; -.
DR OrthoDB; 1522941at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000077164; 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:UniProtKB-KW.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
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 352 AA; 39817 MW; F3EB10A1323C741A CRC64;
MTLETKKSVF VELGKFLGQF SKDNTVKNPA VLHNETFFDA FIALINLSQS HNGWYTADNV
YFSIHSWAEA LTEENLTQWL SDYDLQNKKS KNIALILAGN IPLVGFHDFL SVLITGNNVV
VKTSSNDQHL LPFLAKYMIA ADPELGNSIN FVTGKLENFD AVIATGSNNT ARYFEYYFKD
KPSIIRKSRN SVAVLTGDET GEELSALGED IFRYFGLGCR NVSKLFVPVG YSFVAFFEAI
FEYQDVIHYE KYANNYDYNK AVFLMSNFKL LDNGFLTLKE DKSHASPISS VFYETYDNID
ALKTRLQSES EHIQCIVSDS SIENSIGFGQ TQKPKLWNYA DNIDTISFLL TT
//
