ID A0A1G9ILK6_9ACTN Unreviewed; 442 AA.
AC A0A1G9ILK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05421874_118104 {ECO:0000313|EMBL:SDL26148.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDL26148.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDL26148.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDL26148.1,
RC ECO:0000313|Proteomes:UP000198683};
RA de Groot N.N.;
RL Submitted (OCT-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; FNFB01000018; SDL26148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9ILK6; -.
DR STRING; 683260.SAMN05421874_118104; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000198683; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198683}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 48382 MW; 4A1386B46ABDDF9B CRC64;
MPHDATTHDA TGQDATTHSN TTHSKTTHDV TRHDSAFLDD AMLDVRFPAD GRVPVAELLS
RVRGSLEVGD ERVRDFLTAF GRRLLRPALA RRHPELGSLG FFLRPSELAR TVESLDREHV
RVPRGLVLHI PPANVDTVFV YSWALSALMG NRNVVRLSPR SGAVSEVIVR TLRETLGDAD
PVVAASQAIV SYERSDAVTS ALSAACDLRV VWGGDRTVTE IRRHPLAPHA RELTFPDRSS
FAVVRAAAWL CAPRPARVTT AEGFVNDTYW FDQAACSSPR TVFWVGDERD CESARADFTD
HVERAVTARG WGVDAAMAVE KRVSTYGLAA DGLAESVEFR GNALANVRLS AAAAAPRRWL
GAGTFAHARL ATLAELAPLV ERRDQTMTHF GFGREELEEL ARGLAGRGVD RMVPVGSALS
FHRVWDGVDL PAEFTRLVTV VR
//
