ID A0A1H6ESC9_9ACTN Unreviewed; 408 AA.
AC A0A1H6ESC9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05444920_113210 {ECO:0000313|EMBL:SEG99614.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEG99614.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEG99614.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEG99614.1,
RC ECO:0000313|Proteomes:UP000236732};
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; FNVT01000013; SEG99614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ESC9; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000236732; 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:UP000236732}.
SQ SEQUENCE 408 AA; 44094 MW; 6B47BB478AFEE7FE CRC64;
MLDVRFPAAG SMSAEALLRQ VRGAVLDGDG GLEVGDERVR AFLSSFGKRL LRPVLARRHP
ELGSLGFFLR PSELARTVAS LGREHVRVPR GLIFHIPPAN VDTVFVYSWA LSALMGNRNV
VRLSPRSGPV AEVIVETLHE ALAEADPAVA ATQRIVSYDR SDAVTAALSA ACDLRVVWGG
DRTVREIRLQ PLPPHARDLV FPDRSSFAVV RAAAWLCAPR AARVTVAEGF VNDTYWFDQA
ACSSPRTVFW VGAEGDCEAA RTDFIDHLSR VLTVRGWGVD AAMAVEKRVS TYGLAADGLA
ESVEFRGNAL ASVRLAAATA APRRWLGAGT FAHARLAALG ELVGLVERRD QTMTHFGFGG
DELEELARGL GGRGVDRMVP VGSALSFHRV WDGVDLPAEF TRLVTVIR
//
