ID A0A3R9W923_9ACTN Unreviewed; 720 AA.
AC A0A3R9W923;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE RecName: Full=long-chain-fatty-acyl-CoA reductase {ECO:0000256|ARBA:ARBA00013020};
DE EC=1.2.1.50 {ECO:0000256|ARBA:ARBA00013020};
DE Flags: Fragment;
GN ORFNames=EF918_23070 {ECO:0000313|EMBL:RSS76748.1};
OS Streptomyces sp. WAC06614.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS76748.1, ECO:0000313|Proteomes:UP000277644};
RN [1] {ECO:0000313|EMBL:RSS76748.1, ECO:0000313|Proteomes:UP000277644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC06614 {ECO:0000313|EMBL:RSS76748.1,
RC ECO:0000313|Proteomes:UP000277644};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL Submitted (NOV-2018) 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:RSS76748.1}.
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DR EMBL; RPRY01000189; RSS76748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9W923; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000277644; 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 Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR008670; CoA_reduct_LuxC.
DR PANTHER; PTHR43845; BLR5969 PROTEIN; 1.
DR PANTHER; PTHR43845:SF1; BLR5969 PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF05893; LuxC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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:UP000277644}.
FT DOMAIN 468..665
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT NON_TER 720
FT /evidence="ECO:0000313|EMBL:RSS76748.1"
SQ SEQUENCE 720 AA; 77338 MW; 6703601F6FF3A40A CRC64;
MPSAVEAALG TVLEPETVLA ACDALATALR DAEHPVRARL AAHLPEDAGP QVLSELGHHL
GRRELTRKLR RELGSAAPGR LERADPRETV YEAWAPVGLV AHVAPGNAAT VAPLSIVEGL
LAGNVNILKT SGSDTLFTQH LMAELAALDP TGAVAARVMV LRFPSSRQDW LQLMCAPADA
VAVWGGEGAV EGVAAHVPAG CRLVEWGHRI SFAYLTRDAW ADGAALDALA DDVCRYEQQA
CASPQVVYLD TEDEAEVFAF AERFAAVLAK RPAAAPLPGG QQPDPAEEAE LTTTELVARL
EEHLGLTRVF AAADGSWRVM ADTRSPLTAS PLHRSVWVKP LPRARLIGTL RPMRRYLQTA
GIAGSRTDIA ELSRTVLAAG ATRVTPVGAM LDSYAGEPHD GVYALQRYSR RVAVQADPGR
FATTACLDDL ARTVVLPPPA GPLLGKEEVQ GLNRQVARAD AELYFRSGGS TGAPALSLFS
YDDYDTQMHA AARGLLAAGY DPAGDRTANL FYCGGMYGSF ISFFSVLERL GGVQLPLAAG
PDHRATAQTL IDHGVDTLFG MPSYLWQLLH AESDALRAYG GLRKVFYGGE HFTEEQQRTL
KDTFGIEVVR SITYGSTDLG PLGYQCTEST GGVHHLHADL HSLEILDLEE DRPVPPGGTG
RLVFTTHARR GQQLGRYVIG DLGRAVPGRC PCGNRAPRFE LRGRTGDVMR VATYFLNHRR
//
