ID A0A0F2TKL7_STRR3 Unreviewed; 846 AA.
AC A0A0F2TKL7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=VM95_09670 {ECO:0000313|EMBL:KJS62267.1};
OS Streptomyces rubellomurinus (strain ATCC 31215).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS62267.1, ECO:0000313|Proteomes:UP000033699};
RN [1] {ECO:0000313|EMBL:KJS62267.1, ECO:0000313|Proteomes:UP000033699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS62267.1,
RC ECO:0000313|Proteomes:UP000033699};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJS62267.1}.
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DR EMBL; JZKH01000014; KJS62267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2TKL7; -.
DR PATRIC; fig|359131.3.peg.1422; -.
DR UniPathway; UPA00569; -.
DR Proteomes; UP000033699; 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:UP000033699}.
FT DOMAIN 483..697
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 846 AA; 91163 MW; 196175FC9654408B CRC64;
MNPELASTAP HFWQGSFIDD DEAARRLAEL PDLAARTLAE PLPTELVLSA CQHLADALGA
PGDPVRARLL AELTGGGVDP DEAAATLAEI AGAIARPALE RKLRSELGGL RPERLTRPDA
RETTFEAWAP VGLLVHIAPG NAAAVAPLSV IEGLLTGNLN VLKTSSADTP LAQHLLAELA
AADPTGALAR RIVALRFPSA RTAWLRLMCE AADAVAVWGG EDAVRAVSEL VPAGCRLVEW
GHRVSFAYLT RDAWSDRVTL DALAADVCRF EQQACSSPQV VYLDTEDDEE VFAFAERFAA
HLADASAELP RPELEPAEHA EITTTELVAR LEEHLGLTRV LAAEDGSWRV LADTRPALAA
SPLHRSVWVK PLPRARVMPV LRPMRRYLQT AAIAGSRADV ARLSQAVLAA GVLRVTPVGG
MLDGYHGEPH DGVYALQRYS RRVSVRTDRA FATTACLDDL AAPAFVPAAP SGPLLDKAGV
QEQLRTLAPE HAHLHFRSGG STGAPALSVF TNADYDTQMR ACADGLLAAG FDPARDRAAN
LFYCGGMYGS FISFFSILER LNATQLPIAA GPDHTATAEA LVTNGADTVF GMPSYLWQLF
HARADQLRAY GGIRKVFYGG EHFTAEQRRV LTEEFGVEVI RSAAYGSTDL GPLGYQCTHA
EGSVHHVLTD LHTLEILAPE ADRPVPAGQP GRLVFTSRTR AGQRLERYQI GDLGRAVEGV
CPCGSHTPRL ELLGRYGDVV RVATYFLNVR RFVAVAQEEF GYQGELQLVL DAGEGRERAV
VRLDGRYAQD GPAARAAFLT AIPELGSAVD EELLDFRVET VDSGAFERTP TSGKLRTVID
RRRTTM
//