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Database: UniProt
Entry: A0A0F2TKL7_STRR3
LinkDB: A0A0F2TKL7_STRR3
Original site: A0A0F2TKL7_STRR3 
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
//
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