ID   A0A1Z1WF14_9ACTN        Unreviewed;       852 AA.
AC   A0A1Z1WF14;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SMD44_04416 {ECO:0000313|EMBL:ARX84958.1};
OS   Streptomyces alboflavus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX84958.1, ECO:0000313|Proteomes:UP000195880};
RN   [1] {ECO:0000313|EMBL:ARX84958.1, ECO:0000313|Proteomes:UP000195880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK44 {ECO:0000313|EMBL:ARX84958.1,
RC   ECO:0000313|Proteomes:UP000195880};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT   "Streptomyces alboflavus Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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; CP021748; ARX84958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z1WF14; -.
DR   STRING; 67267.GCA_000716675_04298; -.
DR   KEGG; salf:SMD44_04416; -.
DR   eggNOG; COG1541; Bacteria.
DR   OrthoDB; 580775at2; -.
DR   UniPathway; UPA00569; -.
DR   Proteomes; UP000195880; Chromosome.
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; 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; 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:UP000195880}.
FT   REGION          831..852
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  92920 MW;  F9C11B712F34BDF6 CRC64;
     MSELNHLWQG TRIDDAEAAR RLPELPDLVI DALRRPLPTD VVIEACDRLA RVLDTADHPT
     RAKLAQLLYA AGKSTDDADA AFAVLTSFLG REGLERKLRA ELGDVRPDRL TRPDPRKLTF
     ETWAPVGLVV HIAPGNAPTV GALTAVEGLL AGNVNVVKVP GSAGLFTHEL LAALADCDPT
     GLIEAYTVVM RFGSGRTDWL RLLCGAADAV AVWGGEAAVE GVAAHVPPGC RLVEWGHKIS
     FAYLTADAWA RPDTLRALAD DVCRMEQQAC SSPQVIYLDT DDTDEVFAFA ERFAPALSEA
     SARTPAPDLG LAEQAEITNT EIVAELEEHL GLTRVTAAPD GSWRIIADTR SALRASPLFR
     SVWVKPLPRK DIPAVLRPMR RYLQTVGLAA DRPDTAELAR TFFGAGALRV TAPGGQLDSY
     SGEPHDGVYA LQRYSRRVSL QADERFATDG CLDDLTAPGP RLPAPEGPLT TKSDALAALD
     SVHPDHAQLY VRSGGSTSGP ATWVYTWDDY DAQMRAAGEG LLAAGFDPRH DRAANLFMPG
     QMYGSFTSFF DILERLAATQ IPYGVHADFE AVADALIRYR VNTLFGAPSY LLQLFAAQGE
     RLRDHGRVEK VFYGGAHLTD AQRRVLHDEF GVKVVRSAIY GSNDLGPMGY QCDHATGAVH
     HLFTTQLDLE ILDRAADGPA PADEPGRLVF TPRTRLGQRL DRYETSDLGR WIPGPCACGR
     HTPRFELLGR YGDTARVGAF FISHQHLTRV AAEAFGYAGE LQLVLSEGLE QERLTIRLDH
     RHAPDPATAR RHFLTHYPEL RNAVEVARMA DVEVHVIDGA HFERGATSGK LRNIIDRRPA
     ATGRPTEPQP SH
//