ID   LUXC2_PHOLE             Reviewed;         478 AA.
AC   P29236;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Long-chain acyl-protein thioester reductase 2 {ECO:0000305};
DE            EC=1.2.1.50 {ECO:0000250|UniProtKB:P19841};
DE   AltName: Full=Acyl-CoA reductase 2;
GN   Name=luxC;
OS   Photobacterium leiognathi.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25521 / DSM 21260 / CCUG 16229 / CIP 66.5 / NCIMB 2193 /
RC   L1;
RX   PubMed=1915359; DOI=10.1111/j.1432-1033.1991.tb16269.x;
RA   Lee C.Y., Szittner R.B., Meighen E.A.;
RT   "The lux genes of the luminous bacterial symbiont, Photobacterium
RT   leiognathi, of the ponyfish. Nucleotide sequence, difference in gene
RT   organization, and high expression in mutant Escherichia coli.";
RL   Eur. J. Biochem. 201:161-167(1991).
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:0000250|UniProtKB:P19841}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty aldehyde + NADP(+) + CoA = a long-chain
CC         fatty acyl-CoA + NADPH + H(+); 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:0000250|UniProtKB:P19841};
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC   -!- SIMILARITY: Belongs to the LuxC family. {ECO:0000305}.
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DR   EMBL; M63594; AAA25616.1; -; Genomic_DNA.
DR   PIR; S17836; S17836.
DR   AlphaFoldDB; P29236; -.
DR   SMR; P29236; -.
DR   UniPathway; UPA00569; -.
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:InterPro.
DR   CDD; cd07080; ALDH_Acyl-CoA-Red_LuxC; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR008670; CoA_reduct_LuxC.
DR   Pfam; PF05893; LuxC; 1.
DR   PIRSF; PIRSF009414; LuxC; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Luminescence; NADP; Oxidoreductase.
FT   CHAIN           1..478
FT                   /note="Long-chain acyl-protein thioester reductase 2"
FT                   /id="PRO_0000220197"
SQ   SEQUENCE   478 AA;  53713 MW;  4716EF699BF7FE4A CRC64;
     MIKKIPMIIG GVVQNTSGYG MRELTLNNNK VNIPIITQSD VEAIQSLNIE NKLTINQIVN
     FLYTVGQKWK SETYSRRLTY IRDLIKFLGY SQEMAKLEAN WISMILCSKS ALYDIVENDL
     SSRHIIDEWI PQGECYVKAL PKGKSVHLLA GNVPLSGVTS ILRAILTKNE CIIKTSSADP
     FTATALVNSF IDVDAEHPIT RSISVMYWSH SEDLAIPKQI MSCADVVIAW GGDDAIKWAT
     EHAPSHADIL KFGPKKSISI VDNPTDIKAA AIGVAHDICF YDQQACFSTQ DIYYIGDSID
     IFFDELAQQL NKYKDILPKG ERNFDEKAAF SLTERECLFA KYKVQKGESQ SWLLTQSPAG
     SFGNQPLSRS AYIHQVNDIS EVIPFVHKAV TQTVAIAPWE SSFKYRDILA EHGAERIIEA
     GMNNIFRVGG AHDGMRPLQR LVNYISHERP STYTTKDVSV KIEQTRYLEE DKFLVFVP
//