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Database: UniProt
Entry: LUXC_VIBHA
LinkDB: LUXC_VIBHA
Original site: LUXC_VIBHA 
ID   LUXC_VIBHA              Reviewed;         477 AA.
AC   P08639;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Long-chain acyl-protein thioester reductase {ECO:0000305};
DE            EC=1.2.1.50 {ECO:0000250|UniProtKB:P19841};
DE   AltName: Full=Acyl-CoA reductase;
GN   Name=luxC;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3347497; DOI=10.1093/nar/16.4.1551;
RA   Miyamoto C.M., Graham A.F., Meighen E.A.;
RT   "Nucleotide sequence of the LuxC gene and the upstream DNA from the
RT   bioluminescent system of Vibrio harveyi.";
RL   Nucleic Acids Res. 16:1551-1562(1988).
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 + 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:0000250|UniProtKB:P19841};
CC   -!- PATHWAY: Lipid metabolism; fatty acid reduction for biolumincescence.
CC   -!- SIMILARITY: Belongs to the LuxC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA30117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X07084; CAA30116.1; -; Genomic_DNA.
DR   EMBL; X07084; CAA30117.1; ALT_INIT; Genomic_DNA.
DR   PIR; A28534; A28534.
DR   RefSeq; WP_038897471.1; NZ_UAVF01000022.1.
DR   AlphaFoldDB; P08639; -.
DR   SMR; P08639; -.
DR   PATRIC; fig|669.65.peg.3629; -.
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:UniProtKB-KW.
DR   CDD; cd07080; ALDH_Acyl-CoA-Red_LuxC; 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..477
FT                   /note="Long-chain acyl-protein thioester reductase"
FT                   /id="PRO_0000220202"
SQ   SEQUENCE   477 AA;  54840 MW;  86D776D3474A6918 CRC64;
     MEKHLPLIVN GQIISTEENR FEISFEEKKV KIDSFNNLHL TQMVNHDYLN DLNINNIINF
     LYTTGQRWKS EEYSRRRAYI RSLITYLGYS PQMAKLEANW IAMILCSKSA LYDIIDTELG
     STHIQDEWLP QGECYVRAFP KGRTMHLLAG NVPLSGVTSI LRGILTRNQC IVRMSASDPF
     TAHALAMSFI DVDPNHPISR SISVLYWPHA SDTTLAEELL SHMDAVVAWG GRDAIDWAVK
     HSPSHIDVLK FGPKKSFTVL DHPADLEEAA SGVAHDICFY DQNACFSTQN IYFSGDKYEE
     FKLKLVEKLN LYQEVLPKSK QSFDDEALFS MTRLECQFSG LKVISEPENN WMIIESEPGV
     EYNHPLSRCV YVHKINKVDD VVQYIEKHQT QTISFYPWES SKKYRDAFAA KGVERIVESG
     MNNIFRAGGA HDAMRPLQRL VRFVSHERPY NFTTKDVSVE IEQTRFLEED KFLVFVP
//
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