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 25-MAY-2022, entry version 86.
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; Proteobacteria; 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 GeneID; 57823105; -.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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; SSF53720; 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