[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=MJ-1; Knight T., Papadakis N.; "Vibrio fischeri Lux operon SalI digest."; Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81. DOI=10.1093/nar/15.24.10455; PubMed=3697093 [NCBI, ExPASy, EBI, Israel, Japan] Engebrecht J., Silverman M.; "Nucleotide sequence of the regulatory locus controlling expression of bacterial genes for bioluminescence."; Nucleic Acids Res. 15:10455-10467(1987).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. STRAIN=ATCC 7744 / NCIMB 1281; Devine J.H., Countryman C., Baldwin T.O.; "Nucleotide sequence of the luxR and luxI genes and structure of the primary regulatory region of the lux regulon of Vibrio fischeri ATCC 7744."; Biochemistry 27:837-842(1988).

Comments

FUNCTION: LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.
CATALYTIC ACTIVITY: A long-chain aldehyde + CoA + NADP⁺ = a long-chain acyl-CoA + NADPH.
PATHWAY: Lipid metabolism; bioluminescent fatty acid reduction .
SIMILARITY: Belongs to the luxC family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF170104; AAD48475.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19039; AAA27553.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00509; CAA68563.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S06862; S06862.

3D structure databases

ModBase

P12748.

Ontologies

GO:0050062;	Molecular function: long-chain-fatty-acyl-CoA reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008670; LuxC.
Graphical view of domain structure.

Pfam

PF05893; LuxC; 1.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Luminescence; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 479`	`479`		`Acyl-CoA reductase.`	`PRO_0000220201`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 54578 Da [This is the MW of the unprocessed precursor]

CRC64: 10FD9567E5026340 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKCIPMIIN GMIQDFDNYA YKEVKLNNDN RVKLSVITES SVSKTLNIKD RINLNLNQIV 

        70         80         90        100        110        120 
NFLYTVGQRW KSEEYNRRRT YIRELKTYLG YSDEMARLEA NWIAMLLCSK SALYDIVNYD 

       130        140        150        160        170        180 
LGSIHVLDEW LPRGDCYVKA QPKGVSVHLL AGNVPLSGVT SILRAILTKN ECIIKTSSSD 

       190        200        210        220        230        240 
PFTANALVSS FIDVNADHPI TKSMSVMYWP HDEDMTLSQR IMNHADVVIA WGGDEAIKWA 

       250        260        270        280        290        300 
VKYSPPHVDI LKFGPKKSLS IIEAPKDIEA AAMGVAHDIC FYDQQACFST QDVYYIGDNL 

       310        320        330        340        350        360 
PLFLNELEKQ LDRYAKILPK GSNSFDEKAA FTLTEKESLF AGYEVRKGDK QAWLIVVSPT 

       370        380        390        400        410        420 
NSFGNQPLSR SVYVHQVSDI KEIIPFVNKN RTQTVSIYPW EASLKYRDKL ARSGVERIVE 

       430        440        450        460        470 
SGMNNIFRVG GAHDSLSPLQ YLVRFVSHER PFNYTTKDVA VEIEQTRYLE EDKFLVFVP

P12748 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools