[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371. STRAIN=A13; DOI=10.1093/nar/18.21.6450; PubMed=2243804 [NCBI, ExPASy, EBI, Israel, Japan] Prasher D.C., O'Kane D., Lee J., Woodward B.; "The lumazine protein gene in Photobacterium phosphoreum is linked to the lux operon."; Nucleic Acids Res. 18:6450-6450(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-382. PubMed=2071574 [NCBI, ExPASy, EBI, Israel, Japan] Ferri S.R., Meighen E.A.; "A lux-specific myristoyl transferase in luminescent bacteria related to eukaryotic serine esterases."; J. Biol. Chem. 266:12852-12857(1991).

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

X54690; CAA38506.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64224; AAA25625.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B39853; B39853.
S12116; S12116.

3D structure databases

ModBase

P19841.

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

IPR016162; Ald_DHase_N.
IPR008670; LuxC.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

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`	`1 382`	`382`	`Acyl-CoA reductase.`	`PRO_0000220200`
`NON_CONS`	`371 372`

Sequence information

Length: 382 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 43085 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: B6C6316B49030EE9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MCNAEFKGDC MIKKIPMIIG GAERDTSEHE YRELTLNSYK VSIPIINQDD VEAIKSQNVE 

        70         80         90        100        110        120 
NNLNINQIVN FLYTVGQKWK SENYSRRLTY IRDLVRFLGY SPEMAKLEAN WISMILSSKS 

       130        140        150        160        170        180 
ALYDIVETEL GSRHIVDEWL PQGDCYVKAM PKGKSVHLLA GNVPLSGVTS IIRAILTKNE 

       190        200        210        220        230        240 
CIIKTSSADP FTAIALASSF IDTDEHHPIS RSMSVMYWSH NEDIAIPQQI MNCADVVVSW 

       250        260        270        280        290        300 
GGYDAIKWAT EHTPVNVDIL KFGPKKSIAI VDNPVDITAS AIGVAHDICF YDQQACFSTQ 

       310        320        330        340        350        360 
DIYYIGDNID AFFDELVEQL NLYMDILPKG DQTFDEKASF SLIEKECQFA KYKVEKGDNQ 

       370        380 
SWLLVKSPLG SLEEDKFLVF VP

P19841 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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