NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 25521 / L1 / CIP 665;
PubMed=1915359 [NCBI, ExPASy, EBI, Israel, Japan]
Lee C.Y., Szittner R.B., Meighen E.A.;
"The lux genes of the luminous bacterial symbiont, Photobacterium leiognathi, of the ponyfish. Nucleotide sequence, difference in gene organization, and high expression in mutant Escherichia coli.";
Eur. J. Biochem. 201:161-167(1991).

Comments

FUNCTION: Acyl-protein synthetase activates tetradecanoic acid. It is a component of the fatty acid reductase complex responsible for converting tetradecanoic acid to the aldehyde which serves as substrate in the luciferase-catalyzed reaction.
CATALYTIC ACTIVITY: ATP + an acid + protein = AMP + diphosphate + an acyl-protein thioester.
PATHWAY: Lipid metabolism; bioluminescent fatty acid reduction .
SIMILARITY: Belongs to the luxE 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

M63594; AAA25620.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17955; S17955.

3D structure databases

ModBase

P29334.

Ontologies

GO:0047474;	Molecular function: long-chain-fatty-acid-luciferin-component ligase activity (inferred from electronic annotation from InterPro).
GO:0008218;	Biological process: bioluminescence (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016671; Acyl-protein_synth_LuxE_bac.
IPR007534; LuxE.
Graphical view of domain structure.

Pfam

PF04443; LuxE; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF016580; Acyl-protein_synthetase_LuxE; 1.

ProtoNet

P29334.

Other

UniRef

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

Keywords

Ligase; Luminescence.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 373`	`373`		`Long-chain-fatty-acid--luciferin-component ligase.`	`PRO_0000208063`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 43099 Da [This is the MW of the unprocessed precursor]

CRC64: 1B31848B00BF9921 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTLLNIDAT EIKVSTEIDD IIFTSSPLTL LFEDQEKIQK ELILESFHYH YNHNKDYKYY 

        70         80         90        100        110        120 
CNIQGVDENI QSIDDIPVFP TSMFKYSRLH TADESNIENW FTSSGTKGVK SHIARDRQSI 

       130        140        150        160        170        180 
ERLLGSVNYG MKYLGEFHEH QLELVNMGPD RFSASNVWFK YVMSLVQLLY PTTFTVENDE 

       190        200        210        220        230        240 
IDFEQTILAL KAIQRKGKGI CLIGPPYFIY LLCHYMKEHN IEFNAGAHMF IITGGGWKTK 

       250        260        270        280        290        300 
QKEALNRQDF NQLLMETFSL FHESQIRDIF NQVELNTCFF EDSLQRKHVP PWVYARALDP 

       310        320        330        340        350        360 
VTLTPVEDGQ EGLMSYMDAS STSYPTFIVT DDIGIVRHLK EPDPFQGTTV EIVRRLNTRE 

       370 
QKGCSLSMAT SLK

P29334 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