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P29334 (LUXE_PHOLE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Long-chain-fatty-acid--luciferin-component ligase

EC=6.2.1.19
Alternative name(s):
Acyl-protein synthetase
Gene names
Name:luxE
OrganismPhotobacterium leiognathi
Taxonomic identifier553611 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (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; fatty acid reduction for biolumincescence.

Sequence similarities

Belongs to the luxE family.

Ontologies

Keywords
   Biological processLuminescence
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological processbioluminescence

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

long-chain fatty acid luciferin component ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373Long-chain-fatty-acid--luciferin-component ligase
PRO_0000208063

Sequences

Sequence LengthMass (Da)Tools
P29334 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 1B31848B00BF9921

FASTA37343,099
        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 

« Hide

References

[1]"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."
Lee C.Y., Szittner R.B., Meighen E.A.
Eur. J. Biochem. 201:161-167(1991) [PubMed: 1915359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25521 / L1 / CIP 665.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63594 Genomic DNA. Translation: AAA25620.1.
PIRS17955.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR007534. LuxE.
IPR016671. LuxE_bac.
[Graphical view]
PfamPF04443. LuxE. 1 hit.
[Graphical view]
PIRSFPIRSF016580. Acyl-protein_synthetase_LuxE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLUXE_PHOLE
AccessionPrimary (citable) accession number: P29334
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 21, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families