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Q5WYF5 (LIPA_LEGPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoyl synthase

EC=2.8.1.8
Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene names
Name:lipA
Ordered Locus Names:lpl0781
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives By similarity. HAMAP-Rule MF_00206

Catalytic activity

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_00206

Cofactor

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_00206

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325268

Sites

Metal binding721Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding771Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding831Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding981Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1021Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WYF5 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: ED7555CFA828FC7B

FASTA32936,754
        10         20         30         40         50         60 
MGKLIDIPIV VESGQKYKTS QGVTAIKDGI KSSGQDHERL PKPKWLRIVN HTTPAYSQVK 

        70         80         90        100        110        120 
EQVQKHRLAT VCEEAKCPNI SECWSHGTAT IMLMGAVCTR ACRFCSVDTG NPHGWLDAEE 

       130        140        150        160        170        180 
PENTAETVAL MNLDYVVLTS VNRDDLPDGG ANHYAKTIRA IKKRSPRTKV EALTPDFQGS 

       190        200        210        220        230        240 
ERDVAVLLDS GLDVFAQNVE TVERLTHPVR DNRAGYQQTL NVLAFAKKYR PDVLTKTSLM 

       250        260        270        280        290        300 
LGLGETDEEI IRTMDDLRAH HVDILTLGQY LQPTKNHLPI ARYVTPETFS ELRQIGLKKG 

       310        320 
FFEVASGPLV RSSYRADRVF KRDNLGLDV 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH15015.1.
RefSeqYP_126143.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WYF5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl0781.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH15015; CAH15015; lpl0781.
GeneID3115445.
KEGGlpf:lpl0781.
PATRIC22315117. VBILegPne33733_0893.

Organism-specific databases

LegioListlpl0781.
CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-840-MONOMER.
UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_LEGPL
AccessionPrimary (citable) accession number: Q5WYF5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways