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B3NIL9 (LIAS_DROER) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Name:Las
ORF Names:GG13311
OrganismDrosophila erecta (Fruit fly) [Complete proteome]
Taxonomic identifier7220 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_03123

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_03123

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_03123

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03123.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   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_componentmitochondrion

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

Transit peptide1 – ?Mitochondrion Potential
Chain? – 379Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398217

Sites

Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1111Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B3NIL9 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 59480438DFBEB65A

FASTA37942,807
        10         20         30         40         50         60 
MFGMLRALKT HVEAPIVVAT RAVSTNAEKL EEIRERLAKG PNFQDFVQNP ENSRSEWEKY 

        70         80         90        100        110        120 
EGKLRREKGE EQRLRLPPWL KTTIPVGKNY AKIKAQMREL KLSTVCEEAR CPNIGECWGG 

       130        140        150        160        170        180 
GEHGTQTATI MLMGDTCTRG CRFCSVKTAR RPPPLDVNEP VNTATAIASW GLDYIVLTSV 

       190        200        210        220        230        240 
DRDDLPDGGS KHIAETVREI KARNSNIFVE CLVPDFRGNL ECVETIANSG LDVYAHNIET 

       250        260        270        280        290        300 
VEKLTPYVRD RRAHYRQTLQ VLTEAKRFNP NLITKSSIML GLGETDGEIE CTLKDLREAG 

       310        320        330        340        350        360 
VDCVTLGQYM QPTNKHLKVI EYVTPEKFKH WEERGNALGF LYTASGPLVR SSYKAGEFFI 

       370 
TSILENRKKR QNATEIAKE 

« Hide

References

[1]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 genomes consortium
Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tucson 14021-0224.01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH954178 Genomic DNA. Translation: EDV52515.1.
RefSeqXP_001973489.1. XM_001973453.1.

3D structure databases

ProteinModelPortalB3NIL9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0133365; FBpp0131857; FBgn0105583.
GeneID6545884.
KEGGder:Dere_GG13311.

Organism-specific databases

FlyBaseFBgn0105583. Dere\GG13311.

Phylogenomic databases

KOK03644.
OrthoDBEOG7P2XS7.
PhylomeDBB3NIL9.

Enzyme and pathway databases

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 nameLIAS_DROER
AccessionPrimary (citable) accession number: B3NIL9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 2, 2008
Last modified: July 9, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase