Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4MXR6 (LIAS_DROWI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:GK17689
OrganismDrosophila willistoni (Fruit fly) [Complete proteome]
Taxonomic identifier7260 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length372 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)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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? – 372Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398223

Sites

Metal binding1031Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1081Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1341Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4MXR6 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 49A97DBE8AD6E2A8

FASTA37241,989
        10         20         30         40         50         60 
MLRTIKSPIK VIVRPASASA SANAEKLDEI RERLAKGPSF QDFIQNPNNT KNEWDNYDGK 

        70         80         90        100        110        120 
LRREKVEEQR LRLPPWLKTT IPMGKNYAKI KDQLRELKLS TVCEEARCPN IGECWGGGEH 

       130        140        150        160        170        180 
GTQTATIMLM GDTCTRGCRF CSVKTARAPP PLDENEPVNT AKAVASWGLD YIVLTSVDRD 

       190        200        210        220        230        240 
DLSDGGSKHI AQTVKEIKAR NQNIFVECLV PDFRGDLECV KTIANCGLDV YAHNIETVEK 

       250        260        270        280        290        300 
LTPFVRDRRA HYRQTLKVLS EAKRFNPNLI TKSSIMLGLG ETDAEVEQTM LDLREVGVEC 

       310        320        330        340        350        360 
LTLGQYMQPT KKHLKVIEYV TPEKFKHWEE RGNQLGFLYT ASGPLVRSSY KAGEFFITSI 

       370 
LANRKKQNDA PK 

« 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 14030-0811.24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH963876 Genomic DNA. Translation: EDW76835.1.
RefSeqXP_002065849.1. XM_002065813.1.

3D structure databases

ProteinModelPortalB4MXR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7260.FBpp0246832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0248340; FBpp0246832; FBgn0219688.
GeneID6642928.
KEGGdwi:Dwil_GK17689.

Organism-specific databases

FlyBaseFBgn0219688. Dwil\GK17689.

Phylogenomic databases

eggNOGCOG0320.
InParanoidB4MXR6.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG7P2XS7.

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_DROWI
AccessionPrimary (citable) accession number: B4MXR6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 36 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