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Q2LYK1 (LIAS_DROPS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. 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:GA18753
OrganismDrosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]
Taxonomic identifier46245 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length374 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
Reference 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? – 374Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398221

Sites

Metal binding1011Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1321Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1391Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LYK1 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: E27E02B8B2B5A9F7

FASTA37442,118
        10         20         30         40         50         60 
MLTAFRPNSP TAIVVRAAST NAKKLEEIRE RLAKGPNFQD FVQNPDNLKS VGENYDGKLR 

        70         80         90        100        110        120 
REKGEEQRLR LPPWLKTTIP MGKNYTKIKE QLRELKLSTV CEEARCPNIG ECWGGGENGT 

       130        140        150        160        170        180 
QTATIMLMGD TCTRGCRFCS VKTARIPPPL DENEPVNTAK AIASWGLDYI VLTSVDRDDL 

       190        200        210        220        230        240 
PDGGSKHIAQ TVREIKARNS NIFVECLVPD FRGDLDCVET IANCGLDVYA HNIETVEKLT 

       250        260        270        280        290        300 
PYVRDRRAHY RQTLRVLTEA KRFNPNLITK SSIMLGLGET DEEIERTMTD LREAGVECLT 

       310        320        330        340        350        360 
LGQYMQPTNK HLKVIEYVTP EKFKHWEERG NDLGFLYTAS GPLVRSSYKA GEFFISSILA 

       370 
NRKANQSKDS APKN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH379069 Genomic DNA. Translation: EAL29861.1.
RefSeqXP_001354122.1. XM_001354086.1.

3D structure databases

ProteinModelPortalQ2LYK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7237.FBpp0275593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0277155; FBpp0275593; FBgn0078753.
GeneID4813963.
KEGGdpo:Dpse_GA18753.

Organism-specific databases

FlyBaseFBgn0078753. Dpse\GA18753.

Phylogenomic databases

eggNOGCOG0320.
InParanoidQ2LYK1.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG7P2XS7.
PhylomeDBQ2LYK1.

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_DROPS
AccessionPrimary (citable) accession number: Q2LYK1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 21, 2006
Last modified: July 9, 2014
This is version 58 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