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Q21452 (LIAS_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. 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
ORF Names:M01F1.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length354 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? – 354Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398228

Sites

Metal binding911Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding961Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1021Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1221Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1261Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1291Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21452 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5428CFA42A7FCDEE

FASTA35439,767
        10         20         30         40         50         60 
MLARVWVRGL AATKKKPQVL VKDGPSLQDF ISSASVAEAV EKYEGKLKLE KGDRRLRLPP 

        70         80         90        100        110        120 
WLKKEKILPS ENENVSRLKK QLKHLKLATV CQEARCPNLG ECWGGSDDSL ATATIMLMGD 

       130        140        150        160        170        180 
TCTRGCKFCS VKTARAPPPL DPMEPENTST AVASWGVEYI VLTSVDRDDL PDGGADHLRK 

       190        200        210        220        230        240 
TVQLMKLKKP ELLIECLLPD FAGDKISVEK MATSGLDVYA HNIETVERLT PWVRDPRAKY 

       250        260        270        280        290        300 
RQSLDALRYA KEVSPKLITK TSIMLGLGEA EDEIKQCLAD LRASNVDVVT FGQYMQPTKR 

       310        320        330        340        350 
HLLVKEWVTP EKFDQWAEYS KKLGFLYVAS GPLVRSSYKA GEFYLKNVLR NRQN 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46381 Genomic DNA. Translation: CAA86516.1.
PIRT23655.
RefSeqNP_497722.3. NM_065321.6.
UniGeneCel.38595.

3D structure databases

ProteinModelPortalQ21452.
SMRQ21452. Positions 116-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid532131. 7 interactions.
STRING6239.M01F1.3.3.

Proteomic databases

PaxDbQ21452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaM01F1.3.1; M01F1.3.1; WBGene00010809.
M01F1.3.2; M01F1.3.2; WBGene00010809.
M01F1.3.3; M01F1.3.3; WBGene00010809.
GeneID3564813.
KEGGcel:CELE_M01F1.3.
UCSCM01F1.3.1. c. elegans.

Organism-specific databases

CTD3564813.
WormBaseM01F1.3; CE01031; WBGene00010809.

Phylogenomic databases

eggNOGCOG0320.
GeneTreeENSGT00390000006234.
HOGENOMHOG000235998.
InParanoidQ21452.
KOK03644.
OMATIRAVRH.
PhylomeDBQ21452.

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...

Other

NextBio954083.
PROQ21452.

Entry information

Entry nameLIAS_CAEEL
AccessionPrimary (citable) accession number: Q21452
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase