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A8PF69 (LIAS_BRUMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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, 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:Bm1_23910
OrganismBrugia malayi (Filarial nematode worm) [Complete proteome]
Taxonomic identifier6279 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length357 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? – 357Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398227

Sites

Metal binding891Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding941Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1001Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1201Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1241Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1271Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8PF69 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: D2D111962123E37C

FASTA35739,992
        10         20         30         40         50         60 
MISFTTRISR VTFSSKRVAL PDGPSLHDFI ETGNSNDAVE KYGIQMKLEA NAKRLRLPPW 

        70         80         90        100        110        120 
LKRSIPSVDN TNFTHLKKQV KKLKLATVCE EARCPNIEEC WSGSNNVPST ATIMLMGDTC 

       130        140        150        160        170        180 
TRGCKFCSVK TSLKPPPLNP EEPINTAKAI ADWGINYVVL TSVDRDDIED GGASHIAATV 

       190        200        210        220        230        240 
KHLKQECPNI LVECLVPDFR GSLSSVETIA SSGLDVYAHN METVRRLTPW VRDPRATYDQ 

       250        260        270        280        290        300 
SLKVLEYAKK FRADIVTKTS LMLGLGETDE EVLTTLHDLR KIGVDALTFG QYMQPTKRHL 

       310        320        330        340        350 
LVKEWITPEK FEEWREVGDX LGFLYTASGP LVRSSYKAGE YFLGKVVKNR KQGVQEN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS239138 Genomic DNA. Translation: EDP34906.1.
RefSeqXP_001896239.1. XM_001896204.1.

3D structure databases

ProteinModelPortalA8PF69.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6099682.
KEGGbmy:Bm1_23910.

Organism-specific databases

CTD6099682.

Phylogenomic databases

InParanoidA8PF69.
KOK03644.

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_BRUMA
AccessionPrimary (citable) accession number: A8PF69
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways