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B9WFS9 (LIPA_CANDC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 36. 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:CD36_42180
OrganismCandida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) [Complete proteome]
Taxonomic identifier573826 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length386 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? – 386Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398259

Sites

Metal binding1071Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1181Iron-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
B9WFS9 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: FFA817124590CC52

FASTA38643,349
        10         20         30         40         50         60 
MITRNSIILR RLYPTAIIRT LATDATESTV VKTKRRRTIF TDELNKGPSF DDFVSGKAKD 

        70         80         90        100        110        120 
MLEDPLETAR KDPNAKLPSW LKVPIPKGKS FHNVKKDVRE LKLATVCEEA KCPNIGECWG 

       130        140        150        160        170        180 
GKKSEATATI MLLGDTCTRG CRFCSVKTNR KPAAPDPMEP ENTAEAISRW GLGYVVLTTV 

       190        200        210        220        230        240 
DRDDLVDGGA RHLAETVQKI KQKAPQILVE VLGGDFRGDL SMVEILANSG LDVYAHNLET 

       250        260        270        280        290        300 
VEALTPHIRD RRATYRQSLA VLERAKQTNS SLITKTSLML GFGETDDQVK QTLRDLREIG 

       310        320        330        340        350        360 
CDVVTFGQYM RPTKRHMKVV EYIKPEKFDY WRDTALDMGF LYVASGPLVR SSYKAGEAFI 

       370        380 
ENVLKKRKHN VGETPRLAQE IKPSIY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM992691 Genomic DNA. Translation: CAX42098.1.
RefSeqXP_002419883.1. XM_002419838.1.

3D structure databases

ProteinModelPortalB9WFS9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING573826.CD36_42180.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8047477.
KEGGcdu:CD36_42180.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OrthoDBEOG79KPR7.

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 nameLIPA_CANDC
AccessionPrimary (citable) accession number: B9WFS9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: June 11, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways