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A6ZP42 (LIPA_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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
Name:LIP5
ORF Names:SCY_5257
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length414 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 Potential 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 – 1818Mitochondrion Potential
Chain19 – 414396Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398290

Sites

Metal binding1501Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1611Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1811Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1851Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1881Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A6ZP42 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 962BC3DF9857C3BB

FASTA41446,247
        10         20         30         40         50         60 
MYRRSVGVLF VGRNTRWISS TIRCGTSATR PIRSNALNTD SDNASVRVPV GNSTEVENAT 

        70         80         90        100        110        120 
SQLTGTSGKR RKGNRKRITE FKDALNLGPS FADFVSGKAS KMILDPLEKA RQNTEEAKKL 

       130        140        150        160        170        180 
PRWLKVPIPK GTNYHKLKGD VKELGLSTVC EEARCPNIGE CWGGKDKSKA TATIMLLGDT 

       190        200        210        220        230        240 
CTRGCRFCSV KTNRTPSKPD PMEPENTAEA IKRWGLGYVV LTTVDRDDLV DGGANHLAET 

       250        260        270        280        290        300 
VRKIKQKAPN TLVETLSGDF RGDLKMVDIM AQCGLDVYAH NLETVESLTP HVRDRRATYR 

       310        320        330        340        350        360 
QSLSVLERAK ATVPSLITKT SIMLGLGETD EQITQTLKDL RNIQCDVVTF GQYMRPTKRH 

       370        380        390        400        410 
MKVVEYVKPE KFDYWKERAL EMGFLYCASG PLVRSSYKAG EAFIENVLKK RNMK 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YJM789.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000032 Genomic DNA. Translation: EDN63532.1.

3D structure databases

ProteinModelPortalA6ZP42.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEA6ZP42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

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_YEAS7
AccessionPrimary (citable) accession number: A6ZP42
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 37 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