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Q74ZH6 (LIPA_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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
Ordered Locus Names:AGR231C
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length369 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
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 – 3232Mitochondrion Potential
Chain33 – 369337Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398250

Sites

Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1111Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1431Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74ZH6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 056A20D95C457E4C

FASTA36941,501
        10         20         30         40         50         60 
MLTKGVRALA WSPRRYITLD AEAAKPVVAK RRRMTEFTDK LNKGPSFEDF LTGKAAQMTL 

        70         80         90        100        110        120 
DPLEEARQNA EESKKLPAWL KVPIPKGKNF HKLKEDVRDL KLSTVCEEAK CPNIGECWGG 

       130        140        150        160        170        180 
NKGSATATIM LLGDTCTRGC RFCSVKTNRT PAKPDPKEPE NTAEAISRWG LGYVVLTMVD 

       190        200        210        220        230        240 
RDDLPDGGAH HLAETVQRIK QKAPHILVET LAGDFRGNLE MVDVMARSGL DVYAHNVETV 

       250        260        270        280        290        300 
EALTPHVRDR RATYQQSLSV LKRAKQTVPT LVTKTSIMLG MGETDEQVLQ TMKDLRAVDC 

       310        320        330        340        350        360 
DVVTFGQYMR PTRRHMKVVE YVKPEKFDYW KEKALELGFL YCASGPLVRS SYKAGEAYIE 


NVLRNRRQA 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016820 Genomic DNA. Translation: AAS54721.1.
RefSeqNP_986897.1. NM_211959.1.

3D structure databases

ProteinModelPortalQ74ZH6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_AGR231C.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS54721; AAS54721; AGOS_AGR231C.
GeneID4623199.
KEGGago:AGOS_AGR231C.

Phylogenomic databases

HOGENOMHOG000235998.
KOK03644.
OMATIRAVRH.
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_ASHGO
AccessionPrimary (citable) accession number: Q74ZH6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 76 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