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B0XYY2 (LIPA_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 35. 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:AFUB_042490
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

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)
   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 – 3131Mitochondrion Potential
Chain32 – 414383Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398254

Sites

Metal binding1311Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1621Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1691Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0XYY2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 2E3D2BEA2E111ECA

FASTA41445,479
        10         20         30         40         50         60 
MAVSTSHFRS LCASRPLSRT AIVGHISCRS YATTEPSPSA TSTSTTTTAR RRTTFKDKLN 

        70         80         90        100        110        120 
AGPSFADFVG NGNTPLDPSE AYALKTALVG PAGRKKEMTR LPSWLKTPIP DSKNYQRLKK 

       130        140        150        160        170        180 
DLRGLNLHTV CEEARCPNIS DCWGGSDKSA ATATIMLMGD TCTRGCRFCS VKTSRTPAPL 

       190        200        210        220        230        240 
DPHEPENTAE AISRWGLGYV VLTSVDRDDL ADGGARHFAE TVMKIKQKAP SILVECLTGD 

       250        260        270        280        290        300 
YAGDLEMVKL VARSGLDVYA HNVETVEALT PQVRDRRANF QQSIRVLEAA KNAQPSLITK 

       310        320        330        340        350        360 
TSLMLGLGET DDQLWDALRQ LRAANVDVVT FGQYMRPTKR HMAVHEYVTP DRFELWRQRA 

       370        380        390        400        410 
LDMGFLYCAS GPLVRSSYKA GEAFIENVLK KRRATSGGTE TVGVRPVTVD EVTR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS499596 Genomic DNA. Translation: EDP53078.1.

3D structure databases

ProteinModelPortalB0XYY2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00004238; CADAFUBP00004166; CADAFUBG00004238.

Phylogenomic databases

HOGENOMHOG000235998.
OrthoDBEOG79KPR7.
PhylomeDBB0XYY2.

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_ASPFC
AccessionPrimary (citable) accession number: B0XYY2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 35 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