Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C1GFM3 (LIPA_PARBD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 29. 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:PADG_06059
OrganismParacoccidioides brasiliensis (strain Pb18) [Complete proteome]
Taxonomic identifier502780 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length438 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 – 438407Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398278

Sites

Metal binding1481Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1531Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1831Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1861Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C1GFM3 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 348C53B8A25B3F3C

FASTA43847,521
        10         20         30         40         50         60 
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS SNSTPTPKQR 

        70         80         90        100        110        120 
ITAFKDKLNA GPSFSDFVSG GGGGGASNDR VPLDPAEAYA LKTALVGPPG RKKQIIRLPS 

       130        140        150        160        170        180 
WLKTPIPDTP NYRRIKSDLR GLNLHTVCEE ARCPNISDCW GGSSKSAATA TIMLMGDTCT 

       190        200        210        220        230        240 
RGCRFCSVKT SRTPPPLDPH EPENTAEALS RWGLGYVVMT SVDRDDLADG GARHVVETVR 

       250        260        270        280        290        300 
KVKQKAPGIL LECLTGDYAG DLEMVALVAT SGLDVFAHNV ETVEALTPFV RDRRATFQQS 

       310        320        330        340        350        360 
LRVLKAAKEA RPELITKTSI MLGLGETETQ LWETLRALRA VDVDVVTFGQ YMRPTKRHMA 

       370        380        390        400        410        420 
VHEYVRPEVF DLWKERALEM GFLYCASGPL VRSSYKAGEA FIENVLKKRR GEGADGGDGG 

       430 
NSTRREDVER LVAGGVVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS572756 Genomic DNA. Translation: EEH49980.1.

3D structure databases

ProteinModelPortalC1GFM3.
ModBaseSearch...
MobiDBSearch...

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]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_PARBD
AccessionPrimary (citable) accession number: C1GFM3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 29 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