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C0SDG9 (LIPA_PARBP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 28. 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:PABG_05724
OrganismParacoccidioides brasiliensis (strain Pb03) [Complete proteome]
Taxonomic identifier482561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length434 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 – 434403Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398277

Sites

Metal binding1441Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1491Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1551Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1821Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0SDG9 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 02DABF6FB68CDDA9

FASTA43447,106
        10         20         30         40         50         60 
MAASARGLRT LQSAHSSTTV PRLQLAVSRC YATTTSPDPP ITNSSNSSNS TPTPKQRITA 

        70         80         90        100        110        120 
FKDKLNAGPS FSDFVSGGGG GASNDRVPLD PAEAYALKTA LVGPPGRKKQ IIRLPSWLKT 

       130        140        150        160        170        180 
PIPDTPNYRR IKSDLRGLNL HTVCEEARCP NISDCWGGSS KSAATATIML MGDTCTRGCR 

       190        200        210        220        230        240 
FCSVKTSRTP PPLDPHEPEN TAEALSRWGL GYVVMTSVDR DDLADGGARH VAETVRKVKQ 

       250        260        270        280        290        300 
KAPGILLECL TGDYAGDLEM VALVATSGLD VFAHNVETVE ALTPFVRDRR ATFQQSLRVL 

       310        320        330        340        350        360 
KAAKEARPEL ITKTSIMLGL GETETQLWET LRALRTVDVD VVTFGQYMRP TKRHMAVHEY 

       370        380        390        400        410        420 
VRPGVFDLWK ERALEMGFLY CASGPLVRSS YKAGEAFIEN VLKKRRGEGA DGGDGGNSTR 

       430 
REDVERLVAG GVVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS544811 Genomic DNA. Translation: EEH23513.1.

3D structure databases

ProteinModelPortalC0SDG9.
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_PARBP
AccessionPrimary (citable) accession number: C0SDG9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 5, 2009
Last modified: June 11, 2014
This is version 28 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