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C1H594 (LIPA_PARBA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 32. 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:PAAG_05935
OrganismParacoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis) [Complete proteome]
Taxonomic identifier502779 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesParacoccidioides

Protein attributes

Sequence length439 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 – 3737Mitochondrion Potential
Chain38 – 439402Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398276

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
C1H594 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 3BAB21D357F78492

FASTA43947,567
        10         20         30         40         50         60 
MVASARGLRT LHSAHSSISA LPASTVPRLQ LAVSRCYATT TSPDCPITNS SNSSNSTPTL 

        70         80         90        100        110        120 
TPKQRITAFK DKLNAGPSFS DFVSGGGASN DSVPLDPTEA YSLKTALVGP PGKKKQIIRL 

       130        140        150        160        170        180 
PSWLKTPIPD SPNFRRIKSD LRGLNLHTVC EEARCPNISD CWGGSSKSAA TATIMLMGDT 

       190        200        210        220        230        240 
CTRGCRFCSV KTSRTPPPLD PHEPENTAEA LSRWGLGYVV MTSVDRDDLA DGGARHVAET 

       250        260        270        280        290        300 
VRKVKQKAPN ILLECLTGDY AGDLEMVALV ATSGLDVFAH NVETVEALTP FVRDRRATFQ 

       310        320        330        340        350        360 
QSLRVLKAAK EAKPELITKT SIMLGLGETE AQLWETLKAL RAVDVDVVTF GQYMRPTKRH 

       370        380        390        400        410        420 
MAVHEYVRPD VFDSWKERAL EMGFLYCASG PLVRSSYKAG EAFIENVLKK RRGEGADGSG 

       430 
GSSTRREDVE RLVAGGVVR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS572826 Genomic DNA. Translation: EEH34888.1.
RefSeqXP_002792147.1. XM_002792101.1.

3D structure databases

ProteinModelPortalC1H594.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9095385.
KEGGpbl:PAAG_05935.

Phylogenomic databases

KOK03644.
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_PARBA
AccessionPrimary (citable) accession number: C1H594
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 32 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