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C0NXP6 (LIPA_AJECG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 30. 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:HCBG_07690
OrganismAjellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) [Reference proteome]
Taxonomic identifier447093 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeAjellomyces

Protein attributes

Sequence length430 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)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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 – 430393Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398246

Sites

Metal binding1411Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1461Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1521Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1721Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1761Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0NXP6 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: C0C098FB51E28C50

FASTA43046,821
        10         20         30         40         50         60 
MATSAGKLRT LYSAHSSLSS LPPSARPTLQ LATLRSYATT TPHDSPIGNT SNTPPTVKRP 

        70         80         90        100        110        120 
ATAFKDKLNA GPAFSDFVSG KKDEPLDPAE AYALKTALVG PPGRKKEITR LPPWLKTAIP 

       130        140        150        160        170        180 
DSSNYKRIKN DLRGLNLHTV CEEARCPNIA DCWGGSSKSA ATATIMLMGD TCTRGCRFCS 

       190        200        210        220        230        240 
VKTSNKPPPL DPHEPDNTAE ALSRWGLGYV VLTSVDRDDL ADGGARHFAE TVMKIKQKAP 

       250        260        270        280        290        300 
NILVECLTGD YAGDLDMVAL VANSGLDVFA HNVETVEALT PFVRDRRASF QQSLRVLKAA 

       310        320        330        340        350        360 
KAAKPELITK TSLMLGLGET EAQLWDALRA LRAINVDVVT FGQYMRPTKR HMAVHEYVRP 

       370        380        390        400        410        420 
DVFDLWKERA LEMGFLYCAS GPLVRSSYKA GEAFIENVLK KRRGENAGSV NEKVTTSENV 

       430 
KKLVAGEAMM 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG663376 Genomic DNA. Translation: EEH03564.1.

3D structure databases

ProteinModelPortalC0NXP6.
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]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_AJECG
AccessionPrimary (citable) accession number: C0NXP6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 30 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