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

C5GPL2 (LIPA_AJEDR) 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:BDCG_05907
OrganismAjellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis) [Complete proteome]
Taxonomic identifier559297 [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
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 – 430393Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398248

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
C5GPL2 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 920ED93E44FE430D

FASTA43046,750
        10         20         30         40         50         60 
MAASTGKLRT LFSAHSSLSA RPSSALPALR LTILRSYATT TPPDSSISDP SNSSTTVKRP 

        70         80         90        100        110        120 
PTAFKDKLNA GPAFSDFVSG KKDEPLDPAE AYALKTALVG PAGRKKEITR LPSWLKTPIP 

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

       190        200        210        220        230        240 
VKTSNKPPPL DPHEPENTAE ALSRWGLGYV VLTSVDRDDL ADGGARHFAE TVLKIKQKAP 

       250        260        270        280        290        300 
NILVECLTGD YAGDLEMVAL VANSGLDVYA HNVETVEALT PFVRDRRATF QQSLRVLKAA 

       310        320        330        340        350        360 
KATKPELITK TSLMLGLGET EAQLWDTLRA LRAIDVDVVT FGQYMRPTKR HMAVHEYVRP 

       370        380        390        400        410        420 
DVFDMWKERA LEMGFLYCAS GPLVRSSYKA GEAFIENVLK KKRGKNVGSA SGKGTTSENV 

       430 
EKLVAGEAVR 

« Hide

References

[1]"The genome sequence of Blastomyces dermatitidis strain ER-3."
Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N., Sykes S. expand/collapse author list , Galagan J.E., Nusbaum C., Birren B.W.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ER-3 / ATCC MYA-2586.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ999978 Genomic DNA. Translation: EEQ90787.1.

3D structure databases

ProteinModelPortalC5GPL2.
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_AJEDR
AccessionPrimary (citable) accession number: C5GPL2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 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