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C5PIN8 (LIPA_COCP7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 26. 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:CPC735_057610
OrganismCoccidioides posadasii (strain C735) (Valley fever fungus) [Complete proteome]
Taxonomic identifier222929 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length419 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)
   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 – 2626Mitochondrion Potential
Chain27 – 419393Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398263

Sites

Metal binding1361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1411Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1741Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C5PIN8 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: E41CAE42605B6DEF

FASTA41945,766
        10         20         30         40         50         60 
MAVCAGRLKC FGNPAVSLRT AASRAYATTT SPDPAIPSSS SASSSSALPK RPQTSFRDKL 

        70         80         90        100        110        120 
NAGPSFSDFL SGGNRDDARI LDPNEAYALK TALVGPKGKK KEITRLPSWL KTSIPDSNNY 

       130        140        150        160        170        180 
KRIKNDLRGL GLHTVCEEAR CPNISECWGG SSKSAATATI MLMGDTCTRA CRFCSVKTSK 

       190        200        210        220        230        240 
TPPPLDPHEP ENTAEALSRW GLGYVVLTTV DRDDLIDGGA RHFAETVIRI KQKAPNILVE 

       250        260        270        280        290        300 
CLTGDYAGDL EMVALMAKSG LDVYAHNVET VEALTPHVRD RRANFQTSLR VLKAAKAAVP 

       310        320        330        340        350        360 
SLITKTSMML GLGETEEQMW DALRQLRAAN VDVVTFGQYM RPTKRHMPVH EYVRPDVFEL 

       370        380        390        400        410 
WKDRALEMGF LYCASGPLVR SSYKAGEAFI ENVLKKRRAE STGPESTNVP NVTPDAIVR 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C735.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACFW01000049 Genomic DNA. Translation: EER24391.1.
RefSeqXP_003066536.1. XM_003066490.1.
UniGeneCpo.6500.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222929.C5PIN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9692006.
KEGGcpw:CPC735_057610.

Phylogenomic databases

eggNOGCOG0320.
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]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_COCP7
AccessionPrimary (citable) accession number: C5PIN8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 26 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