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C7Z527 (LIPA_NECH7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 31. 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:NECHADRAFT_66689
OrganismNectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi) [Reference proteome]
Taxonomic identifier660122 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaemitosporic NectriaceaeFusariumFusarium solani species complex

Protein attributes

Sequence length412 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)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: EnsemblFungi

   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 – 2828Mitochondrion Potential
Chain29 – 412384Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398273

Sites

Metal binding1241Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1291Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1351Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1551Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1621Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C7Z527 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 18E930BB46989CFE

FASTA41245,389
        10         20         30         40         50         60 
MASIAPSLKR AHAPLRKALT ASSTIRAFAT VPPTSSETTK PKRKSYFKDT TVAEFSDFLA 

        70         80         90        100        110        120 
TSSPAQPLSP AEAFTLRTAE VGPEGKKRTI TRLPEWLKTP IPAGNDNFKS IKKDLRGLGL 

       130        140        150        160        170        180 
HTVCEEARCP NISECWGGSD KNAATATIML MGDTCTRGCR FCSVKTNRKP AALDPHEPEN 

       190        200        210        220        230        240 
TAEALARWGL GYVVLTSVDR DDLADGGAHH FAETIRRIKQ KKPSLLVEAL TGDFRGDLDM 

       250        260        270        280        290        300 
VKVVAESGLD VYAHNVETVE DLTPYVRDRR ATFRQSLSVL KHVKEVKGKE GIITKTSLML 

       310        320        330        340        350        360 
GLGEQEHEVM AALEDLRKAD VDVVTFGQYM RPTKRHLKVE KYVTPDEFEM WNKRALDMGF 

       370        380        390        400        410 
LYCASGPLVR SSYKAGEAFI ENVLRKRSGE KAMARGTLAK AVALDSETRS SI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG698910 Genomic DNA. Translation: EEU40447.1.
RefSeqXP_003046160.1. XM_003046114.1.

3D structure databases

ProteinModelPortalC7Z527.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiNechaT66689; NechaP66689; NechaG66689.
GeneID9678266.
KEGGnhe:NECHADRAFT_66689.

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

Entry information

Entry nameLIPA_NECH7
AccessionPrimary (citable) accession number: C7Z527
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 13, 2009
Last modified: February 19, 2014
This is version 31 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