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Q7SF84 (LIPA_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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:NCU00565
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

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)
   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 – 2929Mitochondrion Potential
Chain30 – 430401Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398275

Sites

Metal binding1421Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1531Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1731Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1771Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1801Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7SF84 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 74795BCD7AD9FCCE

FASTA43046,902
        10         20         30         40         50         60 
MASPVPIQRL QAPLRRSLAR AAALSTRSYA TIPSGPSSQP TSQESSSAAS ASAPATKPRP 

        70         80         90        100        110        120 
TYFKDTTLAS LDDFIANQSS AAPLAPSEAY TLRTAEVGPA GKKRTITRLP EWLKTPIPSA 

       130        140        150        160        170        180 
GANPEFAKIK ADLRGLNLHT VCEEARCPNI GECWGGSNKA AATATIMLMG DTCTRGCRFC 

       190        200        210        220        230        240 
SVKTSRKPPP LDPHEPENTA EALARWGLGY VVLTSVDRDD LADGGARHFA ETIRRIKQKK 

       250        260        270        280        290        300 
PTLLVEALTG DFAGDLDMVK IVAESGLDVY AHNVETVENL TPYVRDRRAT FRQSLKVLEH 

       310        320        330        340        350        360 
VKKVRGKEGI ITKTSIMLGL GETEEELWEA LRELRKVDVD VVTFGQYMRP TKRHLAVEKY 

       370        380        390        400        410        420 
ITPDEFELWR QRALDMGFLY CASGPLVRSS YKAGEAFIEN VLRKRSGEKV VSEALGQAVA 

       430 
AEEATSVQSS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM002236 Genomic DNA. Translation: EAA35490.1.
RefSeqXP_964726.1. XM_959633.2.
UniGeneNcr.16964.

3D structure databases

ProteinModelPortalQ7SF84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU00565.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000000796; EFNCRP00000000796; EFNCRG00000000796.
GeneID3880875.
KEGGncr:NCU00565.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
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_NEUCR
AccessionPrimary (citable) accession number: Q7SF84
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 73 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