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A7EV21 (LIPA_SCLS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:SS1G_09179
OrganismSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum) [Reference proteome]
Taxonomic identifier665079 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia

Protein attributes

Sequence length409 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 – 3434Mitochondrion Potential
Chain35 – 409375Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398292

Sites

Metal binding1301Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1351Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1411Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1611Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1651Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1681Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A7EV21 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 8EA97891D4BC7425

FASTA40945,637
        10         20         30         40         50         60 
MASIVPRFRC LNAPPLRQTS RNILAIPTAT SRSFATEIDV SKPTPIVKRR PTYFKDKINA 

        70         80         90        100        110        120 
VPSFSEFVGL PEKAFTPEDA LELRTAMVGP PGKKRQITRL PEWLKTPIPD NSNYKKIKKD 

       130        140        150        160        170        180 
LRGLNLHTVC EEARCPNISD CWGGSDKSAA TATIMLMGDT CTRGCRFCSV KTSKAPPPLD 

       190        200        210        220        230        240 
PHEPEHTAEA LSRWGLGYVV LTSVDRDDLA DGGARHFAET IMKIKQKKSS ILVEALTGDY 

       250        260        270        280        290        300 
GGDLEMVKLV AESGLDVYAH NMETTEELTP FVRDRRAKYR QSLKVLEAAK KAKPSLITKT 

       310        320        330        340        350        360 
SIMLGLGETE EALWQALRDL REVDVDVVTF GQYMRPTKRH MKVEEYVTPE VFEIWRQRAL 

       370        380        390        400 
DLGFLYCASG PLVRSSYKAG EAFIENVLKK RKGVTILSDE ATGMDKAIV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476633 Genomic DNA. Translation: EDN93313.1.
RefSeqXP_001589458.1. XM_001589408.1.

3D structure databases

ProteinModelPortalA7EV21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING665079.A7EV21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEDN93313; EDN93313; SS1G_09179.
GeneID5485857.
KEGGssl:SS1G_09179.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAEEYVTPE.
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_SCLS1
AccessionPrimary (citable) accession number: A7EV21
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 42 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