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A5ABM5 (LIPA_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:An11g09760
OrganismAspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]
Taxonomic identifier425011 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length416 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 – 3333Mitochondrion Potential
Chain34 – 416383Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398255

Sites

Metal binding1331Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1441Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1641Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1681Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1711Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5ABM5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F5F6F7FE2537C5AB

FASTA41645,541
        10         20         30         40         50         60 
MAAASTNRLR LLYTSTRASL PQSTPSILTT RTYATTDSST SATSTPKPRR RTAFTDKLNA 

        70         80         90        100        110        120 
GPSFGDFVSG NNDNAPLIDP SEAYALETAL VGPAGRKKQM TRLPPWLKTP IPDSKNYQRL 

       130        140        150        160        170        180 
KKDLRGLNLH TVCEEARCPN ISDCWGGGDK AAATATIMLM GDTCTRGCSF CSVKTSRRPA 

       190        200        210        220        230        240 
ALDPHEPENT AEAISRWGLG YVVLTSVDRD DLADGGARHF AETVRKIKSK APSTLVECLT 

       250        260        270        280        290        300 
GDYRGDLDMV ALVANSGLDV YAHNIETVEA LTPRVRDRRA TFKQSIAVLE AAKKANPEVI 

       310        320        330        340        350        360 
TKSSLMLGLG ETEEQLEHAL AQLRAVDVDV VTFGQYMRPT KRHMAVHEYV HPRWFEHWQR 

       370        380        390        400        410 
RAEELGFLYC ASGPLVRSSY KAGEAFIENV LKKRRAGVSD AVAEKKVAAA VDEAAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM270251 Genomic DNA. Translation: CAK97060.1.
RefSeqXP_001394934.1. XM_001394897.2.

3D structure databases

ProteinModelPortalA5ABM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5061.CADANGAP00009116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANGAT00009293; CADANGAP00009116; CADANGAG00009293.
GeneID4985192.
KEGGang:ANI_1_2510094.

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_ASPNC
AccessionPrimary (citable) accession number: A5ABM5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 44 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