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A1CJC4 (LIPA_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:ACLA_034510
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length415 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 – 415382Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398251

Sites

Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1431Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1671Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1701Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CJC4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: DE25AD5BD2982A90

FASTA41545,519
        10         20         30         40         50         60 
MAASTSHLRS LCSSTRSLSR SGVIVTPIAC RGYATTDPSP SATTPTPVRR RTTFKDKLNA 

        70         80         90        100        110        120 
GPSFSDFVSN GNDNAPLDPS EAYALKTALV GPAGRKKEMT RLPSWLKTPI PDSKNYQRLK 

       130        140        150        160        170        180 
KDLRGLNLHT VCEEARCPNI SDCWGGSDKS SATATIMLMG DTCTRGCRFC SVKTSRAPPP 

       190        200        210        220        230        240 
LDPHEPENTA EAISRWGLGY VVLTSVDRDD LVDGGARHFA ETVIKIKQKA PSILVECLTG 

       250        260        270        280        290        300 
DYAGDLDMVK LVARSGLDVY AHNVETVEAL TPQVRDRRAN FQQSLRVLDA AKKAQPTLIT 

       310        320        330        340        350        360 
KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT PDRFELWRQR 

       370        380        390        400        410 
ALEMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAASGGA ETIGERPVAV DEASR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027056 Genomic DNA. Translation: EAW09248.1.
RefSeqXP_001270674.1. XM_001270673.1.

3D structure databases

ProteinModelPortalA1CJC4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00003729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00003809; CADACLAP00003729; CADACLAG00003809.
GeneID4702900.
KEGGact:ACLA_034510.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAVQKYWTP.
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_ASPCL
AccessionPrimary (citable) accession number: A1CJC4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 45 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