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B0CQH8 (LIPA_LACBS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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:LACBIDRAFT_181332
OrganismLaccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor) [Complete proteome]
Taxonomic identifier486041 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesTricholomataceaeLaccaria

Protein attributes

Sequence length390 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 – 1919Mitochondrion Potential
Chain20 – 390371Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123
PRO_0000398269

Sites

Metal binding981Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1031Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1091Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1431Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CQH8 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 2A065A3789CD906B

FASTA39042,676
        10         20         30         40         50         60 
MPTLLRILRP PRSPFTRCLA TFATPSSSGS SSRSKFTESL ETGPGLDDFI SEEVPDRVVL 

        70         80         90        100        110        120 
GNTKGPRLPS YLKTSIPSGA SFNKIKKDLR GLGLHTVCEE ARCPNIGDCW GGKPGATEAE 

       130        140        150        160        170        180 
GRSAATATIM LMGDTCTRGC RFCSVKTSRT PPPLDPHEPE NTAEAISRWG LGYIVLTSVD 

       190        200        210        220        230        240 
RDDLLDGGAH HFAETIRKIK YKAPQILVEA LTGDFAGSLD HVSIVAQSGL DVYAHNIETV 

       250        260        270        280        290        300 
EELTPFVRDR RATFRQSLKV LEHAKKSGVR ITKTSIMLGV GETKEQVLAA LKELRKIDVD 

       310        320        330        340        350        360 
VVTFGQYMRP TKRHMKVDRY VEPAEFDNWK EVAENLGFLY VASGPLVRSS YKAGEFYIEN 

       370        380        390 
VLRGKNKAIG GLGISQLEGS EKGSMTGIDR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS547091 Genomic DNA. Translation: EDR15648.1.
RefSeqXP_001873856.1. XM_001873821.1.

3D structure databases

ProteinModelPortalB0CQH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING29883.JGI181332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6069333.
KEGGlbc:LACBIDRAFT_181332.

Phylogenomic databases

eggNOGCOG0320.
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_LACBS
AccessionPrimary (citable) accession number: B0CQH8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 32 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