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Q6CLS2 (LIPA_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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
Ordered Locus Names:KLLA0F00836g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length370 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 By similarity 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 – ?Mitochondrion Potential
Chain? – 370Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398268

Sites

Metal binding1041Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1091Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1351Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1391Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1421Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CLS2 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 86A501949025496B

FASTA37041,470
        10         20         30         40         50         60 
MLKPGIRSVQ KRFITETVVR STQPSVSRRR KTTHFTDKLN KGPSFEDFVN GNAQKFTLDP 

        70         80         90        100        110        120 
LEKARQNSEE VQRLPTWLKV PIAKGSNFHK LKNDVKELKL STVCEEAKCP NIGECWGGGD 

       130        140        150        160        170        180 
KSKATATIML LGDTCTRGCR FCSVKTNRKP SAPDPTEPEN TAEAISRWGL GYVVLTTVDR 

       190        200        210        220        230        240 
DDLVDGGAYH LAETVQKIKQ KAPNILVETL SGDFRGDLEM VKVMALSGLD VYAHNMETVE 

       250        260        270        280        290        300 
ALTPHVRDRR ATYRQSLSVL ECAKKTVPTL VTKTSVMLGL GETDEQVLQT MKDLRAIGCD 

       310        320        330        340        350        360 
VITFGQYMRP TKRHMKVVEY VTPEKFDYWK QKALELGFLY CASGPLVRSS YKAGESFIEN 

       370 
VLRGRSRARI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382126 Genomic DNA. Translation: CAG97824.1.
RefSeqXP_455117.1. XM_455117.1.

3D structure databases

ProteinModelPortalQ6CLS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.Q6CLS2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2895837.
KEGGkla:KLLA0F00836g.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
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_KLULA
AccessionPrimary (citable) accession number: Q6CLS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: August 16, 2004
Last modified: February 19, 2014
This is version 68 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