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A5DGI1 (LIPA_PICGU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:PGUG_02382
OrganismMeyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]
Taxonomic identifier294746 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeMeyerozyma

Protein attributes

Sequence length385 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)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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? – 385Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398281

Sites

Metal binding1071Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1181Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5DGI1 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: F348661FA3522D91

FASTA38543,175
        10         20         30         40         50         60 
MVPVRGQITA FRCSQNPTKT IWRTLATAEP PKPKRKRTMF TDKLNQGPSF ADFVSGKASN 

        70         80         90        100        110        120 
MTIDPLEAAR QDPDQRLPSW LKVPIPKGKS FHTLKKDVRE LKLATVCEEA KCPNIGECWG 

       130        140        150        160        170        180 
GKKSEATATI MLMGDTCTRG CRFCSVKTSR KPAPPDPMEP ENTAEAISRW GLGYVVLTTV 

       190        200        210        220        230        240 
DRDDLVDGGA HHLAETVRKI KEKAPQILVE VLGGDFRGDL DMASVLARSG LDVYAHNIET 

       250        260        270        280        290        300 
VEDLTPHVRD RRATYRQSLS ILQRAKETKP SLVTKTSMML GFGETDEQIM QTLRDLREIK 

       310        320        330        340        350        360 
CDVVTFGQYM RPTKRHMKVV EYVTPEKFDY WRDTALKMGF LYVASGPLVR SSYKAGEAFI 

       370        380 
ENVIRKRNHN VGETPRLESA SAAQL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408157 Genomic DNA. Translation: EDK38284.2.
RefSeqXP_001484653.1. XM_001484603.1.

3D structure databases

ProteinModelPortalA5DGI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4929.A5DGI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5126776.
KEGGpgu:PGUG_02382.

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_PICGU
AccessionPrimary (citable) accession number: A5DGI1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 22, 2008
Last modified: June 11, 2014
This is version 44 of the entry and version 2 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