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C3Y3G4 (LIAS_BRAFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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:BRAFLDRAFT_125969
OrganismBranchiostoma floridae (Florida lancelet) (Amphioxus) [Reference proteome]
Taxonomic identifier7739 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCephalochordataBranchiostomidaeBranchiostoma

Protein attributes

Sequence length376 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
Reference 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? – 376Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398213

Sites

Metal binding1021Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1071Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1131Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1331Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1401Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
C3Y3G4 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 9B44DD05AF6265F9

FASTA37641,818
        10         20         30         40         50         60 
MATCLLMSTF TFIRCSVLKW GSGSSLPQEQ KEKITKGPGL GDFISGEVES TDSWEDYMGK 

        70         80         90        100        110        120 
LRLEKGDKRL RLPPWLKKEI PIGKNYHSLK GTLRELNLAT VCEEAKCPNI GECWGGGEDK 

       130        140        150        160        170        180 
TATATIMVMG DTCTRGCRFC SVKTARSPPP LDPNEPVHTA EAISRWGVDY IVITSVDRDD 

       190        200        210        220        230        240 
VADGGSAHFS ECVKEIKKRI PSMLVECLTP DFRGDMEAVA TVAQSGLDVF AHNIETVKRL 

       250        260        270        280        290        300 
TPFVRDPRAK YDQSLQVLSH VKKTVPDMVT KSSIMLGLGE TDQEVRTAME DLRRAGVDCL 

       310        320        330        340        350        360 
TLGQYMQPTK RHLKVQEYVT PTKFKHWEEV GGEMGFAYTA SGPLVRSSYR AGEFYIKNLL 

       370 
NKKRTEATLD TSSQES 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GG666483 Genomic DNA. Translation: EEN65231.1.
RefSeqXP_002609221.1. XM_002609175.1.
UniGeneBfl.339.

3D structure databases

ProteinModelPortalC3Y3G4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7739.JGI125969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7219245.
KEGGbfo:BRAFLDRAFT_125969.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAEEYVTPE.

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 nameLIAS_BRAFL
AccessionPrimary (citable) accession number: C3Y3G4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways