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B4J3F3 (LIAS_DROGR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Name:Las
ORF Names:GH16746
OrganismDrosophila grimshawi (Fruit fly) (Idiomyia grimshawi) [Complete proteome]
Taxonomic identifier7222 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaHawaiian Drosophila

Protein attributes

Sequence length364 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? – 364Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398218

Sites

Metal binding991Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1041Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1301Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1341Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4J3F3 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 818C9B89D4E8459D

FASTA36441,106
        10         20         30         40         50         60 
MLRRLNSPTA ILVRTASTRT EKLEEIRDRL SKGPNFQDFI QNSDNSKDDF ENYDGKLRRE 

        70         80         90        100        110        120 
KGETQQLRLP PWLKTTIPMG KNYAKIKSQL RDLKLSTVCE EARCPNIGEC WGGGEHGTQT 

       130        140        150        160        170        180 
ATIMLMGDTC TRGCRFCSVK TARAPPPLDV NEPVNTAKAI SSWGLDYIVL TSVDRDDLPD 

       190        200        210        220        230        240 
GGSKHIAETV REIKARNSNI FVECLVPDFR GNLECVQTIA GCGLDVYAHN IETVEKLTPF 

       250        260        270        280        290        300 
VRDRRAHYRQ TLKVLNEAKQ FNPNLITKSS LMLGLGETDA EVEQTMLDLR EAGVECLTLG 

       310        320        330        340        350        360 
QYMQPTKRHL KVIEYVTPEK FKHWEQRGNE LGFLYTASGP LVRSSYKAGE FFITSILANR 


RKSV 

« Hide

References

[1]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 genomes consortium
Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tucson 15287-2541.00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH916366 Genomic DNA. Translation: EDV97252.1.
RefSeqXP_001984904.1. XM_001984868.1.

3D structure databases

ProteinModelPortalB4J3F3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7222.FBpp0150652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0152160; FBpp0150652; FBgn0124217.
GeneID6556978.
KEGGdgr:Dgri_GH16746.

Organism-specific databases

FlyBaseFBgn0124217. Dgri\GH16746.

Phylogenomic databases

eggNOGCOG0320.
InParanoidB4J3F3.
KOK03644.
OMAPEEPYNT.
OrthoDBEOG7P2XS7.
PhylomeDBB4J3F3.

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_DROGR
AccessionPrimary (citable) accession number: B4J3F3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase