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D0A0G6 (LIPA_TRYB9) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 21. 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:TbgDal_X18270
OrganismTrypanosoma brucei gambiense (strain MHOM/CI/86/DAL972) [Complete proteome]
Taxonomic identifier679716 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length409 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? – 409Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398240

Sites

Metal binding1251Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1301Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
D0A0G6 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: C622CA44663B9186

FASTA40945,476
        10         20         30         40         50         60 
MFQRWSFALC RPIVAAAQVS QQQVPPSEEP RNESGAANPP LVKEEFLRQF RERLANDKTG 

        70         80         90        100        110        120 
RNSLEGFLDL PENLPPTAAS IGPLKRGKEP LPPWLKLKVP MGASRQPRFN KIRRNMREKR 

       130        140        150        160        170        180 
LATVCEEAKC PNIGECWGGG DEEGDGTATA TIMVMGAHCT RGCRFCSVMT SRTPPPLDPE 

       190        200        210        220        230        240 
EPRKTADAVA DMGVEYIVMT MVDRDDLADG GAAHVVRCVT AVKERNPGLL LEALVGDFHG 

       250        260        270        280        290        300 
DLKLVEMVAG SPLNVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNNF TKGAMLTKSS 

       310        320        330        340        350        360 
IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPSRTRL KVSRYAHPKE FEMWEKEALD 

       370        380        390        400 
MGFLYCASGP MVRSSYRAGE YYIKNILKQR ETVEAPSVSD GGNEPKDSE 

« Hide

References

[1]"The genome sequence of Trypanosoma brucei gambiense, causative agent of chronic human african trypanosomiasis."
Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A., Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W., Barry J.D., Berriman M., Hertz-Fowler C.
PLoS Negl. Trop. Dis. 4:E658-E658(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MHOM/CI/86/DAL972.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FN554973 Genomic DNA. Translation: CBH16724.1.

3D structure databases

ProteinModelPortalD0A0G6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_TRYB9
AccessionPrimary (citable) accession number: D0A0G6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 24, 2009
Last modified: June 11, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways