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Q86G50 (LIPA_TOXGO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipoyl synthase, apicoplast

EC=2.8.1.8
Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase
Gene names
Name:lipA
OrganismToxoplasma gondii
Taxonomic identifier5811 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaConoidasidaCoccidiaEucoccidioridaEimeriorinaSarcocystidaeToxoplasma

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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. Ref.1

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

Plastidapicoplast Ref.1.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentApicoplast
Plastid
   DomainSignal
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentapicoplast

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

Signal peptide1 – 6363 Potential
Chain64 – 543480Lipoyl synthase, apicoplast HAMAP-Rule MF_03123
PRO_0000398234

Sites

Metal binding2521Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2571Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2631Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2781Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2821Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2851Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q86G50 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1DDCD0A1150680E6

FASTA54358,706
        10         20         30         40         50         60 
MAYFFDFPTD TWVEDASPGG PPKRAFGHGL AAGSSHFASP VSRRRLPTIT ALLLFSLLSA 

        70         80         90        100        110        120 
SQSGALSVSQ CSRRVSLGPL LSRVSSVSCT PSAAASALAS SLYPTDSLSS VEGSVAPRPP 

       130        140        150        160        170        180 
PSSLAFVLRR VPPAAYSSSL SPSVLRFKHS LPRPLQGSLV CAPGILGGAA GSARFAGCCG 

       190        200        210        220        230        240 
SQGRSCGSGK NPELPLKGSK DEVIPRVGTS TAGPRPDWFH VPAPQAASRG AEESRYQQLQ 

       250        260        270        280        290        300 
KQIRGLDLHT VCEEAKCPNI GECWNGGTAT LILLGDTCTR GCRFCAIKTS SKPPPPDPLE 

       310        320        330        340        350        360 
PEKVADAVAK WDIDYVVMTS VDRDDMPDGG AGHFARTVQL VKKAKPSMLI ECLVSDFQGM 

       370        380        390        400        410        420 
EESVRTLAQS GLDVYAHNIE TVRRLTPYVR DKRAKYDQSL RVLHLAKQFN PSLFTKSSIM 

       430        440        450        460        470        480 
LGLGETSEEV VRTLRDLRDH DVDVVTLGQY LRPTKQQLGV VEYVTPETFK KYQDIAEEMG 

       490        500        510        520        530        540 
FKYVASGPLV RSSYKAGEYY MKHLIDDARK HGRRETVKQV KLEADVGTLK GTTTTFQVNE 


KEA 

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References

[1]"Apicomplexan parasites contain a single lipoic acid synthase located in the plastid."
Thomsen-Zieger N., Schachtner J., Seeber F.
FEBS Lett. 547:80-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
Strain: RH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ556158 mRNA. Translation: CAD88789.1.

3D structure databases

ProteinModelPortalQ86G50.
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]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_TOXGO
AccessionPrimary (citable) accession number: Q86G50
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 48 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