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Q7RBD6 (LIPA_PLAYO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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, 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
ORF Names:PY06208
OrganismPlasmodium yoelii yoelii [Reference proteome]
Taxonomic identifier73239 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

Protein attributes

Sequence length502 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

Plastidapicoplast By similarity HAMAP-Rule MF_03123.

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
   Technical termComplete proteome
Reference proteome
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 – 1616 Potential
Chain17 – 502486Lipoyl synthase, apicoplast HAMAP-Rule MF_03123
PRO_0000398233

Sites

Metal binding1921Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1971Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2031Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2181Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2221Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2251Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7RBD6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 77AD72396A80E94D

FASTA50257,463
        10         20         30         40         50         60 
MNFLVLFFSY SIFVLPYSIL VYGISKDRKC CEYGNSVDSS KILYIAGSVR KRRKTFEKKI 

        70         80         90        100        110        120 
NVSNFEREGN ANGYKHIDNK GIYATKQNLE FDEARNKEAN ENNKNDATTV NRKIIIESEN 

       130        140        150        160        170        180 
KNNHNNQEQN IKDCYTNENA QNDEKNKKVK IPKVGNAMPE KKPDWFHVPA PNGEKYKKLK 

       190        200        210        220        230        240 
SDLGKLKLHT VCEEAQCPNI GECWNIGTAT IMLLGDTCTR GCKFCSIKTS SKPPPPDINE 

       250        260        270        280        290        300 
PFNTAKAICE WDINYIVITS VDRDDLPDGG ADHFAKTVEL IKFSKPSILI ECLVSDFQGN 

       310        320        330        340        350        360 
IDSIKRLALS GLDVYAHNIE TVKRLQKYVR DKRANYEQSL YVLKKAKEIN PNLYTKTSIM 

       370        380        390        400        410        420 
LGLGETQDEV LQTMKDARSN DIDVITFGQY LRPTKNHLNV VEYISPQMFN YYKDVGLKMG 

       430        440        450        460        470        480 
FKYIASGPLV RSSYMAGEYF MKNMVEKGRN QKNQQIKPVE LKLVTELDKL TECIQKEIKH 

       490        500 
REISVFIQVH AFLVNVFVLV RA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABL01002075 Genomic DNA. Translation: EAA18375.1.
RefSeqXP_726810.1. XM_721717.1.

3D structure databases

ProteinModelPortalQ7RBD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING73239.Q7RBD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3792150.
KEGGpyo:PY06208.

Organism-specific databases

EuPathDBPlasmoDB:PY06208.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.

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_PLAYO
AccessionPrimary (citable) accession number: Q7RBD6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 61 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