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A5K883 (LIPA_PLAVS) 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
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:PVX_083125
OrganismPlasmodium vivax (strain Salvador I) [Reference proteome]
Taxonomic identifier126793 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Plasmodium)

Protein attributes

Sequence length442 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 – 2525 Potential
Chain26 – 442417Lipoyl synthase, apicoplast HAMAP-Rule MF_03123
PRO_0000398232

Sites

Metal binding1771Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1881Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding2031Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2071Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding2101Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5K883 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 0EFA968BB12F4E3F

FASTA44250,317
        10         20         30         40         50         60 
MHVLTPSLYI YAFFIVCVRL KCGRSKRVAN AKHATYDMPP KGLRVRDMLE KTAQQNCNQR 

        70         80         90        100        110        120 
KRGKCRKFFF LWKMDKMGDT HLGGQANGRK NLLRSESATD EASLGGNPLK EKLKESPANW 

       130        140        150        160        170        180 
GKDKQEEQQS TDRLPLPKVG NKMPEKKPDW FHVPAPTGKK YNELKADLKK LKLHTVCEEA 

       190        200        210        220        230        240 
QCPNIGECWN IGTATIMLLG DTCTRGCKFC SIKTSSKPLP PDANEPFNTA KAICEWDINY 

       250        260        270        280        290        300 
VVLTSVDRDD LPDGGASHFA KTIELIKFSR PEILIECLVS DFQGNVDSIR KLANSGMEVY 

       310        320        330        340        350        360 
AHNIETVRRL QKFVRDRRAN YEQSLWVLKT AKEINPLLYT KTSIMLGLGE TKQEVLQAMA 

       370        380        390        400        410        420 
DVRQNNIDVI TFGQYLRPTK NHLNVVEYVS PQMFDYYKEE GMKMGFKYIA SGPLVRSSYK 

       430        440 
AGEYFMKNLV EQRRGVKLHA EG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAKM01000009 Genomic DNA. Translation: EDL44497.1.
RefSeqXP_001614224.1. XM_001614174.1.

3D structure databases

ProteinModelPortalA5K883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5855.PVX_083125.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5473509.
KEGGpvx:PVX_083125.

Organism-specific databases

EuPathDBPlasmoDB:PVX_083125.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
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_PLAVS
AccessionPrimary (citable) accession number: A5K883
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 10, 2007
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