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Protein

Lipoyl synthase, apicoplast

Gene

lipA

Organism
Plasmodium vivax (strain Salvador I)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi182 – 1821Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi188 – 1881Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi203 – 2031Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi207 – 2071Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi210 – 2101Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, apicoplastUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:lipAUniRule annotation
ORF Names:PVX_083125
OrganismiPlasmodium vivax (strain Salvador I)
Taxonomic identifieri126793 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Plasmodium)
ProteomesiUP000008333: Chromosome 12, UP000008333: Unassembled WGS sequence

Organism-specific databases

EuPathDBiPlasmoDB:PVX_083125.

Subcellular locationi

Plastidapicoplast UniRule annotation

GO - Cellular componenti

  1. apicoplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Apicoplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525UniRule annotationAdd
BLAST
Chaini26 – 442417Lipoyl synthase, apicoplastPRO_0000398232Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5855.PVX_083125.

Structurei

3D structure databases

ProteinModelPortaliA5K883.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiA5K883.
KOiK03644.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5K883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHVLTPSLYI YAFFIVCVRL KCGRSKRVAN AKHATYDMPP KGLRVRDMLE
60 70 80 90 100
KTAQQNCNQR KRGKCRKFFF LWKMDKMGDT HLGGQANGRK NLLRSESATD
110 120 130 140 150
EASLGGNPLK EKLKESPANW GKDKQEEQQS TDRLPLPKVG NKMPEKKPDW
160 170 180 190 200
FHVPAPTGKK YNELKADLKK LKLHTVCEEA QCPNIGECWN IGTATIMLLG
210 220 230 240 250
DTCTRGCKFC SIKTSSKPLP PDANEPFNTA KAICEWDINY VVLTSVDRDD
260 270 280 290 300
LPDGGASHFA KTIELIKFSR PEILIECLVS DFQGNVDSIR KLANSGMEVY
310 320 330 340 350
AHNIETVRRL QKFVRDRRAN YEQSLWVLKT AKEINPLLYT KTSIMLGLGE
360 370 380 390 400
TKQEVLQAMA DVRQNNIDVI TFGQYLRPTK NHLNVVEYVS PQMFDYYKEE
410 420 430 440
GMKMGFKYIA SGPLVRSSYK AGEYFMKNLV EQRRGVKLHA EG
Length:442
Mass (Da):50,317
Last modified:July 10, 2007 - v1
Checksum:i0EFA968BB12F4E3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAKM01000009 Genomic DNA. Translation: EDL44497.1.
RefSeqiXP_001614224.1. XM_001614174.1.

Genome annotation databases

GeneIDi5473509.
KEGGipvx:PVX_083125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAKM01000009 Genomic DNA. Translation: EDL44497.1.
RefSeqiXP_001614224.1. XM_001614174.1.

3D structure databases

ProteinModelPortaliA5K883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5855.PVX_083125.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5473509.
KEGGipvx:PVX_083125.

Organism-specific databases

EuPathDBiPlasmoDB:PVX_083125.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiA5K883.
KOiK03644.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Salvador I.

Entry informationi

Entry nameiLIPA_PLAVS
AccessioniPrimary (citable) accession number: A5K883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 10, 2007
Last modified: March 4, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.