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Protein

Lipoyl synthase, apicoplast

Gene

lipA

Organism
Plasmodium falciparum (isolate Dd2)
Status
Unreviewed-Annotation score: -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 N6-(octanoyl)lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyl synthase, apicoplast (lipA)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi153Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi158Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi164Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi179Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi183Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi186Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

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:PFDG_04038Imported
OrganismiPlasmodium falciparum (isolate Dd2)Imported
Taxonomic identifieri57267 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000054282 Componenti: Unassembled WGS sequence

Subcellular locationi

  • apicoplast UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei6 – 25HelicalSequence analysisAdd BLAST20

GO - Cellular componenti

Keywords - Cellular componenti

ApicoplastUniRule annotation, Membrane, Plastid

Structurei

3D structure databases

ProteinModelPortaliA0A0L7M871
SMRiA0A0L7M871
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini169 – 383Elp3InterPro annotationAdd BLAST215

Sequence similaritiesi

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

Keywords - Domaini

SignalUniRule annotation, Transmembrane, Transmembrane helixSequence analysis

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR007197 rSAM
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF005963 Lipoyl_synth, 1 hit
SFLDiSFLDF00271 lipoyl_synthase, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

A0A0L7M871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHFGIPSLFY LYILFSIIMR IKCVITKNLK KTKKRTCSYI PHGNMEKGII
60 70 80 90 100
LNYIEKPNPA YLKRGKNKNK NKNKKGDIYK LRNVEILLYA NRYVHEGNEN
110 120 130 140 150
FSSTTKKLLL TPKVGNKMPE GKKPDWFHVA APTVAKYNKL KDDIKKLNLH
160 170 180 190 200
TVCEEAQCPN IGECWNIGTA TIMLLGDTCT RGCKFCSIKT SSNPLPPDIN
210 220 230 240 250
EPFNTAKAIC EWNIDYVVLT SVDRDDLPDG GASHFAKTVE LVKFSRPDIL
260 270 280 290 300
IECLVSDFQG NIDSVRKLAF SGLDVYAHNI ETVKRLQKYV RDKRANYDQS
310 320 330 340 350
LFVLKTAKEI NPQLYTKTSI MLGLGETKEE VIQTMYDARK NNIDVITFGQ
360 370 380 390 400
YLRPTKNHLS IVQYISPQMF EYYKEEGLKM GFKYIASGPL VRSSYKAGEY
410
FIKNLVNQRN KDKKN
Length:415
Mass (Da):47,593
Last modified:November 11, 2015 - v1
Checksum:iFB6D7CE36D52E2C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GG701861 Genomic DNA Translation: KOB88998.1

Genome annotation databases

EnsemblProtistsiKOB88998; KOB88998; PFDG_04038

Similar proteinsi

Entry informationi

Entry nameiA0A0L7M871_PLAF4
AccessioniPrimary (citable) accession number: A0A0L7M871
Entry historyiIntegrated into UniProtKB/TrEMBL: November 11, 2015
Last sequence update: November 11, 2015
Last modified: July 18, 2018
This is version 17 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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