Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, apicoplast

Gene

lipA

Organism
Plasmodium yoelii yoelii
Status
Reviewed-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 bindingi192Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi197Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi203Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi218Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi222Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi225Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-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:PY06208
OrganismiPlasmodium yoelii yoelii
Taxonomic identifieri73239 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Vinckeia)
Proteomesi
  • UP000008553 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiPlasmoDB:PY06208

Subcellular locationi

  • apicoplast UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Apicoplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16UniRule annotationAdd BLAST16
ChainiPRO_000039823317 – 502Lipoyl synthase, apicoplastAdd BLAST486

Proteomic databases

PRIDEiQ7RBD6

Interactioni

Protein-protein interaction databases

STRINGi352914.XP_726810.1

Structurei

3D structure databases

ProteinModelPortaliQ7RBD6
SMRiQ7RBD6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
InParanoidiQ7RBD6

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
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q7RBD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFLVLFFSY SIFVLPYSIL VYGISKDRKC CEYGNSVDSS KILYIAGSVR
60 70 80 90 100
KRRKTFEKKI NVSNFEREGN ANGYKHIDNK GIYATKQNLE FDEARNKEAN
110 120 130 140 150
ENNKNDATTV NRKIIIESEN KNNHNNQEQN IKDCYTNENA QNDEKNKKVK
160 170 180 190 200
IPKVGNAMPE KKPDWFHVPA PNGEKYKKLK SDLGKLKLHT VCEEAQCPNI
210 220 230 240 250
GECWNIGTAT IMLLGDTCTR GCKFCSIKTS SKPPPPDINE PFNTAKAICE
260 270 280 290 300
WDINYIVITS VDRDDLPDGG ADHFAKTVEL IKFSKPSILI ECLVSDFQGN
310 320 330 340 350
IDSIKRLALS GLDVYAHNIE TVKRLQKYVR DKRANYEQSL YVLKKAKEIN
360 370 380 390 400
PNLYTKTSIM LGLGETQDEV LQTMKDARSN DIDVITFGQY LRPTKNHLNV
410 420 430 440 450
VEYISPQMFN YYKDVGLKMG FKYIASGPLV RSSYMAGEYF MKNMVEKGRN
460 470 480 490 500
QKNQQIKPVE LKLVTELDKL TECIQKEIKH REISVFIQVH AFLVNVFVLV

RA
Length:502
Mass (Da):57,463
Last modified:December 15, 2003 - v1
Checksum:i77AD72396A80E94D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABL01002075 Genomic DNA Translation: EAA18375.1

Genome annotation databases

EnsemblProtistsiEAA18375; EAA18375; EAA18375

Similar proteinsi

Entry informationi

Entry nameiLIPA_PLAYO
AccessioniPrimary (citable) accession number: Q7RBD6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: December 15, 2003
Last modified: May 23, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health