Q7RBD6 (LIPA_PLAYO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Plasmodium yoelii yoelii [Reference proteome]

Taxonomic identifier

73239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Vinckeia) › Plasmodium yoelii

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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 + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 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	Plastid › apicoplast By similarity.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Apicoplast Plastid
Domain	Signal
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	apicoplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 502	486	Lipoyl synthase, apicoplast HAMAP-Rule MF_03123		PRO_0000398233
Sites
	Metal binding	192	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	197	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	203	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	218	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	222	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	225	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7RBD6 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 77AD72396A80E94D	FASTA	502	57,463
	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

References

[1]

"Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii." Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C., Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M., Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E., Riedmuller S.B. , Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M., Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D., Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., Carucci D.J. Nature 419:512-519(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 17XNL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABL01002075 Genomic DNA. Translation: EAA18375.1.
RefSeq	XP_726810.1. XM_721717.1.
3D structure databases
ProteinModelPortal	Q7RBD6.
ModBase	Search...
Protein-protein interaction databases
STRING	73239.Q7RBD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3792150.
KEGG	pyo:PY06208.
Organism-specific databases
EuPathDB	PlasmoDB:PY06208.
Phylogenomic databases
eggNOG	COG0320.
KO	K03644.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR003698. Lipoyl_synth. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LIPA_PLAYO

Accession

Primary (citable) accession number: Q7RBD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	December 15, 2003
Last modified:	April 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)