A4RZ86 (LIAS_OSTLU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase, mitochondrial
EC=2.8.1.8

Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase

Gene names

Name:	LIP1
ORF Names:	OSTLU_32294

Organism

Ostreococcus lucimarinus (strain CCE9901) [Complete proteome]

Taxonomic identifier

436017 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Chlorophyta › Mamiellophyceae › Mamiellales › Ostreococcus › Ostreococcus 'lucimarinus'

Protein attributes

Sequence length	399 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_03128
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_03128
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_03128
Subcellular location	Mitochondrion Potential HAMAP-Rule MF_03128.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate synthase activity Inferred from electronic annotation. Source: EC 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
	Transit peptide	1 – 30	30	Mitochondrion Potential
	Chain	31 – 399	369	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398850
Sites
	Metal binding	131	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	136	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	142	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	162	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	166	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	169	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4RZ86 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 2D648EC52BE8F0E5	FASTA	399	43,907
	10 20 30 40 50 60 MRAVLELTRR RARNARFARA RAVVGARARA ADAQELRDDS KGGSSVDKAT STAAEARETA 70 80 90 100 110 120 HTLEGFREAL RHGPGFDDFV RGDVAYSVPA PKSLKDKTTR KPAWLKREVP GGERYTEIKS 130 140 150 160 170 180 KLRELKLATV CEEAKCPNLG ECWGGGDGKT ATATIMIMGD TCTRGCRFCA VKTAKAPPPL 190 200 210 220 230 240 DKDEPANVSK AIAAWGLDYV VLTSVDRDDI EDQGAGHFRE TVQRLKASCD VLVEALTPDF 250 260 270 280 290 300 RGEKHLVELV ATSGLDVFAH NVETVPELQR DVRDRRANWD QSIEVLKHAK KSGAKITKTS 310 320 330 340 350 360 IMLGLGETHE QVVNALKLLR EADVDVVTFG QYMRPTKKHL AVVEYVTPEA FKRYQEIAEE 370 380 390 MGFLYVASGA MVRSSYKAGE FFLANVIKQR KAKEAAAAN

References

[1]

"The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation." Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., Manuell A. , Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., Van de Peer Y., Moreau H., Grigoriev I.V. Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CCE9901.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000586 Genomic DNA. Translation: ABO96579.1.
RefSeq	XP_001418286.1. XM_001418249.1.
3D structure databases
ProteinModelPortal	A4RZ86.
ModBase	Search...
Protein-protein interaction databases
STRING	436017.A4RZ86.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5002530.
KEGG	olu:OSTLU_32294.
Phylogenomic databases
eggNOG	COG0320.
KO	K03644.
OMA	DPHEPQR.
ProtClustDB	PLN02428.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_03128. Lipoyl_synth_plantM.
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]
PIRSF	PIRSF005963. Lipoyl_synth. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LIAS_OSTLU

Accession

Primary (citable) accession number: A4RZ86

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	May 15, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program