C3Y3G4 (LIAS_BRAFL) 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

ORF Names:

BRAFLDRAFT_125969

Organism

Branchiostoma floridae (Florida lancelet) (Amphioxus) [Reference proteome]

Taxonomic identifier

7739 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Cephalochordata › Branchiostomidae › Branchiostoma

Protein attributes

Sequence length	376 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	Mitochondrion By similarity HAMAP-Rule MF_03123.
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 Reference proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	mitochondrion 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 376		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000398213
Sites
	Metal binding	102	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	107	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	113	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	133	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	137	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	140	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C3Y3G4 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 9B44DD05AF6265F9	FASTA	376	41,818
	10 20 30 40 50 60 MATCLLMSTF TFIRCSVLKW GSGSSLPQEQ KEKITKGPGL GDFISGEVES TDSWEDYMGK 70 80 90 100 110 120 LRLEKGDKRL RLPPWLKKEI PIGKNYHSLK GTLRELNLAT VCEEAKCPNI GECWGGGEDK 130 140 150 160 170 180 TATATIMVMG DTCTRGCRFC SVKTARSPPP LDPNEPVHTA EAISRWGVDY IVITSVDRDD 190 200 210 220 230 240 VADGGSAHFS ECVKEIKKRI PSMLVECLTP DFRGDMEAVA TVAQSGLDVF AHNIETVKRL 250 260 270 280 290 300 TPFVRDPRAK YDQSLQVLSH VKKTVPDMVT KSSIMLGLGE TDQEVRTAME DLRRAGVDCL 310 320 330 340 350 360 TLGQYMQPTK RHLKVQEYVT PTKFKHWEEV GGEMGFAYTA SGPLVRSSYR AGEFYIKNLL 370 NKKRTEATLD TSSQES

References

[1]

"The amphioxus genome and the evolution of the chordate karyotype." Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U., Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K., Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J. , Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H., Satoh N., Rokhsar D.S. Nature 453:1064-1071(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S238N-H82. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG666483 Genomic DNA. Translation: EEN65231.1.
RefSeq	XP_002609221.1. XM_002609175.1.
UniGene	Bfl.339.
3D structure databases
ProteinModelPortal	C3Y3G4.
ModBase	Search...
Protein-protein interaction databases
STRING	7739.JGI125969.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7219245.
KEGG	bfo:BRAFLDRAFT_125969.
Phylogenomic databases
eggNOG	COG0320.
KO	K03644.
OMA	EEYVTPE.
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]
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_BRAFL

Accession

Primary (citable) accession number: C3Y3G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	July 28, 2009
Last modified:	April 3, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program