B3M996 (LIAS_DROAN) 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:	Las
ORF Names:	GF24134

Organism

Drosophila ananassae (Fruit fly) [Complete proteome]

Taxonomic identifier

7217 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › ananassae subgroup › ananassae species complex

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.
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)
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_0000398216
Sites
	Metal binding	103	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	108	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	134	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	138	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	141	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B3M996 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: 49136A35750CDB7C	FASTA	376	42,549
	10 20 30 40 50 60 MLRALKGHVE SPLIVVTRAA STNAEKLEEI RERLAKGPNF QDFVQNPDYS KSEWENYEGK 70 80 90 100 110 120 LRREKGEEQR LRLPPWLKTT IPMGKNYAKI KNQLRELKLS TVCEEARCPN IGECWGGGEH 130 140 150 160 170 180 GTQTATIMLM GDTCTRGCRF CSVKTARKPP PLDENEPVNT ATAIASWGLD YIVLTSVDRD 190 200 210 220 230 240 DLPDGGSKHI AKTVKEIKAR NSNIFVECLV PDFRGDLGCV ETIANCGLDV YAHNIETVEK 250 260 270 280 290 300 LTPYVRDRRA HYRQTLKVLS EAKRFNPNLI TKSSIMLGLG ETDEEVENTL KDLREAGVDC 310 320 330 340 350 360 ITLGQYMQPT NKHLKVIEYV TPEKFKHWED RGNQLGFLYT ASGPLVRSSY KAGEFFITSI 370 LENRKKRQAL NSKPEQ

References

[1]	"Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tucson 14024-0371.13.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH902618 Genomic DNA. Translation: EDV40080.1.
RefSeq	XP_001957274.1. XM_001957238.1.
3D structure databases
ProteinModelPortal	B3M996.
ModBase	Search...
Protein-protein interaction databases
STRING	7217.FBpp0127326.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0128834; FBpp0127326; FBgn0101128.
GeneID	6506768.
KEGG	dan:Dana_GF24134.
Organism-specific databases
FlyBase	FBgn0101128. Dana\GF24134.
Phylogenomic databases
eggNOG	COG0320.
InParanoid	B3M996.
KO	K03644.
OrthoDB	EOG4RN8R2.
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_DROAN

Accession

Primary (citable) accession number: B3M996

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	September 2, 2008
Last modified:	April 3, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project