A5ABM5 (LIPA_ASPNC) 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:

An11g09760

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	416 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 Potential 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
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 – 33	33	Mitochondrion Potential
	Chain	34 – 416	383	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000398255
Sites
	Metal binding	133	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	138	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	144	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	164	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	168	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	171	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5ABM5 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: F5F6F7FE2537C5AB	FASTA	416	45,541
	10 20 30 40 50 60 MAAASTNRLR LLYTSTRASL PQSTPSILTT RTYATTDSST SATSTPKPRR RTAFTDKLNA 70 80 90 100 110 120 GPSFGDFVSG NNDNAPLIDP SEAYALETAL VGPAGRKKQM TRLPPWLKTP IPDSKNYQRL 130 140 150 160 170 180 KKDLRGLNLH TVCEEARCPN ISDCWGGGDK AAATATIMLM GDTCTRGCSF CSVKTSRRPA 190 200 210 220 230 240 ALDPHEPENT AEAISRWGLG YVVLTSVDRD DLADGGARHF AETVRKIKSK APSTLVECLT 250 260 270 280 290 300 GDYRGDLDMV ALVANSGLDV YAHNIETVEA LTPRVRDRRA TFKQSIAVLE AAKKANPEVI 310 320 330 340 350 360 TKSSLMLGLG ETEEQLEHAL AQLRAVDVDV VTFGQYMRPT KRHMAVHEYV HPRWFEHWQR 370 380 390 400 410 RAEELGFLYC ASGPLVRSSY KAGEAFIENV LKKRRAGVSD AVAEKKVAAA VDEAAR

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270251 Genomic DNA. Translation: CAK97060.1.
RefSeq	XP_001394934.1. XM_001394897.2.
3D structure databases
ProteinModelPortal	A5ABM5.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00009116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00009293; CADANGAP00009116; CADANGAG00009293.
GeneID	4985192.
KEGG	ang:ANI_1_2510094.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OrthoDB	EOG4G1QR3.
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

LIPA_ASPNC

Accession

Primary (citable) accession number: A5ABM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	June 12, 2007
Last modified:	April 3, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program