C6HLY2 (LIPA_AJECH) 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:

HCDG_07601

Organism

Ajellomyces capsulata (strain H143) (Darling's disease fungus) (Histoplasma capsulatum) [Complete proteome]

Taxonomic identifier

544712 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Ajellomyces › Ajellomyces capsulatus

Protein attributes

Sequence length	430 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 – 37	37	Mitochondrion Potential
	Chain	38 – 430	393	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000398247
Sites
	Metal binding	141	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	146	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	152	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	172	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	176	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	179	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C6HLY2 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: ED3348D459576A68	FASTA	430	46,742
	10 20 30 40 50 60 MATSAGKLRT LYSAHSSLSS LPPSARPTLQ LATLRSYATT TPHDSPIGNT SNTPPTVKRP 70 80 90 100 110 120 ATAFKDKLNA GPAFSDFVSG KKDEPLDPAE AYALKTALVG PPGRKKEITR LPPWLKTPIP 130 140 150 160 170 180 DSSNYKRIKN DLRGLNLHTV CEEARCPNIA DCWGGSSKSA ATATIMLMGD TCTRGCRFCS 190 200 210 220 230 240 VKTSNKPPPL DPHEPDNTAE ALSRWGLGYV VLTTVDRDDL ADGGARHCAE TVMKIKQKAP 250 260 270 280 290 300 NILVECLTGD YAGDLDMVAL VANSGLDVFA HNVETVEALT PFVRDRRASF QQSLRVLKAA 310 320 330 340 350 360 KAAKPELITK TSLMLGLGET EAQLWDALRA LRAINVDVVT FGQYMRPTKR HMAVHEYVRP 370 380 390 400 410 420 DVFDLWKERA LEMGFLYCAS GPLVRSSYKA GEAFIENVLK KRKGGNAGSV NEKVTTSENV 430 KKLVAGEAMR

References

[1]

"The genome sequence of Ajellomyces capsulatus strain H143." Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J. , Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W. Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: H143.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG692431 Genomic DNA. Translation: EER38732.1.
3D structure databases
ProteinModelPortal	C6HLY2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_AJECH

Accession

Primary (citable) accession number: C6HLY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	September 1, 2009
Last modified:	April 3, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program