P32875 (LIPA_YEAST) 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:	LIP5
Ordered Locus Names:	YOR196C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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 Probable. Ref.1 Ref.8
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 Ref.5 Ref.7.
Miscellaneous	Present with 1630 molecules/cell in log phase SD medium. 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 mutant phenotype Ref.8. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 11914276Ref.5Ref.7PubMed 16823961. Source: SGD
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from sequence alignment Ref.1. Source: SGD 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 – 18	18	Mitochondrion Potential
	Chain	19 – 414	396	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000017726
Sites
	Metal binding	150	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	155	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	161	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	181	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	185	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	188	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P32875 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 962BC3DF9857C3BB	FASTA	414	46,247
	10 20 30 40 50 60 MYRRSVGVLF VGRNTRWISS TIRCGTSATR PIRSNALNTD SDNASVRVPV GNSTEVENAT 70 80 90 100 110 120 SQLTGTSGKR RKGNRKRITE FKDALNLGPS FADFVSGKAS KMILDPLEKA RQNTEEAKKL 130 140 150 160 170 180 PRWLKVPIPK GTNYHKLKGD VKELGLSTVC EEARCPNIGE CWGGKDKSKA TATIMLLGDT 190 200 210 220 230 240 CTRGCRFCSV KTNRTPSKPD PMEPENTAEA IKRWGLGYVV LTTVDRDDLV DGGANHLAET 250 260 270 280 290 300 VRKIKQKAPN TLVETLSGDF RGDLKMVDIM AQCGLDVYAH NLETVESLTP HVRDRRATYR 310 320 330 340 350 360 QSLSVLERAK ATVPSLITKT SIMLGLGETD EQITQTLKDL RNIQCDVVTF GQYMRPTKRH 370 380 390 400 410 MKVVEYVKPE KFDYWKERAL EMGFLYCASG PLVRSSYKAG EAFIENVLKK RNMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae." Sulo P., Martin N.C. J. Biol. Chem. 268:17634-17639(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: DBY745.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lipoic acid synthesis and attachment in yeast mitochondria." Schonauer M.S., Kastaniotis A.J., Kursu V.A., Hiltunen J.K., Dieckmann C.L. J. Biol. Chem. 284:23234-23242(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11999 Genomic DNA. Translation: AAA34745.1. Z75104 Genomic DNA. Translation: CAA99409.1. AY558046 Genomic DNA. Translation: AAS56372.1. BK006948 Genomic DNA. Translation: DAA10971.1.
PIR	S42159.
RefSeq	NP_014839.1. NM_001183615.1.
3D structure databases
ProteinModelPortal	P32875.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3931N.
IntAct	P32875. 1 interaction.
MINT	MINT-522178.
STRING	4932.YOR196C.
Proteomic databases
PaxDb	P32875.
PeptideAtlas	P32875.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR196C; YOR196C; YOR196C.
GeneID	854371.
KEGG	sce:YOR196C.
Organism-specific databases
CYGD	YOR196c.
SGD	S000005722. LIP5.
Phylogenomic databases
eggNOG	COG0320.
GeneTree	ENSGT00390000006234.
KO	K03644.
OMA	EEYVTPE.
OrthoDB	EOG4G1QR3.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Gene expression databases
Genevestigator	P32875.
GermOnline	YOR196C. Saccharomyces cerevisiae.
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...
Other
NextBio	976499.

Entry information

Entry name

LIPA_YEAST

Accession

Primary (citable) accession number: P32875
Secondary accession number(s): D6W2Q5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program