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Protein

Lipoyl synthase, mitochondrial

Gene

LIP5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi150 – 1501Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi161 – 1611Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi181 – 1811Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi185 – 1851Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi188 – 1881Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: SGD
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:YOR196C-MONOMER.
YEAST:YOR196C-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:LIP5UniRule annotation
Ordered Locus Names:YOR196C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR196c.
SGDiS000005722. LIP5.

Subcellular locationi

Mitochondrion UniRule annotation2 Publications

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionUniRule annotationAdd
BLAST
Chaini19 – 414396Lipoyl synthase, mitochondrialPRO_0000017726Add
BLAST

Proteomic databases

MaxQBiP32875.
PaxDbiP32875.
PeptideAtlasiP32875.
PRIDEiP32875.

Expressioni

Gene expression databases

GenevestigatoriP32875.

Interactioni

Protein-protein interaction databases

BioGridi34594. 141 interactions.
DIPiDIP-3931N.
IntActiP32875. 1 interaction.
MINTiMINT-522178.
STRINGi4932.YOR196C.

Structurei

3D structure databases

ProteinModelPortaliP32875.
SMRiP32875. Positions 121-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
GeneTreeiENSGT00390000006234.
InParanoidiP32875.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG79KPR7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRRSVGVLF VGRNTRWISS TIRCGTSATR PIRSNALNTD SDNASVRVPV
60 70 80 90 100
GNSTEVENAT SQLTGTSGKR RKGNRKRITE FKDALNLGPS FADFVSGKAS
110 120 130 140 150
KMILDPLEKA RQNTEEAKKL PRWLKVPIPK GTNYHKLKGD VKELGLSTVC
160 170 180 190 200
EEARCPNIGE CWGGKDKSKA TATIMLLGDT CTRGCRFCSV KTNRTPSKPD
210 220 230 240 250
PMEPENTAEA IKRWGLGYVV LTTVDRDDLV DGGANHLAET VRKIKQKAPN
260 270 280 290 300
TLVETLSGDF RGDLKMVDIM AQCGLDVYAH NLETVESLTP HVRDRRATYR
310 320 330 340 350
QSLSVLERAK ATVPSLITKT SIMLGLGETD EQITQTLKDL RNIQCDVVTF
360 370 380 390 400
GQYMRPTKRH MKVVEYVKPE KFDYWKERAL EMGFLYCASG PLVRSSYKAG
410
EAFIENVLKK RNMK
Length:414
Mass (Da):46,247
Last modified:October 1, 1993 - v1
Checksum:i962BC3DF9857C3BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11999 Genomic DNA. Translation: AAA34745.1.
Z75104 Genomic DNA. Translation: CAA99409.1.
AY558046 Genomic DNA. Translation: AAS56372.1.
BK006948 Genomic DNA. Translation: DAA10971.1.
PIRiS42159.
RefSeqiNP_014839.1. NM_001183615.1.

Genome annotation databases

EnsemblFungiiYOR196C; YOR196C; YOR196C.
GeneIDi854371.
KEGGisce:YOR196C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11999 Genomic DNA. Translation: AAA34745.1.
Z75104 Genomic DNA. Translation: CAA99409.1.
AY558046 Genomic DNA. Translation: AAS56372.1.
BK006948 Genomic DNA. Translation: DAA10971.1.
PIRiS42159.
RefSeqiNP_014839.1. NM_001183615.1.

3D structure databases

ProteinModelPortaliP32875.
SMRiP32875. Positions 121-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34594. 141 interactions.
DIPiDIP-3931N.
IntActiP32875. 1 interaction.
MINTiMINT-522178.
STRINGi4932.YOR196C.

Proteomic databases

MaxQBiP32875.
PaxDbiP32875.
PeptideAtlasiP32875.
PRIDEiP32875.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR196C; YOR196C; YOR196C.
GeneIDi854371.
KEGGisce:YOR196C.

Organism-specific databases

CYGDiYOR196c.
SGDiS000005722. LIP5.

Phylogenomic databases

eggNOGiCOG0320.
GeneTreeiENSGT00390000006234.
InParanoidiP32875.
KOiK03644.
OMAiCAFCQVE.
OrthoDBiEOG79KPR7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciMetaCyc:YOR196C-MONOMER.
YEAST:YOR196C-MONOMER.

Miscellaneous databases

NextBioi976499.
PROiP32875.

Gene expression databases

GenevestigatoriP32875.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION.

Entry informationi

Entry nameiLIPA_YEAST
AccessioniPrimary (citable) accession number: P32875
Secondary accession number(s): D6W2Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 4, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.