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Protein

Lipoyl synthase, mitochondrial

Gene

LIP5

Organism
Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

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: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

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
ORF Names:AWRI1631_153490
OrganismiSaccharomyces cerevisiae (strain AWRI1631) (Baker's yeast)
Taxonomic identifieri545124 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000008988 Componenti: Unassembled WGS sequence

Subcellular locationi

Mitochondrion UniRule annotation

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_0000398286Add
BLAST

Proteomic databases

PRIDEiB5VS81.

Structurei

3D structure databases

ProteinModelPortaliB5VS81.
SMRiB5VS81. 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

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]
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.

B5VS81-1 [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:November 24, 2008 - v1
Checksum:i962BC3DF9857C3BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ABSV01002195 Genomic DNA. Translation: EDZ69210.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
ABSV01002195 Genomic DNA. Translation: EDZ69210.1.

3D structure databases

ProteinModelPortaliB5VS81.
SMRiB5VS81. Positions 121-401.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiB5VS81.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiEOG79KPR7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

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]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genome analysis of a Saccharomyces cerevisiae wine strain."
    Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.
    FEMS Yeast Res. 8:1185-1195(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AWRI1631.

Entry informationi

Entry nameiLIPA_YEAS6
AccessioniPrimary (citable) accession number: B5VS81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 4, 2010
Last sequence update: November 24, 2008
Last modified: March 31, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.