Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

LIP5

Organism
Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
Status
Reviewed-Annotation score: -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 N6-(octanoyl)lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (SCRG_04192)
  2. Lipoyl synthase, mitochondrial (LIP5)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi150Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi155Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi161Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi181Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi185Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi188Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Ligand4Fe-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:SCRG_01588
OrganismiSaccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
Taxonomic identifieri285006 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000008335 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 18MitochondrionUniRule annotationAdd BLAST18
ChainiPRO_000039828919 – 414Lipoyl synthase, mitochondrialAdd BLAST396

Proteomic databases

PRIDEiB3LJM6

Structurei

3D structure databases

ProteinModelPortaliB3LJM6
SMRiB3LJM6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

OrthoDBiEOG092C13O2

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR007197 rSAM
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF005963 Lipoyl_synth, 1 hit
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

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

B3LJM6-1 [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:September 2, 2008 - v1
Checksum:i962BC3DF9857C3BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408045 Genomic DNA Translation: EDV10779.1

Genome annotation databases

EnsemblFungiiEDV10779; EDV10779; SCRG_01588

Similar proteinsi

Entry informationi

Entry nameiLIPA_YEAS1
AccessioniPrimary (citable) accession number: B3LJM6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 2, 2008
Last modified: May 23, 2018
This is version 52 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health