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

YOR196C

Organism
Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889) (Yeast)
Status
Unreviewed-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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

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 (YLR239C)
  2. Lipoyl synthase, mitochondrial (YOR196C)
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 bindingi151Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi156Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi162Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi182Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi186Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi189Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

Enzyme and pathway databases

UniPathwayi
UPA00538;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:YOR196CImported
Synonyms:LIP5UniRule annotation
ORF Names:SKUD_177005Imported
OrganismiSaccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889) (Yeast)Imported
Taxonomic identifieri226230 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002753 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

MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliJ5RSQ1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini172 – 381Elp3InterPro annotationAdd BLAST210

Sequence similaritiesi

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

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
SFLDiSFLDF00271 lipoyl_synthase, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

J5RSQ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRRSAVVLC AGRNARWFSL SISRGTSATP PIGSNELNTN SDHADARVSA
60 70 80 90 100
RNATDIEGVV SQISTAYPGK KLRKSRRRIT EFKDALNLGP SFADFVSGKA
110 120 130 140 150
SDMILDPLEK ARQNTEEAKK LPRWLKVPIP KGTNYHKLKG DVKELKLSTV
160 170 180 190 200
CEEARCPNIG ECWGGKDKSK ATATIMLLGD TCTRGCRFCS VKTNRTPSKP
210 220 230 240 250
DPMEPENTAE AIKRWGLGYV VLTTVDRDDL IDGGANHLAE TVRKIKQKAP
260 270 280 290 300
KTLVETLSGD FRGDLNMVDI MAQSGLDVYA HNLETVEALT PHVRDRRAAY
310 320 330 340 350
KQSLSVLKRA KTTVPTLITK TSIMLGLGET DEQIIRTLRD LRDVKCDVVT
360 370 380 390 400
FGQYMRPTKR HMKVVEYVKP EKFDYWKEKA LEMGFLYCAS GPLVRSSYKA
410
GEAFIENVLK KRNHEIDAQ
Length:419
Mass (Da):46,814
Last modified:October 31, 2012 - v1
Checksum:i9E0DD6A2267B6BF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACI03001362 Genomic DNA Translation: EJT42621.1

Genome annotation databases

EnsemblFungiiEJT42621; EJT42621; SKUD_177005

Similar proteinsi

Entry informationi

Entry nameiJ5RSQ1_SACK1
AccessioniPrimary (citable) accession number: J5RSQ1
Entry historyiIntegrated into UniProtKB/TrEMBL: October 31, 2012
Last sequence update: October 31, 2012
Last modified: July 18, 2018
This is version 35 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again