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Protein

Lipoyl synthase, mitochondrial

Gene

SS1G_09179

Organism
Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
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. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (SS1G_09179), Lipoyl synthase, mitochondrial (sscle_15g106970)
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 bindingi130Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi135Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi141Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi161Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi165Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi168Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

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
ORF Names:SS1G_09179
OrganismiSclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) (Whetzelinia sclerotiorum)
Taxonomic identifieri665079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeSclerotinia
Proteomesi
  • UP000001312 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SS1G_09179

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 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000039829235 – 409Lipoyl synthase, mitochondrialAdd BLAST375

Interactioni

Protein-protein interaction databases

STRINGi5180.EDN93313

Structurei

3D structure databases

ProteinModelPortaliA7EV21
SMRiA7EV21
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiA7EV21
KOiK03644
OMAiPYCDIDF
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.

A7EV21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIVPRFRC LNAPPLRQTS RNILAIPTAT SRSFATEIDV SKPTPIVKRR
60 70 80 90 100
PTYFKDKINA VPSFSEFVGL PEKAFTPEDA LELRTAMVGP PGKKRQITRL
110 120 130 140 150
PEWLKTPIPD NSNYKKIKKD LRGLNLHTVC EEARCPNISD CWGGSDKSAA
160 170 180 190 200
TATIMLMGDT CTRGCRFCSV KTSKAPPPLD PHEPEHTAEA LSRWGLGYVV
210 220 230 240 250
LTSVDRDDLA DGGARHFAET IMKIKQKKSS ILVEALTGDY GGDLEMVKLV
260 270 280 290 300
AESGLDVYAH NMETTEELTP FVRDRRAKYR QSLKVLEAAK KAKPSLITKT
310 320 330 340 350
SIMLGLGETE EALWQALRDL REVDVDVVTF GQYMRPTKRH MKVEEYVTPE
360 370 380 390 400
VFEIWRQRAL DLGFLYCASG PLVRSSYKAG EAFIENVLKK RKGVTILSDE

ATGMDKAIV
Length:409
Mass (Da):45,637
Last modified:September 11, 2007 - v1
Checksum:i8EA97891D4BC7425
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476633 Genomic DNA Translation: EDN93313.1
RefSeqiXP_001589458.1, XM_001589408.1

Genome annotation databases

EnsemblFungiiEDN93313; EDN93313; SS1G_09179
GeneIDi5485857
KEGGissl:SS1G_09179

Similar proteinsi

Entry informationi

Entry nameiLIPA_SCLS1
AccessioniPrimary (citable) accession number: A7EV21
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 11, 2007
Last modified: May 23, 2018
This is version 64 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, Reference proteome

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