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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: 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: 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)
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

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
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

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000039829235 – 409Lipoyl synthase, mitochondrialAdd BLAST375

Structurei

3D structure databases

ProteinModelPortaliA7EV21.
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.
OMAiNVCTRSC.
OrthoDBiEOG092C13O2.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. 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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliA7EV21.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEDN93313; EDN93313; SS1G_09179.
GeneIDi5485857.
KEGGissl:SS1G_09179.

Organism-specific databases

EuPathDBiFungiDB:SS1G_09179.

Phylogenomic databases

InParanoidiA7EV21.
KOiK03644.
OMAiNVCTRSC.
OrthoDBiEOG092C13O2.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_SCLS1
AccessioniPrimary (citable) accession number: A7EV21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 11, 2007
Last modified: September 7, 2016
This is version 57 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, Reference proteome

Documents

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

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 one 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.