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Protein

Lipoyl synthase, mitochondrial

Gene

YALI0E10571g

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
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

Pathway:iprotein 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 (YALI0_F27357g)
  2. Lipoyl synthase, mitochondrial (YALI0E10571g)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi89 – 891Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi95 – 951Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi115 – 1151Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi119 – 1191Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi122 – 1221Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

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
Ordered Locus Names:YALI0E10571g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300 Componenti: Chromosome E

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 351Lipoyl synthase, mitochondrialPRO_0000398296
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6C6C6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ6C6C6.
KOiK03644.
OMAiNVCTRSC.
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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
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.

Q6C6C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKRQLHSAS KRSATRFSDA LNKGPSFDDF LTGRAGKAAA VDPVLAASSD
60 70 80 90 100
GKRLPKWLKT EIPKGKNLHN IREDLRGLGL HTVCEEARCP NIGECWGGSD
110 120 130 140 150
KSKATATIML MGDTCTRGCR FCSVKTNRNP GPLDPNEPEN TAVAISKWGL
160 170 180 190 200
GYVVLTTVDR DDLSDGGSWH FADTVKRIKE KAPHILVETL SGDFRGNLDH
210 220 230 240 250
VTTLAESGLD VFAHNMETVE ALTPFVRDRR ATFQQSLSVL RQAKVAVPDL
260 270 280 290 300
ITKTSIMLGF GETDEQVEDT LMQLRGVGVD IVTFGQYMRP TIRHLKVAEY
310 320 330 340 350
VTPEKFDYWQ KRAMDMGFLY CASGPLVRSS YKAGEVFIEN VLKKRNAAKA

V
Length:351
Mass (Da):38,779
Last modified:August 16, 2004 - v1
Checksum:iF472C5B0FBBC1D52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79377.1.
RefSeqiXP_503786.1. XM_503786.1.

Genome annotation databases

EnsemblFungiiCAG79377; CAG79377; YALI0_E10571g.
GeneIDi2912634.
KEGGiyli:YALI0E10571g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382131 Genomic DNA. Translation: CAG79377.1.
RefSeqiXP_503786.1. XM_503786.1.

3D structure databases

ProteinModelPortaliQ6C6C6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG79377; CAG79377; YALI0_E10571g.
GeneIDi2912634.
KEGGiyli:YALI0E10571g.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ6C6C6.
KOiK03644.
OMAiNVCTRSC.
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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_YARLI
AccessioniPrimary (citable) accession number: Q6C6C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: August 16, 2004
Last modified: July 22, 2015
This is version 76 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

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.