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Protein

Lipoyl synthase, mitochondrial

Gene

M01F1.3

Organism
Caenorhabditis elegans
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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.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. Putative lipoyltransferase 2, mitochondrial (lpl-1)
  2. Lipoyl synthase, mitochondrial (M01F1.3)
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 bindingi91Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi96Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi102Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi122Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi126Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi129Iron-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

ReactomeiR-CEL-389661 Glyoxylate metabolism and glycine degradation
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:M01F1.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiM01F1.3 ; CE01031 ; WBGene00010809

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome 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
ChainiPRO_00003982281 – 354Lipoyl synthase, mitochondrialAdd BLAST354

Proteomic databases

EPDiQ21452
PaxDbiQ21452
PeptideAtlasiQ21452
PRIDEiQ21452

Expressioni

Gene expression databases

BgeeiWBGene00010809

Interactioni

Protein-protein interaction databases

BioGridi532131, 7 interactors
STRINGi6239.M01F1.3.3

Structurei

3D structure databases

ProteinModelPortaliQ21452
SMRiQ21452
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
GeneTreeiENSGT00390000006234
HOGENOMiHOG000235998
InParanoidiQ21452
KOiK03644
OMAiPYCDIDF
OrthoDBiEOG091G0AXJ
PhylomeDBiQ21452

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.

Q21452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLARVWVRGL AATKKKPQVL VKDGPSLQDF ISSASVAEAV EKYEGKLKLE
60 70 80 90 100
KGDRRLRLPP WLKKEKILPS ENENVSRLKK QLKHLKLATV CQEARCPNLG
110 120 130 140 150
ECWGGSDDSL ATATIMLMGD TCTRGCKFCS VKTARAPPPL DPMEPENTST
160 170 180 190 200
AVASWGVEYI VLTSVDRDDL PDGGADHLRK TVQLMKLKKP ELLIECLLPD
210 220 230 240 250
FAGDKISVEK MATSGLDVYA HNIETVERLT PWVRDPRAKY RQSLDALRYA
260 270 280 290 300
KEVSPKLITK TSIMLGLGEA EDEIKQCLAD LRASNVDVVT FGQYMQPTKR
310 320 330 340 350
HLLVKEWVTP EKFDQWAEYS KKLGFLYVAS GPLVRSSYKA GEFYLKNVLR

NRQN
Length:354
Mass (Da):39,767
Last modified:November 1, 1996 - v1
Checksum:i5428CFA42A7FCDEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46381 Genomic DNA Translation: CAA86516.1
PIRiT23655
RefSeqiNP_497722.3, NM_065321.6
UniGeneiCel.38595

Genome annotation databases

EnsemblMetazoaiM01F1.3.1; M01F1.3.1; WBGene00010809
M01F1.3.2; M01F1.3.2; WBGene00010809
M01F1.3.3; M01F1.3.3; WBGene00010809
GeneIDi3564813
KEGGicel:CELE_M01F1.3
UCSCiM01F1.3.1 c. elegans

Similar proteinsi

Entry informationi

Entry nameiLIAS_CAEEL
AccessioniPrimary (citable) accession number: Q21452
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health