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Protein

Lipoyl synthase, mitochondrial

Gene

MCYG_08114

Organism
Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
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. Octanoyltransferase (MCYG_08137)
  2. Lipoyl synthase, mitochondrial (MCYG_08114)
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 bindingi129Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi134Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi140Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi160Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi164Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi167Iron-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:MCYG_08114
OrganismiArthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis)
Taxonomic identifieri554155 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeMicrosporum
Proteomesi
  • UP000002035 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

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 29MitochondrionUniRule annotationAdd BLAST29
ChainiPRO_000039827230 – 410Lipoyl synthase, mitochondrialAdd BLAST381

Proteomic databases

PRIDEiC5FZJ2

Interactioni

Protein-protein interaction databases

STRINGi554155.XP_002843031.1

Structurei

3D structure databases

ProteinModelPortaliC5FZJ2
SMRiC5FZJ2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
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.

C5FZJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTTVCSAA RIRVASSQVL RSIANTRTYA TTSPESSIPE TKPTAKRTPT
60 70 80 90 100
TFKDKLNKGP SFSDFIGGAT EPPLSPDEAY ALKTALVGPA GKKKEITRLP
110 120 130 140 150
SWLKTPIPDS SSYKKIKNDL RGLNLHTVCE EARCPNISEC WGGGSKAAAT
160 170 180 190 200
ATIMLMGDTC TRGCRFCSVK TSRTPPPLDP HEPENTAEAL SRWGLGYVVL
210 220 230 240 250
TAVDRDDLVD GGARHFAETV RRIKGKAPNI LVECLTGDFS GDMEMVSLMA
260 270 280 290 300
ESGMDVFAHN VETVEALTPF VRDRRASFQQ SLSVLRGAKA ANPELITKTS
310 320 330 340 350
LMLGLGETKE QVLDALKQLR ASQVDVVTFG QYMRPTKRHM AVHEYVRPDV
360 370 380 390 400
FDMWKEKAME MGFLYCASGP LVRSSYKAGE AFIENVLKKR AKERIGGAVE
410
DSVKGKDVLL
Length:410
Mass (Da):44,727
Last modified:July 28, 2009 - v1
Checksum:iB3FAF375C58B00DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS995708 Genomic DNA Translation: EEQ35295.1
RefSeqiXP_002843031.1, XM_002842985.1

Genome annotation databases

EnsemblFungiiEEQ35295; EEQ35295; MCYG_08114
GeneIDi9226245

Similar proteinsi

Entry informationi

Entry nameiLIPA_ARTOC
AccessioniPrimary (citable) accession number: C5FZJ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: May 23, 2018
This is version 52 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

Documents

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

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