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Protein

Lipoyl synthase, mitochondrial

Gene

CLUG_04975

Organism
Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae)
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 (CLUG_03573)
  2. Lipoyl synthase, mitochondrial (CLUG_04975)
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 bindingi120Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi125Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi131Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi150Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi154Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi157Iron-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:CLUG_04975
OrganismiClavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae)
Taxonomic identifieri306902 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesMetschnikowiaceaeClavispora
Proteomesi
  • UP000007703 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:CLUG_04975

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 – 44MitochondrionUniRule annotationAdd BLAST44
ChainiPRO_000039826245 – 391Lipoyl synthase, mitochondrialAdd BLAST347

Interactioni

Protein-protein interaction databases

STRINGi306902.XP_002614960.1

Structurei

3D structure databases

ProteinModelPortaliC4YA37
SMRiC4YA37
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
InParanoidiC4YA37
KOiK03644
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.

C4YA37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVHPHLSRTK RTFFSHSSQM ISRHIRKTNS LAFVRALSAS ETAVTPRRKR
60 70 80 90 100
TVFTDELNKG PSFEDFVSGK AADVFVDPLE AARKDPEAKL PKWLKVPIPK
110 120 130 140 150
GRSFHSVKKD VRELKLATVC EEAKCPNISE CWGGKKSEAT ATIMLLGDTC
160 170 180 190 200
TRGCRFCSVK TSRTPAKPDP MEPENTAEAI SRWGLGYVVL TTVDRDDLAD
210 220 230 240 250
GGAAHLAETV RLIKQKAPQI LVEVLGGDFR GDLTSCDTLA VSGLDVYAHN
260 270 280 290 300
LETVEALTPH VRDRRATYRQ SLSILERAKQ AKPSLITKTS LMLGFGETDE
310 320 330 340 350
QIMQTLRDLR GIGCDVVTFG QYMRPTKRHM KVVEYVRPEK FDYWKEVALE
360 370 380 390
MGFLYVASGP LVRSSYKAGE AFIENVLRKR KHNVGDSPRL A
Length:391
Mass (Da):43,682
Last modified:July 28, 2009 - v1
Checksum:iEE362CDEE68AFA88
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH408081 Genomic DNA Translation: EEQ40847.1
RefSeqiXP_002614960.1, XM_002614914.1

Genome annotation databases

EnsemblFungiiEEQ40847; EEQ40847; CLUG_04975
GeneIDi8495745
KEGGiclu:CLUG_04975

Similar proteinsi

Entry informationi

Entry nameiLIPA_CLAL4
AccessioniPrimary (citable) accession number: C4YA37
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: May 23, 2018
This is version 49 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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