Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

ZYRO0F10758g

Organism
Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii)
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. Octanoyltransferase (ZYRO0C04488g)
  2. Lipoyl synthase, mitochondrial (ZYRO0F10758g)
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 bindingi110Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi115Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi121Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi141Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi145Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi148Iron-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
Ordered Locus Names:ZYRO0F10758g
OrganismiZygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii)
Taxonomic identifieri559307 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeZygosaccharomyces
Proteomesi
  • UP000008536 Componenti: Chromosome F

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
ChainiPRO_00003982971 – 386Lipoyl synthase, mitochondrialAdd BLAST386

Interactioni

Protein-protein interaction databases

STRINGi4956.XP_002497665.1

Structurei

3D structure databases

ProteinModelPortaliC5DY71
SMRiC5DY71
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000235998
InParanoidiC5DY71
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.

C5DY71-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRVRTSLKK CDVSLGLRLI STTRTNPTTP TTPRKRRATV FKDTLNKGPS
60 70 80 90 100
FEDFVSGRAA EVSLDPLERA RSTVEENQRL PKWLKTPIPK GSNFHKLKED
110 120 130 140 150
VRDLKLSTVC EEARCPNIGD CWGGNDKSKA TATIMLLGDT CTRGCRFCSV
160 170 180 190 200
KTNRKPGAPD PMEPENTAEA ISRWGLGYVV LTTVDRDDLI DGGSHHLAET
210 220 230 240 250
VRKIKQKAPN TLVETLAGDF RGDFQAVDVM AQSGLDVYAH NLETVESLTP
260 270 280 290 300
HVRDRRATYR QSLNVLKRAK QTVPTLVTKT SLMLGLGETH EEVIQTLRDL
310 320 330 340 350
REIKCDVVTF GQYMRPTKRH MKVVEYVTPE KFEFWKEQAL EMGFLYCASG
360 370 380
PLVRSSYKAG EAFIENVLRK RKPLEQQQES LSAFRI
Length:386
Mass (Da):43,530
Last modified:July 28, 2009 - v1
Checksum:iC444F390DA19C102
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928178 Genomic DNA Translation: CAR28732.1
RefSeqiXP_002497665.1, XM_002497620.1

Genome annotation databases

EnsemblFungiiCAR28732; CAR28732; ZYRO0F10758g
GeneIDi8205431
KEGGizro:ZYRO0F10758g

Similar proteinsi

Entry informationi

Entry nameiLIPA_ZYGRC
AccessioniPrimary (citable) accession number: C5DY71
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: May 23, 2018
This is version 59 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health