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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: 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: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi115 – 1151Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi121 – 1211Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi145 – 1451Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi148 – 1481Iron-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:ZYRO0F10758g
OrganismiZygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229) (Candida mogii)
Taxonomic identifieri559307 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeZygosaccharomyces
ProteomesiUP000008536 Componenti: Chromosome F

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? – 386Lipoyl synthase, mitochondrialPRO_0000398297
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi4956.XP_002497665.1.

Structurei

3D structure databases

ProteinModelPortaliC5DY71.
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.
InParanoidiC5DY71.
KOiK03644.
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.

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

GeneIDi8205431.
KEGGizro:ZYRO0F10758g.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliC5DY71.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4956.XP_002497665.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8205431.
KEGGizro:ZYRO0F10758g.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiC5DY71.
KOiK03644.
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...

Publicationsi

  1. "Comparative genomics of protoploid Saccharomycetaceae."
    The Genolevures Consortium
    Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V., Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V., Vacherie B., Val M.-E.
    , Fulton R.S., Minx P., Wilson R., Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.
    Genome Res. 19:1696-1709(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568 / NRRL Y-229.

Entry informationi

Entry nameiLIPA_ZYGRC
AccessioniPrimary (citable) accession number: C5DY71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: June 24, 2015
This is version 45 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.