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Protein

Lipoyl synthase, mitochondrial

Gene

KLTH0D09548g

Organism
Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284) (Yeast) (Kluyveromyces thermotolerans)
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:iprotein 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 (KLTH0F08272g)
  2. Lipoyl synthase, mitochondrial (KLTH0D09548g)
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 bindingi107 – 1071Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi112 – 1121Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi118 – 1181Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi142 – 1421Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi145 – 1451Iron-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:KLTH0D09548g
OrganismiLachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284) (Yeast) (Kluyveromyces thermotolerans)
Taxonomic identifieri559295 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea
ProteomesiUP000002036 Componenti: Chromosome D

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
Transit peptidei1 – 2424MitochondrionUniRule annotationAdd
BLAST
Chaini25 – 371347Lipoyl synthase, mitochondrialPRO_0000398270Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC5DGZ5.
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.
InParanoidiC5DGZ5.
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.

C5DGZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRFKCSRL QLQKRAISVT KATTTTASQP KRRRTTTFSD ALNKGPSFED
60 70 80 90 100
FVSGKAAKFT LDPLQQARSN IEEAKRLPRW LKVPIPKGTN YHKLKKDVRE
110 120 130 140 150
LKLSTVCEEA KCPNISECWG GGDSSKATAT IMLLGDTCTR GCRFCSVKTN
160 170 180 190 200
RAPSKPDPAE PENTAEAISR WGLGYVVLTT VDRDDLADGG AHHLAETVCR
210 220 230 240 250
IKQKAPKTLV ETLSGDFRGD LEMVKVMAQS GLDVYAHNLE TVKDLTPHVR
260 270 280 290 300
DRRATYEQSL SVLNQAKKTV PTLITKTSLM LGLGETDEQV LQTLQDLRAI
310 320 330 340 350
GCDVVTFGQY MRPTKRHMKV VEYVKPEKFD YWRDKALELG FLYCASGPLV
360 370
RSSYKAGEAF IENVLRKRAN N
Length:371
Mass (Da):41,451
Last modified:July 28, 2009 - v1
Checksum:i54736E8D8C575ECB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928168 Genomic DNA. Translation: CAR22687.1.
RefSeqiXP_002553125.1. XM_002553079.1.

Genome annotation databases

GeneIDi8295363.
KEGGilth:KLTH0D09548g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928168 Genomic DNA. Translation: CAR22687.1.
RefSeqiXP_002553125.1. XM_002553079.1.

3D structure databases

ProteinModelPortaliC5DGZ5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8295363.
KEGGilth:KLTH0D09548g.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiC5DGZ5.
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 56472 / CBS 6340 / NRRL Y-8284.

Entry informationi

Entry nameiLIPA_LACTC
AccessioniPrimary (citable) accession number: C5DGZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 28, 2009
Last modified: July 22, 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.