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Protein

Lipoyl synthase, mitochondrial

Gene

KLLA0F00836g

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
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

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 + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(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

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, mitochondrial (LIPB)
  2. Lipoyl synthase, mitochondrial (KLLA0F00836g)
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 bindingi104Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi109Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi115Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi135Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi139Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi142Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

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:KLLA0F00836g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 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_00003982681 – 370Lipoyl synthase, mitochondrialAdd BLAST370

Interactioni

Protein-protein interaction databases

STRINGi284590.XP_455117.1.

Structurei

3D structure databases

ProteinModelPortaliQ6CLS2.
SMRiQ6CLS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
HOGENOMiHOG000235998.
InParanoidiQ6CLS2.
KOiK03644.
OMAiPYCDIDF.
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.

Q6CLS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKPGIRSVQ KRFITETVVR STQPSVSRRR KTTHFTDKLN KGPSFEDFVN
60 70 80 90 100
GNAQKFTLDP LEKARQNSEE VQRLPTWLKV PIAKGSNFHK LKNDVKELKL
110 120 130 140 150
STVCEEAKCP NIGECWGGGD KSKATATIML LGDTCTRGCR FCSVKTNRKP
160 170 180 190 200
SAPDPTEPEN TAEAISRWGL GYVVLTTVDR DDLVDGGAYH LAETVQKIKQ
210 220 230 240 250
KAPNILVETL SGDFRGDLEM VKVMALSGLD VYAHNMETVE ALTPHVRDRR
260 270 280 290 300
ATYRQSLSVL ECAKKTVPTL VTKTSVMLGL GETDEQVLQT MKDLRAIGCD
310 320 330 340 350
VITFGQYMRP TKRHMKVVEY VTPEKFDYWK QKALELGFLY CASGPLVRSS
360 370
YKAGESFIEN VLRGRSRARI
Length:370
Mass (Da):41,470
Last modified:August 16, 2004 - v1
Checksum:i86A501949025496B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382126 Genomic DNA. Translation: CAG97824.1.
RefSeqiXP_455117.1. XM_455117.1.

Genome annotation databases

EnsemblFungiiCAG97824; CAG97824; KLLA0_F00836g.
GeneIDi2895837.
KEGGikla:KLLA0F00836g.

Similar proteinsi

Entry informationi

Entry nameiLIPA_KLULA
AccessioniPrimary (citable) accession number: Q6CLS2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: August 16, 2004
Last modified: October 25, 2017
This is version 89 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