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Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila pseudoobscura pseudoobscura (Fruit fly)
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. Putative lipoyltransferase 2, mitochondrial (Dpse\GA22047)
  2. Lipoyl synthase, mitochondrial (Las)
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 bindingi101Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi106Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi112Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi132Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi136Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi139Iron-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
Name:LasUniRule annotation
ORF Names:GA18753
OrganismiDrosophila pseudoobscura pseudoobscura (Fruit fly)
Taxonomic identifieri46245 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000001819 Componenti: Partially assembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0078753. Dpse\GA18753.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome 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_00003982211 – 374Lipoyl synthase, mitochondrialAdd BLAST374

Expressioni

Gene expression databases

BgeeiFBgn0078753.

Interactioni

Protein-protein interaction databases

STRINGi7237.FBpp0275593.

Structurei

3D structure databases

ProteinModelPortaliQ2LYK1.
SMRiQ2LYK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

InParanoidiQ2LYK1.
KOiK03644.
OMAiPYCDIDF.
PhylomeDBiQ2LYK1.

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.

Q2LYK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTAFRPNSP TAIVVRAAST NAKKLEEIRE RLAKGPNFQD FVQNPDNLKS
60 70 80 90 100
VGENYDGKLR REKGEEQRLR LPPWLKTTIP MGKNYTKIKE QLRELKLSTV
110 120 130 140 150
CEEARCPNIG ECWGGGENGT QTATIMLMGD TCTRGCRFCS VKTARIPPPL
160 170 180 190 200
DENEPVNTAK AIASWGLDYI VLTSVDRDDL PDGGSKHIAQ TVREIKARNS
210 220 230 240 250
NIFVECLVPD FRGDLDCVET IANCGLDVYA HNIETVEKLT PYVRDRRAHY
260 270 280 290 300
RQTLRVLTEA KRFNPNLITK SSIMLGLGET DEEIERTMTD LREAGVECLT
310 320 330 340 350
LGQYMQPTNK HLKVIEYVTP EKFKHWEERG NDLGFLYTAS GPLVRSSYKA
360 370
GEFFISSILA NRKANQSKDS APKN
Length:374
Mass (Da):42,118
Last modified:February 21, 2006 - v1
Checksum:iE27E02B8B2B5A9F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH379069 Genomic DNA. Translation: EAL29861.1.
RefSeqiXP_001354122.1. XM_001354086.2.

Genome annotation databases

EnsemblMetazoaiFBtr0277155; FBpp0275593; FBgn0078753.
GeneIDi4813963.
KEGGidpo:Dpse_GA18753.

Similar proteinsi

Entry informationi

Entry nameiLIAS_DROPS
AccessioniPrimary (citable) accession number: Q2LYK1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 21, 2006
Last modified: October 25, 2017
This is version 75 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families