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Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila ananassae (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 (Dana\GF16807)
  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 bindingi103Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi108Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi114Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi134Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi138Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi141Iron-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:GF24134
OrganismiDrosophila ananassae (Fruit fly)
Taxonomic identifieri7217 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000007801 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0101128. Dana\GF24134.

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_00003982161 – 376Lipoyl synthase, mitochondrialAdd BLAST376

Expressioni

Gene expression databases

BgeeiFBgn0101128.

Interactioni

Protein-protein interaction databases

STRINGi7217.FBpp0127326.

Structurei

3D structure databases

ProteinModelPortaliB3M996.
SMRiB3M996.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672. Eukaryota.
COG0320. LUCA.
InParanoidiB3M996.
KOiK03644.
OMAiPYCDIDF.
OrthoDBiEOG091G0AXJ.
PhylomeDBiB3M996.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiView protein in InterPro
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
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.

B3M996-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRALKGHVE SPLIVVTRAA STNAEKLEEI RERLAKGPNF QDFVQNPDYS
60 70 80 90 100
KSEWENYEGK LRREKGEEQR LRLPPWLKTT IPMGKNYAKI KNQLRELKLS
110 120 130 140 150
TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP
160 170 180 190 200
PLDENEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSKHI AKTVKEIKAR
210 220 230 240 250
NSNIFVECLV PDFRGDLGCV ETIANCGLDV YAHNIETVEK LTPYVRDRRA
260 270 280 290 300
HYRQTLKVLS EAKRFNPNLI TKSSIMLGLG ETDEEVENTL KDLREAGVDC
310 320 330 340 350
ITLGQYMQPT NKHLKVIEYV TPEKFKHWED RGNQLGFLYT ASGPLVRSSY
360 370
KAGEFFITSI LENRKKRQAL NSKPEQ
Length:376
Mass (Da):42,549
Last modified:September 2, 2008 - v1
Checksum:i49136A35750CDB7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH902618 Genomic DNA. Translation: EDV40080.1.
RefSeqiXP_001957274.1. XM_001957238.2.

Genome annotation databases

EnsemblMetazoaiFBtr0128834; FBpp0127326; FBgn0101128.
GeneIDi6506768.
KEGGidan:Dana_GF24134.

Similar proteinsi

Entry informationi

Entry nameiLIAS_DROAN
AccessioniPrimary (citable) accession number: B3M996
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 2, 2008
Last modified: October 25, 2017
This is version 51 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