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Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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 + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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 (Dmel\CG9804), Putative lipoyltransferase 2, mitochondrial (CG9804)
  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

GO - Biological processi

Keywordsi

Molecular functionTransferase
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-DME-389661 Glyoxylate metabolism and glycine degradation
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:CG5231
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0029158 Las

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_00003982191 – 377Lipoyl synthase, mitochondrialAdd BLAST377

Proteomic databases

PaxDbiQ7JQW6
PRIDEiQ7JQW6

Expressioni

Gene expression databases

BgeeiFBgn0029158
GenevisibleiQ7JQW6 DM

Interactioni

Protein-protein interaction databases

BioGridi65517, 1 interactor
IntActiQ7JQW6, 1 interactor
STRINGi7227.FBpp0288705

Structurei

3D structure databases

ProteinModelPortaliQ7JQW6
SMRiQ7JQW6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2672 Eukaryota
COG0320 LUCA
GeneTreeiENSGT00390000006234
InParanoidiQ7JQW6
KOiK03644
OMAiPYCDIDF
OrthoDBiEOG091G0AXJ
PhylomeDBiQ7JQW6

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.

Q7JQW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRALKTHAE APIVVATRAA STNAEKLEEI RERLAKGPNF HDFVQNPDNT
60 70 80 90 100
RNEWEQYDGK LRREKGEEQR LRLPPWLKTT IPVGKNYAKI KAQMRELKLS
110 120 130 140 150
TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP
160 170 180 190 200
PLDVNEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSEHI AETVREIKAR
210 220 230 240 250
NSNIFVECLV PDFRGNLECV KTIANSGLDV YAHNIETVEK LTPYVRDRRA
260 270 280 290 300
HYRQTLQVLT EAKRFNPNLI TKSSIMLGLG ETDEEIENTL KDLREAGVDC
310 320 330 340 350
VTLGQYMQPT NKHLKVIEYV TPEKFKHWEE RGNELGFLYT ASGPLVRSSY
360 370
KAGEFFITSI LENRKKRQND TEVPKKQ
Length:377
Mass (Da):42,734
Last modified:October 5, 2010 - v2
Checksum:iE702B1AB55DD5DC3
GO

Sequence cautioni

The sequence AAL13786 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAO41414 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA Translation: AAF51596.2
AY058557 mRNA Translation: AAL13786.1 Different initiation.
BT003750 mRNA Translation: AAO41414.1 Different initiation.
RefSeqiNP_524183.2, NM_079459.3
UniGeneiDm.2512

Genome annotation databases

EnsemblMetazoaiFBtr0290266; FBpp0288705; FBgn0029158
GeneIDi40259
KEGGidme:Dmel_CG5231

Similar proteinsi

Entry informationi

Entry nameiLIAS_DROME
AccessioniPrimary (citable) accession number: Q7JQW6
Secondary accession number(s): Q9VPF7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 23, 2018
This is version 68 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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