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Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila erecta (Fruit fly)
Status
Reviewed-Annotation score: -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 + 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 (Dere\GG11554)
  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 bindingi106Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi111Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi117Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi137Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi141Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi144Iron-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:GG13311
OrganismiDrosophila erecta (Fruit fly)
Taxonomic identifieri7220 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000008711 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0105583 Dere\GG13311

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_00003982171 – 379Lipoyl synthase, mitochondrialAdd BLAST379

Proteomic databases

PRIDEiB3NIL9

Structurei

3D structure databases

ProteinModelPortaliB3NIL9
SMRiB3NIL9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK03644
OMAiPYCDIDF
OrthoDBiEOG091G0AXJ
PhylomeDBiB3NIL9

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.

B3NIL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGMLRALKT HVEAPIVVAT RAVSTNAEKL EEIRERLAKG PNFQDFVQNP
60 70 80 90 100
ENSRSEWEKY EGKLRREKGE EQRLRLPPWL KTTIPVGKNY AKIKAQMREL
110 120 130 140 150
KLSTVCEEAR CPNIGECWGG GEHGTQTATI MLMGDTCTRG CRFCSVKTAR
160 170 180 190 200
RPPPLDVNEP VNTATAIASW GLDYIVLTSV DRDDLPDGGS KHIAETVREI
210 220 230 240 250
KARNSNIFVE CLVPDFRGNL ECVETIANSG LDVYAHNIET VEKLTPYVRD
260 270 280 290 300
RRAHYRQTLQ VLTEAKRFNP NLITKSSIML GLGETDGEIE CTLKDLREAG
310 320 330 340 350
VDCVTLGQYM QPTNKHLKVI EYVTPEKFKH WEERGNALGF LYTASGPLVR
360 370
SSYKAGEFFI TSILENRKKR QNATEIAKE
Length:379
Mass (Da):42,807
Last modified:September 2, 2008 - v1
Checksum:i59480438DFBEB65A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH954178 Genomic DNA Translation: EDV52515.1
RefSeqiXP_001973489.1, XM_001973453.2

Genome annotation databases

EnsemblMetazoaiFBtr0133365; FBpp0131857; FBgn0105583
GeneIDi6545884
KEGGider:Dere_GG13311

Similar proteinsi

Entry informationi

Entry nameiLIAS_DROER
AccessioniPrimary (citable) accession number: B3NIL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 2, 2008
Last modified: May 23, 2018
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

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