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Protein

Lipoyl synthase, mitochondrial

Gene

Las

Organism
Drosophila sechellia (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

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(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

Pathway:iprotein 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. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi103 – 1031Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi108 – 1081Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi134 – 1341Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-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:GM22215
OrganismiDrosophila sechellia (Fruit fly)
Taxonomic identifieri7238 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000001292 Componenti: Unassembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0177085. Dsec\GM22215.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 377Lipoyl synthase, mitochondrialPRO_0000398222
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB4IAA7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK03644.
OMAiNVCTRSC.
OrthoDBiEOG7P2XS7.
PhylomeDBiB4IAA7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B4IAA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRALKTHVE APIVVATRAA STNAEKLEEI RERLAKGPNF QDFVQNPDNT
60 70 80 90 100
RSEWEQYDGK LRREKGEEQR LRLPPWLKTT IPVGKNYAKI KAQMRELKLS
110 120 130 140 150
TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP
160 170 180 190 200
PLDVNEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSKHI AETVREIKAR
210 220 230 240 250
NSNIFVECLV PDFRGNLECV ETIANSGLDV 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 LENRKKRQNA TEVPKEQ
Length:377
Mass (Da):42,683
Last modified:September 23, 2008 - v1
Checksum:i9618EEDA95C3F884
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH480826 Genomic DNA. Translation: EDW44220.1.
RefSeqiXP_002040667.1. XM_002040631.1.

Genome annotation databases

EnsemblMetazoaiFBtr0205200; FBpp0203692; FBgn0177085.
GeneIDi6616303.
KEGGidse:Dsec_GM22215.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH480826 Genomic DNA. Translation: EDW44220.1.
RefSeqiXP_002040667.1. XM_002040631.1.

3D structure databases

ProteinModelPortaliB4IAA7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0205200; FBpp0203692; FBgn0177085.
GeneIDi6616303.
KEGGidse:Dsec_GM22215.

Organism-specific databases

FlyBaseiFBgn0177085. Dsec\GM22215.

Phylogenomic databases

KOiK03644.
OMAiNVCTRSC.
OrthoDBiEOG7P2XS7.
PhylomeDBiB4IAA7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Evolution of genes and genomes on the Drosophila phylogeny."
    Drosophila 12 genomes consortium
    Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Rob3c / Tucson 14021-0248.25.

Entry informationi

Entry nameiLIAS_DROSE
AccessioniPrimary (citable) accession number: B4IAA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 23, 2008
Last modified: July 22, 2015
This is version 41 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.