Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi106 – 1061Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi112 – 1121Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi132 – 1321Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi136 – 1361Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi139 – 1391Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
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:GA18753
OrganismiDrosophila pseudoobscura pseudoobscura (Fruit fly)
Taxonomic identifieri46245 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000001819 Componenti: Partially assembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0078753. Dpse\GA18753.

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 374Lipoyl synthase, mitochondrialPRO_0000398221
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi7237.FBpp0275593.

Structurei

3D structure databases

ProteinModelPortaliQ2LYK1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiQ2LYK1.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ2LYK1.

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.

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_001354086.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ2LYK1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7237.FBpp0275593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

FlyBaseiFBgn0078753. Dpse\GA18753.

Phylogenomic databases

eggNOGiCOG0320.
InParanoidiQ2LYK1.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ2LYK1.

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. "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
    Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L.
    , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A.
    Genome Res. 15:1-18(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MV2-25 / Tucson 14011-0121.94.

Entry informationi

Entry nameiLIAS_DROPS
AccessioniPrimary (citable) accession number: Q2LYK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 21, 2006
Last modified: March 4, 2015
This is version 63 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.