SubmitCancel

Skip Header

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

Q7JQW6

- LIAS_DROME

UniProt

Q7JQW6 - LIAS_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Lipoyl synthase, mitochondrial
Gene
Las, CG5231
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein 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 By similarity.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi103 – 1031Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi108 – 1081Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi134 – 1341Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

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
Complete GO annotation...

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, mitochondrial (EC:2.8.1.8)
Alternative name(s):
Lipoate synthase
Short name:
LS
Short name:
Lip-syn
Lipoic acid synthase
Gene namesi
Name:Las
ORF Names:CG5231
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0029158. Las.

Subcellular locationi

Mitochondrion By similarity 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? – 377Lipoyl synthase, mitochondrialUniRule annotationPRO_0000398219
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PaxDbiQ7JQW6.

Expressioni

Gene expression databases

BgeeiQ7JQW6.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG11808Q7K1H51EBI-126542,EBI-159475

Protein-protein interaction databases

BioGridi65517. 1 interaction.
IntActiQ7JQW6. 1 interaction.
MINTiMINT-1650285.
STRINGi7227.FBpp0288705.

Structurei

3D structure databases

ProteinModelPortaliQ7JQW6.
SMRiQ7JQW6. Positions 125-307.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
GeneTreeiENSGT00390000006234.
InParanoidiQ9VPF7.
KOiK03644.
OMAiPEEPYNT.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ7JQW6.

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.

Q7JQW6-1 [UniParc]FASTAAdd to Basket

« Hide

MLRALKTHAE APIVVATRAA STNAEKLEEI RERLAKGPNF HDFVQNPDNT    50
RNEWEQYDGK LRREKGEEQR LRLPPWLKTT IPVGKNYAKI KAQMRELKLS 100
TVCEEARCPN IGECWGGGEH GTQTATIMLM GDTCTRGCRF CSVKTARKPP 150
PLDVNEPVNT ATAIASWGLD YIVLTSVDRD DLPDGGSEHI AETVREIKAR 200
NSNIFVECLV PDFRGNLECV KTIANSGLDV YAHNIETVEK LTPYVRDRRA 250
HYRQTLQVLT EAKRFNPNLI TKSSIMLGLG ETDEEIENTL KDLREAGVDC 300
VTLGQYMQPT NKHLKVIEYV TPEKFKHWEE RGNELGFLYT ASGPLVRSSY 350
KAGEFFITSI LENRKKRQND TEVPKKQ 377
Length:377
Mass (Da):42,734
Last modified:October 5, 2010 - v2
Checksum:iE702B1AB55DD5DC3
GO

Sequence cautioni

The sequence AAL13786.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAO41414.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014296 Genomic DNA. Translation: AAF51596.2 .
AY058557 mRNA. Translation: AAL13786.1 . Different initiation.
BT003750 mRNA. Translation: AAO41414.1 . Different initiation.
RefSeqi NP_524183.2. NM_079459.3.
UniGenei Dm.2512.

3D structure databases

ProteinModelPortali Q7JQW6.
SMRi Q7JQW6. Positions 125-307.
ModBasei Search...

Protein-protein interaction databases

BioGridi 65517. 1 interaction.
IntActi Q7JQW6. 1 interaction.
MINTi MINT-1650285.
STRINGi 7227.FBpp0288705.

Proteomic databases

PaxDbi Q7JQW6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0290266 ; FBpp0288705 ; FBgn0029158 .
GeneIDi 40259.
KEGGi dme:Dmel_CG5231.

Organism-specific databases

CTDi 40259.
FlyBasei FBgn0029158. Las.

Phylogenomic databases

eggNOGi COG0320.
GeneTreei ENSGT00390000006234.
InParanoidi Q9VPF7.
KOi K03644.
OMAi PEEPYNT.
OrthoDBi EOG7P2XS7.
PhylomeDBi Q7JQW6.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

Miscellaneous databases

GenomeRNAii 40259.
NextBioi 817833.
PROi Q7JQW6.

Gene expression databases

Bgeei Q7JQW6.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiLIAS_DROME
AccessioniPrimary (citable) accession number: Q7JQW6
Secondary accession number(s): Q9VPF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 41 of the entry and version 2 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