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Q16W22 (LIAS_AEDAE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
ORF Names:AAEL009368
OrganismAedes aegypti (Yellowfever mosquito) (Culex aegypti) [Reference proteome]
Taxonomic identifier7159 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeAediniAedesStegomyia

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_03123

Catalytic activity

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. HAMAP-Rule MF_03123

Cofactor

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

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03123

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03123.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 393Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398214

Sites

Metal binding1111Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1161Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1221Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1421Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1461Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1491Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q16W22 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 54EF5326151DF5D9

FASTA39344,306
        10         20         30         40         50         60 
MSQISSNLLR NTVQNGKFGC LKNSIQCKHT AANPLEKIRE RLESGPSFQD FVQNPSYNRD 

        70         80         90        100        110        120 
DWTDYEGKLR REKGENDRLR LPPWLKTKIP MGKNFSRIKD QLRELKLATV CEEAKCPNIG 

       130        140        150        160        170        180 
ECWGGGEHGT QTATIMLMGD TCTRGCRFCS VKTARVPPPL DPAEPTNTAS AIASWGLDYI 

       190        200        210        220        230        240 
VLTSVDRDDL PDGGSNHIAA TIREIKRQNP RIFVECLAPD FRGDLECVKV VAQSGLDVYA 

       250        260        270        280        290        300 
HNIETVEALT PFVRDRRARY RQSLDVLRSI KEINPSMITK TSIMLGLGET DEQIEQTMKD 

       310        320        330        340        350        360 
LRSVGVDCLT LGQYMQPTKR HLKVIEYVTP EKFKHWETRG NELGFLYTAS GPLVRSSYKA 

       370        380        390 
GEFFITSILK NRAEEAERRK EAAGGQDTKT EQT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH477577 Genomic DNA. Translation: EAT38774.1.
RefSeqXP_001659989.1. XM_001659939.1.
UniGeneAae.14529.

3D structure databases

ProteinModelPortalQ16W22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7159.AAEL009368-PA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAAEL009368-RA; AAEL009368-PA; AAEL009368.
GeneID5571879.
KEGGaag:AaeL_AAEL009368.
VectorBaseAAEL009368. Aedes aegypti.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAHPHIPTK.
OrthoDBEOG7P2XS7.
PhylomeDBQ16W22.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIAS_AEDAE
AccessionPrimary (citable) accession number: Q16W22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 25, 2006
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways