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B0WAU6 (LIAS_CULQU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:CPIJ004250
OrganismCulex quinquefasciatus (Southern house mosquito) (Culex pungens) [Complete proteome]
Taxonomic identifier7176 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeCuliciniCulexCulex

Protein attributes

Sequence length380 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
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

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? – 380Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398215

Sites

Metal binding1041Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1091Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1351Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1391Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1421Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0WAU6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0DAB0709245B4EF8

FASTA38042,657
        10         20         30         40         50         60 
MKYFFSLPFP KVHTTCKHTA AATASQPLQK IRERLESGPG FQEFVQNPSY NREDWSAYEG 

        70         80         90        100        110        120 
KLKREKGEQD RLRLPPWLKT KIPMGKNFSR IKDQLRELKL ATVCEEAKCP NIGECWGGGE 

       130        140        150        160        170        180 
HGTQTATIML MGDTCTRGCR FCSVKTARAP PPLDPDEPKK TASAIASWGL DYIVLTSVDR 

       190        200        210        220        230        240 
DDLPDGGSNH IAETIREIKR QNPRIFVECL APDFRGNLDC IRTVATSGLD VYAHNIETVE 

       250        260        270        280        290        300 
SLTPFVRDRR AEYRQSLKCL ASVKEINPNM VTKTSIMLGL GETDEQVEQT MKDLRAVGVD 

       310        320        330        340        350        360 
CLTLGQYMQP TKRHLKVIEY VTPEKFKHWE TRGNELGFLY TASGPLVRSS YKAGEFFITS 

       370        380 
ILKNRAAAAA EEATATKPSE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS231875 Genomic DNA. Translation: EDS41812.1.
RefSeqXP_001845830.1. XM_001845778.1.

3D structure databases

ProteinModelPortalB0WAU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7176.CPIJ004250-PA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCPIJ004250-RA; CPIJ004250-PA; CPIJ004250.
GeneID6035696.
KEGGcqu:CpipJ_CPIJ004250.
VectorBaseCPIJ004250. Culex quinquefasciatus.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG7P2XS7.
PhylomeDBB0WAU6.

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_CULQU
AccessionPrimary (citable) accession number: B0WAU6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 37 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