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Q6GQ48 (LIAS_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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
Name:lias
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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
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? – 372Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398212

Sites

Metal binding1061Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1111Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1171Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6GQ48 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 905039EBFE3CC48C

FASTA37241,803
        10         20         30         40         50         60 
MRQCGLVRAA QLLRTCGLAE WHTPYRALSS LPDEKKELIK NGPDLQDFLS GELVDKSSWA 

        70         80         90        100        110        120 
AYKGDLKRQK GERLRLPPWV KTEIPMGKNY NKLKNTLRNL NLHTVCEEAR CPNIGECWGG 

       130        140        150        160        170        180 
GEYGTATATI MLMGDTCTRG CRFCSVKTAR NPPPLDPDEP YNTSKAIAEW GLDYVVLTSV 

       190        200        210        220        230        240 
DRDDISDGGA EHIAQTVSML KERNKTILIE CLTPDFRGNM KAVETVAKSG LDVYAHNVET 

       250        260        270        280        290        300 
VPALQRHVRD PRANFDQSLN VLKHAKNVRP DLVSKTSIML GLGETDEQIY STMKALREAG 

       310        320        330        340        350        360 
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKAGNELGF LYTASGPLVR SSYKAGEFFL 

       370 
KNLIEKRKTK AI 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC072900 mRNA. Translation: AAH72900.1.
RefSeqNP_001085534.1. NM_001092065.1.
UniGeneXl.55041.

3D structure databases

ProteinModelPortalQ6GQ48.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID443960.
KEGGxla:443960.

Organism-specific databases

CTD11019.
XenbaseXB-GENE-6251515. lias.

Phylogenomic databases

HOVERGENHBG023328.
KOK03644.

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_XENLA
AccessionPrimary (citable) accession number: Q6GQ48
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways