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Q4QDI6 (LIPA_LEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:LmjF19.0350, LmjF_19_0350
OrganismLeishmania major [Reference proteome]
Taxonomic identifier5664 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length410 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)
   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? – 410Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123PRO_0000398238

Sites

Metal binding1251Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1301Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1361Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1571Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1611Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1641Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QDI6 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 70CED969AE71BD5F

FASTA41045,055
        10         20         30         40         50         60 
MCPTAVPSRV SPVAAAAAAD IAGSSESTVS LVADVDKKNS QYKQIFLERF RKKLQSDKTG 

        70         80         90        100        110        120 
MNNLESFVEL PEGVAPSAAS IGPIKRGSEP LPPWIKLKVP KGMTHRPRFN RIRRSMREKN 

       130        140        150        160        170        180 
LSTVCEEAKC PNIGECWGGS DEEGTATATI MVMGSHCTRG CRFCSVLTSR RPPPLDPEEP 

       190        200        210        220        230        240 
EKVAAAVHEM GVDYIVMTMV DRDDLPDGGA SHVCCCIHTI KKKNPELMLE ALVGDFHGDL 

       250        260        270        280        290        300 
KLVEQLAVTP LSVYAHNIEC VERITPRVRD RRASYRQSLQ TLEHVTKWTN GNMLTKSSIM 

       310        320        330        340        350        360 
LGLGEEEAEV RQTLRDLRTA GVSAVTLGQY LQPSHTRLKV SRYAHPKEFE MWEKEAMDMG 

       370        380        390        400        410 
FLYCASGPMV RSSYRAGEYY IKNILKQRQS AEGGKAAAAA TAVNAGTAIA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR796415 Genomic DNA. Translation: CAJ07120.1.
RefSeqXP_001682612.1. XM_001682560.1.

3D structure databases

ProteinModelPortalQ4QDI6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsLmjF.19.0350:mRNA; LmjF.19.0350:pep; LmjF.19.0350.
GeneID5651134.
KEGGlma:LMJF_19_0350.

Phylogenomic databases

HOGENOMHOG000235998.
KOK03644.
OMAVQKYWTP.
ProtClustDBPTZ00413.

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 nameLIPA_LEIMA
AccessionPrimary (citable) accession number: Q4QDI6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2005
Last modified: February 19, 2014
This is version 53 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