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Q4DC43 (LIPA1_TRYCC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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 1, mitochondrial

EC=2.8.1.8
Alternative name(s):
Lipoate synthase 1
Short name=LS 1
Short name=Lip-syn 1
Lipoic acid synthase 1
Gene names
ORF Names:Tc00.1047053511291.30
OrganismTrypanosoma cruzi (strain CL Brener) [Complete proteome]
Taxonomic identifier353153 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Protein attributes

Sequence length423 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? – 423Lipoyl synthase 1, mitochondrial HAMAP-Rule MF_03123PRO_0000398241

Sites

Metal binding1271Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4DC43 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 7EBC5CA8279BA97D

FASTA42346,531
        10         20         30         40         50         60 
MFHRHLCKLC SKTPSAATLA SPLGKLQEER GEGVAKDLKK DKQHRQIFLQ KFRERLDSDT 

        70         80         90        100        110        120 
TGKNTLAGFI DLPEGISPTM AAVGPLKRGE EPLPPWLKMK VAKGVSRLPR FNSIRKSMRE 

       130        140        150        160        170        180 
KRLATVCEEA KCPNIGECWG GDEEEGTATA TIMVMGSHCT RGCRFCSVLT SRTPPPLDPD 

       190        200        210        220        230        240 
EPQKVANAVA EMGVDYIVMT MVDRDDLNDG GAAHVVRCVN AIKEKNPLLL LEALVGDFHG 

       250        260        270        280        290        300 
DLKLVETVAL SPLSVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNSF TKGAMLTKSS 

       310        320        330        340        350        360 
IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPARTRL KVSRYAHPKE FQMWEEEAMA 

       370        380        390        400        410        420 
MGFLYCASGP LVRSSYRAGE YYIKSLVKQR GAAATKSNTT TTTTNTASLA AATVTDSATL 


QGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHK01000671 Genomic DNA. Translation: EAN90088.1.
RefSeqXP_811939.1. XM_806846.1.

3D structure databases

ProteinModelPortalQ4DC43.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3543008.
KEGGtcr:511291.30.

Phylogenomic databases

KOK03644.
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 nameLIPA1_TRYCC
AccessionPrimary (citable) accession number: Q4DC43
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 46 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