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Protein

Lipoyl synthase 1, mitochondrial

Gene

Tc00.1047053511291.30

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathway:iprotein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyl synthase 1, mitochondrial (Tc00.1047053511291.30), Lipoyl synthase 2, mitochondrial (Tc00.1047053506211.10)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi127 – 1271Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi159 – 1591Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi166 – 1661Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase 1, mitochondrial (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthase 1UniRule annotation
Short name:
LS 1UniRule annotation
Short name:
Lip-syn 1UniRule annotation
Lipoic acid synthase 1UniRule annotation
Gene namesi
ORF Names:Tc00.1047053511291.30
OrganismiTrypanosoma cruzi (strain CL Brener)
Taxonomic identifieri353153 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
ProteomesiUP000002296 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 423Lipoyl synthase 1, mitochondrialPRO_0000398241
Transit peptidei1 – ?MitochondrionUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi353153.XP_811939.1.

Structurei

3D structure databases

ProteinModelPortaliQ4DC43.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK03644.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4DC43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHRHLCKLC SKTPSAATLA SPLGKLQEER GEGVAKDLKK DKQHRQIFLQ
60 70 80 90 100
KFRERLDSDT TGKNTLAGFI DLPEGISPTM AAVGPLKRGE EPLPPWLKMK
110 120 130 140 150
VAKGVSRLPR FNSIRKSMRE KRLATVCEEA KCPNIGECWG GDEEEGTATA
160 170 180 190 200
TIMVMGSHCT RGCRFCSVLT SRTPPPLDPD EPQKVANAVA EMGVDYIVMT
210 220 230 240 250
MVDRDDLNDG GAAHVVRCVN AIKEKNPLLL LEALVGDFHG DLKLVETVAL
260 270 280 290 300
SPLSVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNSF TKGAMLTKSS
310 320 330 340 350
IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPARTRL KVSRYAHPKE
360 370 380 390 400
FQMWEEEAMA MGFLYCASGP LVRSSYRAGE YYIKSLVKQR GAAATKSNTT
410 420
TTTTNTASLA AATVTDSATL QGE
Length:423
Mass (Da):46,531
Last modified:September 13, 2005 - v1
Checksum:i7EBC5CA8279BA97D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHK01000671 Genomic DNA. Translation: EAN90088.1.
RefSeqiXP_811939.1. XM_806846.1.

Genome annotation databases

GeneIDi3543008.
KEGGitcr:511291.30.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHK01000671 Genomic DNA. Translation: EAN90088.1.
RefSeqiXP_811939.1. XM_806846.1.

3D structure databases

ProteinModelPortaliQ4DC43.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353153.XP_811939.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3543008.
KEGGitcr:511291.30.

Phylogenomic databases

KOiK03644.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
    El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L.
    , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
    Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CL Brener.

Entry informationi

Entry nameiLIPA1_TRYCC
AccessioniPrimary (citable) accession number: Q4DC43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: September 13, 2005
Last modified: June 24, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.