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UniProtKB - Q388A7 (LIPA_TRYB2)

UniProt

Q388A7 - LIPA_TRYB2

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Protein

Lipoyl synthase, mitochondrial

Gene

Tb10.61.1530

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
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

Pathwayi: protein 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, mitochondrial (Tb10.61.1530)
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 bindingi125 – 1251Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi130 – 1301Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi136 – 1361Iron-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, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
ORF Names:Tb10.61.1530
OrganismiTrypanosoma brucei brucei (strain 927/4 GUTat10.1)
Taxonomic identifieri185431 [NCBI]
Taxonomic lineageiEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma ›
Proteomesi
  • UP000008524 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiTriTrypDB:Tb927.10.15010.

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? – 409Lipoyl synthase, mitochondrialPRO_0000398239
Transit peptidei1 – ?MitochondrionUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ388A7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiQ388A7.
KOiK03644.
OMAiVQKYWTP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. 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.

Q388A7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQRWSFALC RPIVAAAQVS QQQVPPSEEP RNESGAANPP LVKEEFLRQF 
        60         70         80         90        100
RERLANDKTG RNSLEGFLDL PENLPPTAAS IGPLKRGKEP LPPWLKLKVP 
       110        120        130        140        150
MGASRQPRFN KIRRNMREKR LATVCEEAKC PNIGECWGGG DEEGDGTATA 
       160        170        180        190        200
TIMVMGAHCT RGCRFCSVMT SRTPPPLDPE EPRKTADAVA DMGVEYIVMT 
       210        220        230        240        250
MVDRDDLADG GAAHVVRCVT AVKERNPGLL LEALVGDFHG DLKLVEMVAG 
       260        270        280        290        300
SPLNVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNNF TKGAMLTKSS 
       310        320        330        340        350
IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPSRTRL KVSRYAHPKE 
       360        370        380        390        400
FEMWEKEALD MGFLYCASGP MVRSSYRAGE YYIKNILKQR ETVEAPSVSD 

GGNEPKDSE
Length:409
Mass (Da):45,476
Last modified:November 22, 2005 - v1
Checksum:iC622CA44663B9186
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000208 Genomic DNA. Translation: EAN78865.1.
RefSeqiXP_827977.1. XM_822884.1.

Genome annotation databases

GeneDBiTb927.10.15010:pep.
GeneIDi3661775.
KEGGitbr:Tb10.61.1530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000208 Genomic DNA. Translation: EAN78865.1.
RefSeqiXP_827977.1. XM_822884.1.

3D structure databases

ProteinModelPortaliQ388A7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiTb927.10.15010:pep.
GeneIDi3661775.
KEGGitbr:Tb10.61.1530.

Organism-specific databases

EuPathDBiTriTrypDB:Tb927.10.15010.

Phylogenomic databases

HOGENOMiHOG000235998.
InParanoidiQ388A7.
KOiK03644.
OMAiVQKYWTP.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR031691. LIAS_N.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF16881. LIAS_N. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_TRYB2
AccessioniPrimary (citable) accession number: Q388A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 22, 2005
Last modified: September 7, 2016
This is version 71 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

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 one 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.