Tb10.61.1530

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

Miscellaneous

This protein may be expected to contain an N-terminal transit peptide but none has been predicted.UniRule annotation

Catalytic activityⁱ

Protein N₆-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N₆-(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:

no protein annotated in this organism
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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	125	Iron-sulfur 1 (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	130	Iron-sulfur 1 (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	136	Iron-sulfur 1 (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	159	Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation	1
Metal bindingⁱ	163	Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation	1
Metal bindingⁱ	166	Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation	1

GO - Molecular functionⁱ

4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
lipoate synthase activity Source: GO_Central
metal ion binding Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

lipoate biosynthetic process Source: GO_Central
protein lipoylation Source: GO_Central

Complete GO annotation...

Keywordsⁱ

Molecular function	Transferase
Ligand	4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayⁱ	UPA00538; UER00593.

UniPathwayⁱ

UPA00538; 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
Organismⁱ	Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Taxonomic identifierⁱ	185431 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei › Trypanosoma brucei brucei
Proteomesⁱ	UP000008524 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	TriTrypDB:Tb927.10.15010.

EuPathDBⁱ

TriTrypDB:Tb927.10.15010.

Subcellular locationⁱ

Mitochondrion
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03123

GO - Cellular componentⁱ

mitochondrion
Source: GeneDB
Inferred from sequence modelⁱ
- 15223320

Complete GO annotation...

Keywords - Cellular componentⁱ

Mitochondrion

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000398239	1 – 409	Lipoyl synthase, mitochondrialAdd BLAST		409

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	5691.EAN78865.

STRINGⁱ

5691.EAN78865.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q388A7.
SMRⁱ	Q388A7.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

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

Phylogenomic databases

HOGENOMⁱ	HOG000235998.
InParanoidⁱ	Q388A7.
KEGG Orthology (KO) More...KOⁱ	K03644.
OMAⁱ	PYCDIDF.

Family and domain databases

Gene3Dⁱ	3.20.20.70. 1 hit.
HAMAPⁱ	MF_00206. Lipoyl_synth. 1 hit.
InterProⁱ	View protein in InterPro IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR031691. LIAS_N. IPR003698. Lipoyl_synth. IPR007197. rSAM.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16881. LIAS_N. 1 hit. PF04055. Radical_SAM. 1 hit.
PIRSFⁱ	PIRSF005963. Lipoyl_synth. 1 hit.
SFLDⁱ	SFLDG01058. lipoyl_synthase_like. 1 hit.
SMARTⁱ	View protein in SMART SM00729. Elp3. 1 hit.
TIGRFAMsⁱ	TIGR00510. lipA. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q388A7-1 [UniParc]FASTA Add 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.
NCBI Reference Sequences More...RefSeqⁱ	XP_827977.1. XM_822884.1.

Genome annotation databases

EnsemblProtistsⁱ	EPrT00001300334; EPrP00001314892; EPrG00001288062.
GeneDBⁱ	Tb927.10.15010:pep.
GeneIDⁱ	3661775.
KEGGⁱ	tbr:Tb10.61.1530.

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.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CM000208 Genomic DNA. Translation: EAN78865.1.
NCBI Reference Sequences More...RefSeqⁱ	XP_827977.1. XM_822884.1.

3D structure databases

ProteinModelPortalⁱ	Q388A7.
SMRⁱ	Q388A7.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	5691.EAN78865.

STRINGⁱ

5691.EAN78865.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblProtistsⁱ	EPrT00001300334; EPrP00001314892; EPrG00001288062.
GeneDBⁱ	Tb927.10.15010:pep.
GeneIDⁱ	3661775.
KEGGⁱ	tbr:Tb10.61.1530.

Organism-specific databases

EuPathDBⁱ	TriTrypDB:Tb927.10.15010.

EuPathDBⁱ

TriTrypDB:Tb927.10.15010.

Phylogenomic databases

HOGENOMⁱ	HOG000235998.
InParanoidⁱ	Q388A7.
KEGG Orthology (KO) More...KOⁱ	K03644.
OMAⁱ	PYCDIDF.

Enzyme and pathway databases

UniPathwayⁱ	UPA00538; UER00593.

UniPathwayⁱ

UPA00538; UER00593.

Family and domain databases

Gene3Dⁱ	3.20.20.70. 1 hit.
HAMAPⁱ	MF_00206. Lipoyl_synth. 1 hit.
InterProⁱ	View protein in InterPro IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR031691. LIAS_N. IPR003698. Lipoyl_synth. IPR007197. rSAM.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16881. LIAS_N. 1 hit. PF04055. Radical_SAM. 1 hit.
PIRSFⁱ	PIRSF005963. Lipoyl_synth. 1 hit.
SFLDⁱ	SFLDG01058. lipoyl_synthase_like. 1 hit.
SMARTⁱ	View protein in SMART SM00729. Elp3. 1 hit.
TIGRFAMsⁱ	TIGR00510. lipA. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LIPA_TRYB2
Accessionⁱ	Q388A7Primary (citable) accession number: Q388A7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
	Last sequence update:	November 22, 2005
	Last modified:	July 5, 2017
	This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q388A7 (LIPA_TRYB2)

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Lipoyl synthase, mitochondrial

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein lipoylation via endogenous pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: protein lipoylation via endogenous pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ