Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

Tb10.61.1530

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Status
Reviewed-Annotation score: -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

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 + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [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)DescriptionActionsGraphical viewLength
Metal bindingi125Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi130Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi136Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi159Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi163Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi166Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Ligand4Fe-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 lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma
Proteomesi
  • UP000008524 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiTriTrypDB:Tb927.10.15010

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003982391 – 409Lipoyl synthase, mitochondrialAdd BLAST409

Proteomic databases

PaxDbiQ388A7

Interactioni

Protein-protein interaction databases

STRINGi5691.EAN78865

Structurei

3D structure databases

ProteinModelPortaliQ388A7
SMRiQ388A7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000235998
InParanoidiQ388A7
KOiK03644
OMAiPYCDIDF

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR007197 rSAM
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF005963 Lipoyl_synth, 1 hit
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

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

Similar proteinsi

Entry informationi

Entry nameiLIPA_TRYB2
AccessioniPrimary (citable) accession number: Q388A7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 22, 2005
Last modified: May 23, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health