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: 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

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

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
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 lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma
ProteomesiUP000008524 Componenti: Chromosome 10

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
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

Interactioni

Protein-protein interaction databases

STRINGi5691.Tb10.61.1530.

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

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ388A7.
KOiK03644.
OMAiCAFCQVE.

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.

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 21, 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

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...

Protein-protein interaction databases

STRINGi5691.Tb10.61.1530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3661775.
KEGGitbr:Tb10.61.1530.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ388A7.
KOiK03644.
OMAiCAFCQVE.

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 of the African trypanosome Trypanosoma brucei."
    Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., Alsmark U.C.M.
    , Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., White O., Whitehead S., Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.
    Science 309:416-422(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 927/4 GUTat10.1Imported.

Entry informationi

Entry nameiLIPA_TRYB2
AccessioniPrimary (citable) accession number: Q388A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 4, 2010
Last sequence update: November 21, 2005
Last modified: March 31, 2015
This is version 62 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.