Q388A7 (LIPA_TRYB2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase, mitochondrial
EC=2.8.1.8

Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase

Gene names

ORF Names:

Tb10.61.1530

Organism

Trypanosoma brucei brucei (strain 927/4 GUTat10.1) [Reference proteome]

Taxonomic identifier

999953 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei › Trypanosoma brucei brucei

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP-Rule MF_03123
Catalytic activity	Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03123
Cofactor	Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03123
Subcellular location	Mitochondrion By similarity HAMAP-Rule MF_03123.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-HAMAP lipoate synthase activity Inferred from electronic annotation. Source: UniProtKB-HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 409		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000398239
Sites
	Metal binding	125	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	130	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	136	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	159	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	163	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	166	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q388A7 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: C622CA44663B9186	FASTA	409	45,476
	10 20 30 40 50 60 MFQRWSFALC RPIVAAAQVS QQQVPPSEEP RNESGAANPP LVKEEFLRQF RERLANDKTG 70 80 90 100 110 120 RNSLEGFLDL PENLPPTAAS IGPLKRGKEP LPPWLKLKVP MGASRQPRFN KIRRNMREKR 130 140 150 160 170 180 LATVCEEAKC PNIGECWGGG DEEGDGTATA TIMVMGAHCT RGCRFCSVMT SRTPPPLDPE 190 200 210 220 230 240 EPRKTADAVA DMGVEYIVMT MVDRDDLADG GAAHVVRCVT AVKERNPGLL LEALVGDFHG 250 260 270 280 290 300 DLKLVEMVAG SPLNVYAHNI ECVERITPNV RDRRASYRQS LKVLEHVNNF TKGAMLTKSS 310 320 330 340 350 360 IMLGLGEKEE EVRQTLRDLR TAGVSAVTLG QYLQPSRTRL KVSRYAHPKE FEMWEKEALD 370 380 390 400 MGFLYCASGP MVRSSYRAGE YYIKNILKQR ETVEAPSVSD GGNEPKDSE

References

[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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 927/4 GUTat10.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000208 Genomic DNA. Translation: EAN78865.1.
RefSeq	XP_827977.1. XM_822884.1.
3D structure databases
ProteinModelPortal	Q388A7.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	5691.Tb10.61.1530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3661775.
KEGG	tbr:Tb10.61.1530.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OMA	HPHIPTK.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR003698. Lipoyl_synth. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005963. Lipoyl_synth. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LIPA_TRYB2

Accession

Primary (citable) accession number: Q388A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	November 22, 2005
Last modified:	June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)