B7FM45 (LIAS_MEDTR) 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

Name:

LIP1

Organism

Medicago truncatula (Barrel medic) (Medicago tribuloides)

Taxonomic identifier

3880 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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_03128
Catalytic activity	Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03128
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_03128
Subcellular location	Mitochondrion By similarity.
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
Gene Ontology (GO)
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate synthase activity Inferred from electronic annotation. Source: EC 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	? – 378		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398847
Sites
	Metal binding	109	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	120	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	140	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	144	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	147	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7FM45 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 26864D640120AAF2	FASTA	378	41,913
	10 20 30 40 50 60 MMYSRFRTVA KNLKSTTKPF SFTTATTTTT VSSSEFPQNL TELRARLARE SPSLSDFISL 70 80 90 100 110 120 KSNNAYSVEV GTKKNPLPKP KWMKESIPGG WKYVQIKKKL RELKLHTVCE EAKCPNMGEC 130 140 150 160 170 180 WSGGETGTAT ATIMILGDTC TRGCRFCNVK TSRTPPPPDP DEPTNVAEAI ASWGLDYVVI 190 200 210 220 230 240 TSVGRDDLPD QGSSHFTETV QKLKILKPSI LIEALVPDFR GNAECVEKVS KSGLDVFAHN 250 260 270 280 290 300 IETVEELQSA VRDHRANFNQ SLDVLRMAKD YAPAGTLTKT SIMLGCGETP DQIVKTMEKV 310 320 330 340 350 360 RAAGVDVMTF GQYMRPSKRH MPVSEYITPE AFEKYQTLGM EMGFRYVASG PMVRSSYKAG 370 EFYIKSMIDS DRAVSSQS

References

[1]	"Medicago truncatula full length cDNA cloning project." Moskal W., Chan A., Cheung F., Xiao Y., Town C.D. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT053168 mRNA. Translation: ACJ85828.1.
3D structure databases
ProteinModelPortal	B7FM45.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_03128. Lipoyl_synth_plantM.
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

LIAS_MEDTR

Accession

Primary (citable) accession number: B7FM45

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	February 10, 2009
Last modified:	March 6, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program