C5Y9R0 (LIAS_SORBI) 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
Ordered Locus Names:	Sb06g018660

Organism

Sorghum bicolor (Sorghum) (Sorghum vulgare) [Reference proteome]

Taxonomic identifier

4558 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Sorghum

Protein attributes

Sequence length	386 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_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
Technical term	Complete proteome Reference proteome
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	? – 386		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398856
Sites
	Metal binding	113	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	118	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	124	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	144	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	148	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	151	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C5Y9R0 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: A19F3845489C859C	FASTA	386	42,141
	10 20 30 40 50 60 MHGRRHLAAS LTRALTQAPS RSISSTPSLL QTLDPSVPSP SPPPAAEPGR LAELRRRLQA 70 80 90 100 110 120 DAPSLGDFAY SVEVGTRQRP LPKPKWMKET VPGGAKYAAI KAKLRELKLH TVCEEARCPN 130 140 150 160 170 180 LGECWSGGET GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPDEPSNV AQAIASWGLE 190 200 210 220 230 240 YIVITSVDRD DLPDQGSGHF AETVQKLKAL KPEMLIEALV PDFRGDPSCV EKVATSGLHV 250 260 270 280 290 300 FAHNIETVEE LQRNVRDYRA NFKQSIDVLK MAKEYAPPGT LTKTSIMLGC GETPDQVIST 310 320 330 340 350 360 MEKVRAAGVD VITFGQYMRP SKRHMPVSEY VTPEAFEKYR ALGVEMGFRY VASGPMVRSS 370 380 YKAGEFYIKA MIEADRSKAT TADSSA

References

[1]

"The Sorghum bicolor genome and the diversification of grasses." Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., Feltus F.A. , Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman M., Ware D., Westhoff P., Mayer K.F.X., Messing J., Rokhsar D.S. Nature 457:551-556(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. BTx623.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000765 Genomic DNA. Translation: EES12278.1.
RefSeq	XP_002447950.1. XM_002447905.1.
UniGene	Sbi.15755.
3D structure databases
ProteinModelPortal	C5Y9R0.
ModBase	Search...
Protein-protein interaction databases
STRING	4558.Sb06g018660.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8057459.
KEGG	sbi:SORBI_06g018660.
Organism-specific databases
Gramene	C5Y9R0.
Phylogenomic databases
eggNOG	COG0320.
KO	K03644.
OMA	PIGKASE.
ProtClustDB	PLN02428.
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_SORBI

Accession

Primary (citable) accession number: C5Y9R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	September 1, 2009
Last modified:	April 3, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program