Q9ZWT1 (LIAS_ARATH) 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:	At2g20860
ORF Names:	F5H14.17

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	374 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. Ref.1
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 Ref.1.
Tissue specificity	Expressed in leaves and flowers, but not in roots. Ref.1
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	glycine catabolic process Traceable author statement Ref.1. Source: TAIR
Cellular_component	mitochondrial matrix Inferred from direct assay Ref.1. Source: TAIR
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW lipoate synthase activity Inferred from genetic interaction Ref.1. Source: TAIR 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 – 19	19	Mitochondrion Potential
	Chain	20 – 374	355	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398844
Sites
	Metal binding	103	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	108	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	134	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	138	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	141	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZWT1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 9527359AA5E9AF6A	FASTA	374	41,344
	10 20 30 40 50 60 MHSRSALLYR FLRPASRCFS SSSAVTPVTV TQSPKSLEAL RARLANESPS LTDFIHGDTY 70 80 90 100 110 120 SVEVGTKKKP LPKPKWMKES IPGGERYVQI KKKLRDLKLH TVCEEAKCPN LGECWSGGET 130 140 150 160 170 180 GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPNEPNNV AEAIASWGVD YVVITSVDRD 190 200 210 220 230 240 DLPDQGSGHF AETVQRLKFL KPEMLIEALV PDFRGDGGCV EKVSKSGLDV LAHNIETVEE 250 260 270 280 290 300 LQSFVRDHRA NFKQSLDVLR MAKEYAPAGT LTKTSVMLGC GETPDQVVKT MEKVRAAGVD 310 320 330 340 350 360 VMTFGQYMRP SKRHMPVAEY VTPDAFERYR LLGMEMGFRY VASGPMVRSS YKAGEYYIKS 370 MIEADRVASP STSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization of the cDNA for lipoic acid synthase." Yasuno R., Wada H. Plant Physiol. 118:935-943(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB007987 mRNA. Translation: BAA34701.1. AC006234 Genomic DNA. Translation: AAD20909.1. CP002685 Genomic DNA. Translation: AEC07088.1. AY035143 mRNA. Translation: AAK59647.1. AF424583 mRNA. Translation: AAL11577.1. AY059077 mRNA. Translation: AAL15183.1.
IPI	IPI00539120.
PIR	T44259.
RefSeq	NP_179682.1. NM_127655.3.
UniGene	At.21247.
3D structure databases
ProteinModelPortal	Q9ZWT1.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G20860.1-P.
Proteomic databases
PaxDb	Q9ZWT1.
PRIDE	Q9ZWT1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G20860.1; AT2G20860.1; AT2G20860.
GeneID	816619.
KEGG	ath:AT2G20860.
Organism-specific databases
TAIR	At2g20860.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
InParanoid	Q9ZWT1.
KO	K03644.
OMA	PIGKASE.
ProtClustDB	PLN02428.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Gene expression databases
Genevestigator	Q9ZWT1.
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_ARATH

Accession

Primary (citable) accession number: Q9ZWT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program