A2XU53 (LIAS_ORYSI) 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
ORF Names:	H0523F07.4, OsI_16128

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	382 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.
Sequence caution	The sequence EAY94363.1 differs from that shown. Reason: Erroneous termination at position 361. Translated as Lys.

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 – 30	30	Mitochondrion Potential
	Chain	31 – 382	352	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398848
Sites
	Metal binding	112	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	117	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	123	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	143	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	147	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	150	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Experimental info
	Sequence conflict	32 – 34	3	TLD → NLE in CAH67016. Ref.1
	Sequence conflict	41 – 45	5	AAAPP → EDDPT in CAH67016. Ref.1
	Sequence conflict	50	1	L → I in CAH67016. Ref.1
	Sequence conflict	55	1	Q → K in CAH67016. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A2XU53 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 754A727161F5B3D0	FASTA	382	41,682
	10 20 30 40 50 60 MHGRRHLAAS LARALTYAPS RSISSTPSLL QTLDPSTPSP AAAPPTAGRL AELRQRLQAD 70 80 90 100 110 120 APSLGDFTYS VEVGTRKKPL PKPKWMKETI PGGAKYAGIK AKLRELKLHT VCEEARCPNL 130 140 150 160 170 180 GECWSGGETG TATATIMILG DTCTRGCRFC NVKTSRTPPP PDPDEPSNVA QAIASWGLEY 190 200 210 220 230 240 IVITSVDRDD LPDQGSGHFA ETVQKLKVLK PEMLIEALVP DFRGDPACVE KVATSGLHVF 250 260 270 280 290 300 AHNIETVEEL QRNVRDHRAN FKQSIDVLKL AKEYAPAGTL TKTSIMLGCG ETPDQVISTM 310 320 330 340 350 360 EKVRAAGVDV MTFGQYMRPS KRHMPVSEYV TPEAFERYRS LGVDMGFRYV ASGPMVRSSY 370 380 KAGEFYIKAM IEADRAKATT AI

References

[1]

"Sequence and analysis of rice chromosome 4." Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B. Nature 420:316-320(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Guang-Lu-Ai No.4.

[2]

"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR855164 Genomic DNA. Translation: CAH67016.1. CM000129 Genomic DNA. Translation: EAY94363.1. Sequence problems.
3D structure databases
ProteinModelPortal	A2XU53.
ModBase	Search...
Protein-protein interaction databases
STRING	39947.LOC_Os04g38330.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	A2XU53.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Gene expression databases
ArrayExpress	A2XU53.
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_ORYSI

Accession

Primary (citable) accession number: A2XU53
Secondary accession number(s): Q01JQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program