B8B016 (LISC2_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase 2, chloroplastic
EC=2.8.1.8

Alternative name(s):
Lipoate synthase 2
Short name=LS 2
Short name=Lip-syn 2
Lipoate synthase, plastidial 2
Short name=LIP1p 2
Lipoic acid synthase 2

Gene names

Name:	LIP1P-2
ORF Names:	OsI_20590

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	384 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_03129
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_03129
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_03129
Subcellular location	Plastid › chloroplast HAMAP-Rule MF_03129.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Gene Ontology (GO)
Cellular_component	chloroplast 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 – 48	48	Chloroplast Potential
	Chain	49 – 384	336	Lipoyl synthase 2, chloroplastic HAMAP-Rule MF_03129		PRO_0000398865
Sites
	Metal binding	108	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	113	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	119	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	145	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	149	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	152	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B8B016 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: 9DA63FA586CDFFA1	FASTA	384	41,545
	10 20 30 40 50 60 MAAYCSRVYH HHPVSPSTMQ GSLARPSIHA GSASLTFRAR PNSVSIVRCD ADSPPEGSAV 70 80 90 100 110 120 AGWAPPGPYT GRDPAARKPA WLRQRAAQGE KYARLRESLG ELKLNTVCVE AQCPNIGECW 130 140 150 160 170 180 NGGGGAGGDG DGIATATIML LGDTCTRGCR FCAVKTSNKP PPPDALEPLR TAVAVASWGV 190 200 210 220 230 240 DYVVLTSVDR DDLPDGGSGH FAQTVKALKE LKPGILVECL TSDFRGDLEA VSSLASSGLD 250 260 270 280 290 300 VFAHNIETVR SLQRIVRDPR AAYDQSLAVL KHAKNCKDGM VTKSSIMLGL GETDEEVKQT 310 320 330 340 350 360 MCDLRAIDVD ILTLGQYLQP TERHLRVREY VTPEKFDFWK EYGESLGFLY VASGPLVRSS 370 380 YRAGELFVQN LVRRKKAELA PTLQ

References

[1]

"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	CM000130 Genomic DNA. Translation: EEC79513.1.
3D structure databases
ProteinModelPortal	B8B016.
ModBase	Search...
Protein-protein interaction databases
STRING	39947.LOC_Os05g43576.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	B8B016.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Gene expression databases
ArrayExpress	B8B016.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_03129. Lipoyl_synth_plantC.
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

LISC2_ORYSI

Accession

Primary (citable) accession number: B8B016

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	March 3, 2009
Last modified:	April 3, 2013
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program