B6TN12 (LISC1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase 1, chloroplastic
EC=2.8.1.8

Alternative name(s):
Lipoate synthase 1
Short name=LS 1
Short name=Lip-syn 1
Lipoate synthase, plastidial 1
Short name=LIP1p 1
Lipoic acid synthase 1

Gene names

Name:

LIP1P-1

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	361 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 – ?		Chloroplast Potential
	Chain	? – 361		Lipoyl synthase 1, chloroplastic HAMAP-Rule MF_03129		PRO_0000398860
Sites
	Metal binding	87	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	92	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	98	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	124	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	128	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6TN12 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: 8892DCA0C5A85299	FASTA	361	38,828
	10 20 30 40 50 60 MQSSLARPLR PPVLAGRGGR RGLVAVARCH AEAAPPVGTA SRAPAGPYTG RDPEVKKPAW 70 80 90 100 110 120 LRQRAAQGEK YARLRESIGE LKLNTVCVEA QCPNIGECWN GGGGAGGEGD GIATATIMVL 130 140 150 160 170 180 GDTCTRGCRF CAVKTSNKPP PPDPLEPLNT ALAVASWGVD YVVLTSVDRD DLPDGGSSHF 190 200 210 220 230 240 AQTVKALKEL KPGILVECLT SDFRGDLEAI SSLASSGLDV YAHNIETVRS LQRIVRDPRA 250 260 270 280 290 300 GYDQSLAVLK HAKACREGMV TKSSIMLGLG ETDEEVKQAM MDLRAIGVDI LTLGQYLQPT 310 320 330 340 350 360 ERHLTVREYV TPEKFQFWKE YGESVGFRYV ASGPLVRSSY RAGELFVQNL VRNNKTGSSS S

References

[1]

"Insights into corn genes derived from large-scale cDNA sequencing." Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V., Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A. Plant Mol. Biol. 69:179-194(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	EU966377 mRNA. Translation: ACG38495.1.
RefSeq	NP_001150279.1. NM_001156807.1.
UniGene	Zm.23626.
3D structure databases
ProteinModelPortal	B6TN12.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100283909.
KEGG	zma:100283909.
Organism-specific databases
Gramene	B6TN12.
Phylogenomic databases
HOGENOM	HOG000235998.
KO	K03644.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
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

LISC1_MAIZE

Accession

Primary (citable) accession number: B6TN12

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	December 16, 2008
Last modified:	March 6, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program