C5XKZ1 (LISC_SORBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase, chloroplastic
EC=2.8.1.8

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

Gene names

Name:	LIP1P
Ordered Locus Names:	Sb03g035760

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	368 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_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
Technical term	Complete proteome Reference proteome
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	? – 368		Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129		PRO_0000398870
Sites
	Metal binding	94	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	99	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	105	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	135	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	138	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C5XKZ1 [UniParc]. Last modified September 1, 2009. Version 1. Checksum: B63753E5085C935C	FASTA	368	39,528
	10 20 30 40 50 60 MQSSLARPLR PPVLAGCGGR RGHGAPRGSV SVARCRAEAA PPTVGTASRA PAGPYTGRDP 70 80 90 100 110 120 EVKKPAWLRQ RAAQGDKYAR LRESIGELKL NTVCVEAQCP NIGECWNGGG GAGGEGDGIA 130 140 150 160 170 180 TATIMVLGDT CTRGCRFCAV KTSNKPPPPD PLEPLNTALA VASWGVDYVV LTSVDRDDLP 190 200 210 220 230 240 DGGSSHFAQT VRALKELKPG ILVECLTSDF RGDLEAVSSL ANSGLDVYAH NIETVRSLQR 250 260 270 280 290 300 IVRDPRAGYD QSLAVLKHAK DCREGMITKS SIMLGLGETD EEVKQAMIDL RAIGVDILTL 310 320 330 340 350 360 GQYLQPTERH LTVREYVTPE KFQFWKEYGE SVGFRYVASG PLVRSSYRAG ELFVQNLVRN NKTGSSSS

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	CM000762 Genomic DNA. Translation: EES01528.1.
RefSeq	XP_002456408.1. XM_002456363.1.
3D structure databases
ProteinModelPortal	C5XKZ1.
ModBase	Search...
Protein-protein interaction databases
STRING	4558.Sb03g035760.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8072124.
KEGG	sbi:SORBI_03g035760.
Organism-specific databases
Gramene	C5XKZ1.
Phylogenomic databases
eggNOG	COG0320.
KO	K03644.
OMA	PSAHHLP.
ProtClustDB	PLN02428.
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

LISC_SORBI

Accession

Primary (citable) accession number: C5XKZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	September 1, 2009
Last modified:	April 3, 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