A9NNH7 (LIAS_PICSI) 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

Organism

Picea sitchensis (Sitka spruce) (Pinus sitchensis)

Taxonomic identifier

3332 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Coniferophyta › Coniferopsida › Coniferales › Pinaceae › Picea

Protein attributes

Sequence length	386 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.

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 – ?		Mitochondrion Potential
	Chain	? – 386		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398853
Sites
	Metal binding	115	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	120	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	126	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	146	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	150	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	153	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NNH7 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 0FAA92A285A950F8	FASTA	386	42,579
	10 20 30 40 50 60 MSINPAFLRR ITWGSKSLHH QFTRCQVRAL SSSVEQTPES TTPALSALRE RLANGGPTLS 70 80 90 100 110 120 DFLTRNLGEE PYSVDVGTKK NPLPKPKWMK AAVPGGDKYT AIKAKLREMN LHTVCEEAKC 130 140 150 160 170 180 PNLGECWSGG ETGTATATIM ILGDTCTRGC RFCAVKTSRT PPPPDPNEPT NVAEAIVSWG 190 200 210 220 230 240 LDYVVLTSVD RDDLPDQGSG HFAKTVQKLK QLKPKMLVEA LVPDFQGNSE CVQKVATSGL 250 260 270 280 290 300 DVFAHNIETV EELQRVVRDH RANFNQSLEV LKMAKTYSPL GVLTKTSVML GCGETPAQVI 310 320 330 340 350 360 ETMEKVREAG VDVITFGQYM RPTKRHMAVS EYVTPEAFEK YQKLGMEMGF RYVASGPMVR 370 380 SSYKAGEFYI KSMIEDDRKK ASSSSI

References

[1]

"A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464 high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea sitchensis)." Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E., Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A., Douglas C.J., Ritland K., Bohlmann J. BMC Genomics 9:484-484(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF082836 mRNA. Translation: ABK22188.1.
3D structure databases
ProteinModelPortal	A9NNH7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
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_PICSI

Accession

Primary (citable) accession number: A9NNH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	February 5, 2008
Last modified:	March 6, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program