B7FRU7 (LIPA1_PHATC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase 1, mitochondrial
EC=2.8.1.8

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

Gene names

ORF Names:

PHATRDRAFT_18029

Organism

Phaeodactylum tricornutum (strain CCAP 1055/1) [Reference proteome]

Taxonomic identifier

556484 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Stramenopiles › Bacillariophyta › Bacillariophyceae › Bacillariophycidae › Naviculales › Phaeodactylaceae › Phaeodactylum › Phaeodactylum tricornutum

Protein attributes

Sequence length	401 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_03123
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_03123
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_03123
Subcellular location	Mitochondrion Potential HAMAP-Rule MF_03123.
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from electronic annotation. Source: HAMAP 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 – 25	25	Mitochondrion Potential
	Chain	26 – 401	376	Lipoyl synthase 1, mitochondrial HAMAP-Rule MF_03123		PRO_0000398243
Sites
	Metal binding	117	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	122	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	128	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	148	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	152	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	155	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7FRU7 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: C5270EA0E1E231A9	FASTA	401	44,192
	10 20 30 40 50 60 MWSSSSSLCR NPSFRRAWLS TVTVTQTAAP TSSRLAALRT QLATEEASID DFSSTNAPTT 70 80 90 100 110 120 TTHYTSSNGS PIVRQKAAPR SAKILPKPRW LKAAPATSDN YRKLRDTVRE LGLATVCEEA 130 140 150 160 170 180 RCPNIGECWG GGEDQTATAT IMIMGDTCTR GCRFCSVKTS RAPPPLDPHE PEKVATAIAQ 190 200 210 220 230 240 WGLDYVVLTS VDRDDLPDQG ADHFRQVVTQ LKLKKPSLLV EALTPDFQGN MDLVHAVATS 250 260 270 280 290 300 GLDVYAHNME TVEALTPKVR DRRATYRQSL EVLRYVKTIQ SDPIGTTNNH NNNNGCLTKT 310 320 330 340 350 360 SLMLGLGETD DQVLTTLRDL RDADVDVVTF GQYLQPTKKH LPVQEYVTPE KFDFWQETAM 370 380 390 400 GMGFAYVASG PLVRSSYKAG ELFLQKYIAQ KKQRNAEVAA A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Phaeodactylum genome reveals the evolutionary history of diatom genomes." Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A., Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T. , Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y., Grigoriev I.V. Nature 456:239-244(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CCAP 1055/1.
[2]	Diatom Consortium Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S., Rokhsar D., Bowler C. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: CCAP 1055/1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000606 Genomic DNA. Translation: EEC50372.1.
RefSeq	XP_002177558.1. XM_002177522.1.
UniGene	Ptc.7635.
3D structure databases
ProteinModelPortal	B7FRU7.
ModBase	Search...
Protein-protein interaction databases
STRING	2850.JGI18029.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	Phatr18029; Phatr18029; Phatr18029.
GeneID	7197080.
KEGG	pti:PHATRDRAFT_18029.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
ProtClustDB	PLN02428.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
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

LIPA1_PHATC

Accession

Primary (citable) accession number: B7FRU7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	February 10, 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)