B9H5L9 (LIAS_POPTR) 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
ORF Names:	POPTRDRAFT_558638

Organism

Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [Reference proteome]

Taxonomic identifier

3694 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Salicaceae › Saliceae › Populus

Protein attributes

Sequence length	385 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_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 HAMAP-Rule MF_03128.
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 – ?		Mitochondrion Potential
	Chain	? – 385		Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128		PRO_0000398854
Sites
	Metal binding	113	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	118	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	124	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	144	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	148	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	151	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9H5L9 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 00A96913F7A8D1A1	FASTA	385	42,613
	10 20 30 40 50 60 MQSRFTFLAT RTLKSTTTKA KNRTFSSSTV ESSTKQPPQF SQTLAGLRAR LAVESPTLSD 70 80 90 100 110 120 FIHLQSNNTY SVEVGTKKKP LPKPKWMREA IPGGEKYVQI KKKLRELKLH TVCEEAKCPN 130 140 150 160 170 180 LGECWSGGET GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPNEPTNV AEAIASWGLD 190 200 210 220 230 240 YVVITSVDRD DLADQGSGHF AETVHKLKTL KPNMLIEALV PDFRGDRGCV EKVAKSGLDV 250 260 270 280 290 300 FAHNIETVEE LQSSVRDHRA NFKQSLDVLM MAKEYAPPGT LTKTSIMLGC GEAPEQVVKT 310 320 330 340 350 360 MEKVRAAGVD VMTFGQYMRP SKRHMPVSEY ITPDAFEKYK TLGMEMGFRY VASGPMVRSS 370 380 YKAGEFYIKS MIESDRSVSS QLPIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)." Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A. , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S. Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nisqually.
[2]	US DOE Joint Genome Institute (JGI-PGF) Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S., Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S., Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M. , Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B., Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D., Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J., Tuskan G., Rokhsar D. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Nisqually.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000341 Genomic DNA. Translation: EEE93357.1.
RefSeq	XP_002306361.1. XM_002306325.1.
3D structure databases
ProteinModelPortal	B9H5L9.
ModBase	Search...
Protein-protein interaction databases
STRING	3694.eugene3.00050253.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	POPTR_0005s08840.1; POPTR_0005s08840.1; POPTR_0005s08840.
GeneID	7486347.
KEGG	pop:POPTR_558638.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OMA	RRPIGNA.
ProtClustDB	PLN02428.
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. IPR027527. Lipoyl_synth_mt. 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_POPTR

Accession

Primary (citable) accession number: B9H5L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	March 24, 2009
Last modified:	May 29, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program