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B9H5L9 (LIAS_POPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [Reference proteome]
Taxonomic identifier3694 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 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 componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 385Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398854

Sites

Metal binding1131Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1181Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1241Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1441Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1481Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1511Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B9H5L9 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 00A96913F7A8D1A1

FASTA38542,613
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqXP_002306361.1. XM_002306325.2.

3D structure databases

ProteinModelPortalB9H5L9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3694.eugene3.00050253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsPOPTR_0005s08840.1; POPTR_0005s08840.1; POPTR_0005s08840.
GeneID7486347.
KEGGpop:POPTR_0005s08840g.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
KOK03644.
OMAHTICQEA.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIAS_POPTR
AccessionPrimary (citable) accession number: B9H5L9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways