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Q8LEE8 (LISC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, 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:At5g08415
ORF Names:F8L15.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.1

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_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

Plastidchloroplast Ref.1.

Tissue specificity

Expressed in roots, leaves and flowers. Ref.1

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Sequence caution

The sequence AAM62684.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAC08341.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   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_componentchloroplast

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 – 3636Chloroplast Potential
Chain37 – 394358Lipoyl synthase, chloroplastic HAMAP-Rule MF_03129
PRO_0000398858

Sites

Metal binding1271Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1321Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1381Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1581Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1621Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1651Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8LEE8 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 3F1B081CF0216255

FASTA39443,622
        10         20         30         40         50         60 
MMHHCSITKP TFSISISTQK LHHHSSKFLN LGFRIRCESG DVSSPLRTKA VSLSSEMEDS 

        70         80         90        100        110        120 
SSLKKSLMEL EGKKSEPYPG GMPKMGPFTG RDPNVKKPAW LRQKAPQGER FQEVKESLSR 

       130        140        150        160        170        180 
LNLNTVCEEA QCPNIGECWN GGGDGVATAT IMVLGDTCTR GCRFCAVKTS RNPPPPDPME 

       190        200        210        220        230        240 
PENTAKAIAS WGVDYIVITS VDRDDIPDGG SGHFAQTVKA MKRHKPDIMI ECLTSDFRGD 

       250        260        270        280        290        300 
LEAVDTLVHS GLDVFAHNVE TVKRLQRLVR DPRAGYEQSM SVLKHAKISK PGMITKTSIM 

       310        320        330        340        350        360 
LGLGETDEEL KEAMADLRAI DVDILTLGQY LQPTPLHLTV KEYVTPEKFD FWKTYGESIG 

       370        380        390 
FRYVASGPLV RSSYRAGELF VKTMVKESYS KSLS 

« Hide

References

« Hide 'large scale' references
[1]"The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana."
Yasuno R., Wada H.
FEBS Lett. 517:110-114(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Arabidopsis ORF clones."
Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB073745 mRNA. Translation: BAB91180.1.
AL392174 Genomic DNA. Translation: CAC08341.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED91298.1.
AY085458 mRNA. Translation: AAM62684.1. Different initiation.
BT025549 mRNA. Translation: ABF58967.1.
RefSeqNP_568196.1. NM_120926.2.
UniGeneAt.32581.

3D structure databases

ProteinModelPortalQ8LEE8.
SMRQ8LEE8. Positions 152-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G08415.1-P.

Proteomic databases

PaxDbQ8LEE8.
PRIDEQ8LEE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G08415.1; AT5G08415.1; AT5G08415.
GeneID830740.
KEGGath:AT5G08415.

Organism-specific databases

TAIRAT5G08415.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
InParanoidQ8LSZ8.
KOK03644.
OMAAHHLPVR.
PhylomeDBQ8LEE8.
ProtClustDBPLN02428.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Gene expression databases

GenevestigatorQ8LEE8.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03129. Lipoyl_synth_plantC.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027526. Lipoyl_synth_chlpt.
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 nameLISC_ARATH
AccessionPrimary (citable) accession number: Q8LEE8
Secondary accession number(s): Q8LSZ8, Q9FT94
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: February 19, 2014
This is version 70 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names