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Q9ZWT1 (LIAS_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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, 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
Ordered Locus Names:At2g20860
ORF Names:F5H14.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length374 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_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 Ref.1.

Tissue specificity

Expressed in leaves and flowers, but not in roots. Ref.1

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1919Mitochondrion Potential
Chain20 – 374355Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128
PRO_0000398844

Sites

Metal binding1031Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1081Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1341Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZWT1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 9527359AA5E9AF6A

FASTA37441,344
        10         20         30         40         50         60 
MHSRSALLYR FLRPASRCFS SSSAVTPVTV TQSPKSLEAL RARLANESPS LTDFIHGDTY 

        70         80         90        100        110        120 
SVEVGTKKKP LPKPKWMKES IPGGERYVQI KKKLRDLKLH TVCEEAKCPN LGECWSGGET 

       130        140        150        160        170        180 
GTATATIMIL GDTCTRGCRF CNVKTSRTPP PPDPNEPNNV AEAIASWGVD YVVITSVDRD 

       190        200        210        220        230        240 
DLPDQGSGHF AETVQRLKFL KPEMLIEALV PDFRGDGGCV EKVSKSGLDV LAHNIETVEE 

       250        260        270        280        290        300 
LQSFVRDHRA NFKQSLDVLR MAKEYAPAGT LTKTSVMLGC GETPDQVVKT MEKVRAAGVD 

       310        320        330        340        350        360 
VMTFGQYMRP SKRHMPVAEY VTPDAFERYR LLGMEMGFRY VASGPMVRSS YKAGEYYIKS 

       370 
MIEADRVASP STSP 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization of the cDNA for lipoic acid synthase."
Yasuno R., Wada H.
Plant Physiol. 118:935-943(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007987 mRNA. Translation: BAA34701.1.
AC006234 Genomic DNA. Translation: AAD20909.1.
CP002685 Genomic DNA. Translation: AEC07088.1.
AY035143 mRNA. Translation: AAK59647.1.
AF424583 mRNA. Translation: AAL11577.1.
AY059077 mRNA. Translation: AAL15183.1.
PIRT44259.
RefSeqNP_179682.1. NM_127655.3.
UniGeneAt.21247.

3D structure databases

ProteinModelPortalQ9ZWT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G20860.1-P.

Proteomic databases

PaxDbQ9ZWT1.
PRIDEQ9ZWT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G20860.1; AT2G20860.1; AT2G20860.
GeneID816619.
KEGGath:AT2G20860.

Organism-specific databases

TAIRAT2G20860.

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235998.
InParanoidQ9ZWT1.
KOK03644.
OMAVQKYWTP.
PhylomeDBQ9ZWT1.
ProtClustDBPLN02428.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Gene expression databases

GenevestigatorQ9ZWT1.

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_ARATH
AccessionPrimary (citable) accession number: Q9ZWT1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 90 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names