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Q9ZWT1

- LIAS_ARATH

UniProt

Q9ZWT1 - LIAS_ARATH

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Protein
Lipoyl synthase, mitochondrial
Gene
LIP1, At2g20860, F5H14.17
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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.UniRule annotation

Cofactori

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi103 – 1031Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi108 – 1081Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S) By similarity
Metal bindingi134 – 1341Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: TAIR
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycine catabolic process Source: TAIR
  2. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LIP1
Ordered Locus Names:At2g20860
ORF Names:F5H14.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G20860.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919Mitochondrion Reviewed prediction
Add
BLAST
Chaini20 – 374355Lipoyl synthase, mitochondrialUniRule annotation
PRO_0000398844Add
BLAST

Proteomic databases

PaxDbiQ9ZWT1.
PRIDEiQ9ZWT1.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9ZWT1.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT2G20860.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9ZWT1.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiQ9ZWT1.
KOiK03644.
OMAiHTICQEA.
PhylomeDBiQ9ZWT1.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZWT1-1 [UniParc]FASTAAdd to Basket

« Hide

MHSRSALLYR FLRPASRCFS SSSAVTPVTV TQSPKSLEAL RARLANESPS    50
LTDFIHGDTY SVEVGTKKKP LPKPKWMKES IPGGERYVQI KKKLRDLKLH 100
TVCEEAKCPN LGECWSGGET GTATATIMIL GDTCTRGCRF CNVKTSRTPP 150
PPDPNEPNNV AEAIASWGVD YVVITSVDRD DLPDQGSGHF AETVQRLKFL 200
KPEMLIEALV PDFRGDGGCV EKVSKSGLDV LAHNIETVEE LQSFVRDHRA 250
NFKQSLDVLR MAKEYAPAGT LTKTSVMLGC GETPDQVVKT MEKVRAAGVD 300
VMTFGQYMRP SKRHMPVAEY VTPDAFERYR LLGMEMGFRY VASGPMVRSS 350
YKAGEYYIKS MIEADRVASP STSP 374
Length:374
Mass (Da):41,344
Last modified:May 1, 1999 - v1
Checksum:i9527359AA5E9AF6A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiT44259.
RefSeqiNP_179682.1. NM_127655.3.
UniGeneiAt.21247.

Genome annotation databases

EnsemblPlantsiAT2G20860.1; AT2G20860.1; AT2G20860.
GeneIDi816619.
KEGGiath:AT2G20860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi T44259.
RefSeqi NP_179682.1. NM_127655.3.
UniGenei At.21247.

3D structure databases

ProteinModelPortali Q9ZWT1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 3702.AT2G20860.1-P.

Proteomic databases

PaxDbi Q9ZWT1.
PRIDEi Q9ZWT1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT2G20860.1 ; AT2G20860.1 ; AT2G20860 .
GeneIDi 816619.
KEGGi ath:AT2G20860.

Organism-specific databases

TAIRi AT2G20860.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
InParanoidi Q9ZWT1.
KOi K03644.
OMAi HTICQEA.
PhylomeDBi Q9ZWT1.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

Gene expression databases

Genevestigatori Q9ZWT1.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiLIAS_ARATH
AccessioniPrimary (citable) accession number: Q9ZWT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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