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Q9LYT7 (LEUD2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 91. 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:
3-isopropylmalate dehydratase small subunit 2

EC=4.2.1.33
Alternative name(s):
AtLEUD2
Isopropylmalate isomerase small subunit 1
Gene names
Name:IPMI1
Ordered Locus Names:At3g58990
ORF Names:F17J16.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. Functions redundantly with LEUD1 in aliphatic glucosinolate biosynthesis. Ref.4

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.

Subunit structure

Heterodimer of LEUC/IIL1 and LEUD (IPMI1, IPMI2 or At2g43090). Ref.4

Subcellular location

Plastidchloroplast stroma Ref.4.

Sequence similarities

Belongs to the LeuD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Chloroplast Potential
Chain57 – 2531973-isopropylmalate dehydratase small subunit 2
PRO_0000425811

Sequences

Sequence LengthMass (Da)Tools
Q9LYT7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A99AB88C4656B0DA

FASTA25327,208
        10         20         30         40         50         60 
MATSQQFLNP TLFKSLASSN KNSCTLCPSP FLQLKSASTI FNYKPLTSSS ATIITRVAAS 

        70         80         90        100        110        120 
SSDSGESITR ETFHGLCFVL KDNIDTDQII PAEYGTLIPS IPEDREKLGS FALNGLPKFY 

       130        140        150        160        170        180 
NERFVVPGEM KSKYSVIIGG DNFGCGSSRE HAPVCLGAAG AKAVVAESYA RIFFRNCVAT 

       190        200        210        220        230        240 
GEIFPLESEV RICDECKTGD VVTIEHKEDG SSLLINHTTR KEYKLKPLGD AGPVIDAGGI 

       250 
FAYARKAGMI PSA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis."
He Y., Chen B., Pang Q., Strul J.M., Chen S.
Plant Cell Physiol. 51:1480-1487(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL163527 Genomic DNA. Translation: CAB86927.1.
CP002686 Genomic DNA. Translation: AEE79857.1.
AY065366 mRNA. Translation: AAL38807.1.
BT006060 mRNA. Translation: AAP04045.1.
PIRT47781.
RefSeqNP_191458.1. NM_115761.3.
UniGeneAt.26842.

3D structure databases

ProteinModelPortalQ9LYT7.
SMRQ9LYT7. Positions 70-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G58990.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G58990.1; AT3G58990.1; AT3G58990.
GeneID825068.
KEGGath:AT3G58990.

Organism-specific databases

TAIRAT3G58990.

Phylogenomic databases

eggNOGCOG0066.
HOGENOMHOG000222940.
InParanoidQ9LYT7.
KOK01704.
OMAYCMEDAR.
PhylomeDBQ9LYT7.

Enzyme and pathway databases

BioCycARA:AT3G58990-MONOMER.
UniPathwayUPA00048; UER00071.

Gene expression databases

GenevestigatorQ9LYT7.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
InterProIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. SSF52016. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEUD2_ARATH
AccessionPrimary (citable) accession number: Q9LYT7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 91 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