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Protein

3-isopropylmalate dehydratase small subunit 2

Gene

IPMI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. Functions redundantly with LEUD1 in aliphatic glucosinolate biosynthesis.1 Publication

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. 3-isopropylmalate dehydratase activity Source: UniProtKB

GO - Biological processi

  1. glucosinolate biosynthetic process Source: UniProtKB
  2. leucine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Enzyme and pathway databases

BioCyciARA:AT3G58990-MONOMER.
BRENDAi4.2.1.33. 399.
UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase small subunit 2 (EC:4.2.1.33)
Alternative name(s):
AtLEUD2
Isopropylmalate isomerase small subunit 1
Gene namesi
Name:IPMI1
Ordered Locus Names:At3g58990
ORF Names:F17J16.40
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G58990.

Subcellular locationi

  1. Plastidchloroplast stroma 1 Publication

GO - Cellular componenti

  1. chloroplast stroma Source: UniProtKB
  2. plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5656ChloroplastSequence AnalysisAdd
BLAST
Chaini57 – 2531973-isopropylmalate dehydratase small subunit 2PRO_0000425811Add
BLAST

Proteomic databases

PRIDEiQ9LYT7.

Expressioni

Gene expression databases

GenevestigatoriQ9LYT7.

Interactioni

Subunit structurei

Heterodimer of LEUC/IIL1 and LEUD (IPMI1, IPMI2 or At2g43090).1 Publication

Protein-protein interaction databases

STRINGi3702.AT3G58990.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9LYT7.
SMRiQ9LYT7. Positions 70-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LeuD family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0066.
HOGENOMiHOG000222940.
InParanoidiQ9LYT7.
KOiK01704.
OMAiEYRIRPY.
PhylomeDBiQ9LYT7.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
InterProiIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9LYT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSQQFLNP TLFKSLASSN KNSCTLCPSP FLQLKSASTI FNYKPLTSSS
60 70 80 90 100
ATIITRVAAS SSDSGESITR ETFHGLCFVL KDNIDTDQII PAEYGTLIPS
110 120 130 140 150
IPEDREKLGS FALNGLPKFY NERFVVPGEM KSKYSVIIGG DNFGCGSSRE
160 170 180 190 200
HAPVCLGAAG AKAVVAESYA RIFFRNCVAT GEIFPLESEV RICDECKTGD
210 220 230 240 250
VVTIEHKEDG SSLLINHTTR KEYKLKPLGD AGPVIDAGGI FAYARKAGMI

PSA
Length:253
Mass (Da):27,208
Last modified:October 1, 2000 - v1
Checksum:iA99AB88C4656B0DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL163527 Genomic DNA. Translation: CAB86927.1.
CP002686 Genomic DNA. Translation: AEE79857.1.
AY065366 mRNA. Translation: AAL38807.1.
BT006060 mRNA. Translation: AAP04045.1.
PIRiT47781.
RefSeqiNP_191458.1. NM_115761.3.
UniGeneiAt.26842.

Genome annotation databases

EnsemblPlantsiAT3G58990.1; AT3G58990.1; AT3G58990.
GeneIDi825068.
KEGGiath:AT3G58990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL163527 Genomic DNA. Translation: CAB86927.1.
CP002686 Genomic DNA. Translation: AEE79857.1.
AY065366 mRNA. Translation: AAL38807.1.
BT006060 mRNA. Translation: AAP04045.1.
PIRiT47781.
RefSeqiNP_191458.1. NM_115761.3.
UniGeneiAt.26842.

3D structure databases

ProteinModelPortaliQ9LYT7.
SMRiQ9LYT7. Positions 70-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G58990.1-P.

Proteomic databases

PRIDEiQ9LYT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G58990.1; AT3G58990.1; AT3G58990.
GeneIDi825068.
KEGGiath:AT3G58990.

Organism-specific databases

TAIRiAT3G58990.

Phylogenomic databases

eggNOGiCOG0066.
HOGENOMiHOG000222940.
InParanoidiQ9LYT7.
KOiK01704.
OMAiEYRIRPY.
PhylomeDBiQ9LYT7.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.
BioCyciARA:AT3G58990-MONOMER.
BRENDAi4.2.1.33. 399.

Miscellaneous databases

PROiQ9LYT7.

Gene expression databases

GenevestigatoriQ9LYT7.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
InterProiIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiLEUD2_ARATH
AccessioniPrimary (citable) accession number: Q9LYT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.