LEUD2_ARATH
ID LEUD2_ARATH Reviewed; 253 AA.
AC Q9LYT7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=3-isopropylmalate dehydratase small subunit 3 {ECO:0000305};
DE EC=4.2.1.33 {ECO:0000305|PubMed:19597944};
DE AltName: Full=2-(omega-methylthio)alkylmalate dehydratase small subunit 3 {ECO:0000305};
DE EC=4.2.1.170 {ECO:0000269|PubMed:19597944};
DE AltName: Full=AtLEUD2 {ECO:0000303|PubMed:20663849};
DE AltName: Full=Isopropylmalate isomerase 1 {ECO:0000305};
DE AltName: Full=Isopropylmalate isomerase small subunit 3 {ECO:0000303|PubMed:19597944};
DE Short=IPMI SSU3 {ECO:0000303|PubMed:19597944};
DE AltName: Full=Methylthioalkylmalate isomerase small subunit {ECO:0000305};
DE Short=MAM-IS {ECO:0000305};
DE Flags: Precursor;
GN Name=SSU3 {ECO:0000303|PubMed:19597944};
GN Synonyms=IPMI1 {ECO:0000305}, LEUD2 {ECO:0000303|PubMed:20663849};
GN OrderedLocusNames=At3g58990 {ECO:0000312|Araport:AT3G58990};
GN ORFNames=F17J16_40 {ECO:0000312|EMBL:CAB86927.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19597944; DOI=10.1007/s11103-009-9519-5;
RA Knill T., Reichelt M., Paetz C., Gershenzon J., Binder S.;
RT "Arabidopsis thaliana encodes a bacterial-type heterodimeric
RT isopropylmalate isomerase involved in both Leu biosynthesis and the Met
RT chain elongation pathway of glucosinolate formation.";
RL Plant Mol. Biol. 71:227-239(2009).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20663849; DOI=10.1093/pcp/pcq113;
RA He Y., Chen B., Pang Q., Strul J.M., Chen S.;
RT "Functional specification of Arabidopsis isopropylmalate isomerases in
RT glucosinolate and leucine biosynthesis.";
RL Plant Cell Physiol. 51:1480-1487(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=24608865; DOI=10.1371/journal.pone.0091071;
RA Imhof J., Huber F., Reichelt M., Gershenzon J., Wiegreffe C., Laechler K.,
RA Binder S.;
RT "The small subunit 1 of the Arabidopsis isopropylmalate isomerase is
RT required for normal growth and development and the early stages of
RT glucosinolate formation.";
RL PLoS ONE 9:E91071-E91071(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=32612621; DOI=10.3389/fpls.2020.00808;
RA Laechler K., Clauss K., Imhof J., Crocoll C., Schulz A., Halkier B.A.,
RA Binder S.;
RT "In Arabidopsis thaliana substrate recognition and tissue- as well as
RT plastid type-specific expression define the roles of distinct small
RT subunits of isopropylmalate isomerase.";
RL Front. Plant Sci. 11:808-808(2020).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate (Probable).
CC Functions redundantly with LEUD1 in the methionine chain elongation
CC pathway of aliphatic glucosinolate formation.
CC {ECO:0000269|PubMed:19597944, ECO:0000269|PubMed:20663849,
CC ECO:0000269|PubMed:32612621, ECO:0000305|PubMed:19597944,
CC ECO:0000305|PubMed:20663849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000305|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-(omega-methylsulfanyl)alkylmalate = a 2-(omega-
CC methylsulfanyl)alkylmaleate + H2O; Xref=Rhea:RHEA:50632, Rhea:RHEA-
CC COMP:12824, Rhea:RHEA-COMP:12826, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:133494, ChEBI:CHEBI:133498; EC=4.2.1.170;
CC Evidence={ECO:0000269|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(3-methylsulfanyl)propylmalate = 2-(2-
CC methylsulfanyl)propylmaleate + H2O; Xref=Rhea:RHEA:50652,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58817, ChEBI:CHEBI:133500;
CC EC=4.2.1.170; Evidence={ECO:0000269|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(omega-methylsulfanyl)alkylmalate = a 2-(omega-
CC methylsulfanyl)alkylmaleate + H2O; Xref=Rhea:RHEA:50636, Rhea:RHEA-
CC COMP:12825, Rhea:RHEA-COMP:12826, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:133496, ChEBI:CHEBI:133498; EC=4.2.1.170;
CC Evidence={ECO:0000269|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-methylsulfanyl)ethylmalate = 2-(2-
CC methylsulfanyl)ethylmaleate + H2O; Xref=Rhea:RHEA:50648,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58816, ChEBI:CHEBI:133499;
CC EC=4.2.1.170; Evidence={ECO:0000269|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(2-methylsulfanyl)ethylmalate = 2-(2-
CC methylsulfanyl)ethylmaleate + H2O; Xref=Rhea:RHEA:50656,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:133497, ChEBI:CHEBI:133499;
CC EC=4.2.1.170; Evidence={ECO:0000269|PubMed:19597944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(3-methylsulfanyl)propylmalate = 2-(2-
CC methylsulfanyl)propylmaleate + H2O; Xref=Rhea:RHEA:50660,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:133500, ChEBI:CHEBI:133501;
CC EC=4.2.1.170; Evidence={ECO:0000269|PubMed:19597944};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000305}.
CC -!- SUBUNIT: Heterodimer of the large LEUC/IIL1 subunit and the small LEUD
CC (SSU1, SSU2 or SSU3) subunits. {ECO:0000269|PubMed:20663849}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:20663849}. Plastid {ECO:0000269|PubMed:32612621}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular bundles of roots, cotyledons
CC and rosette leaves (PubMed:24608865). Expressed in stem vascular
CC bundles which branche off into lateral inflorescences
CC (PubMed:24608865). Expressed in connective tissues in anthers
CC (PubMed:24608865). In hypocotyls, expressed in parenchyma cells
CC surrounding the vasculature (PubMed:32612621). In rosette leaves,
CC expressed in phloem cells and cells close to the xylem along the
CC vascular bundles (PubMed:32612621). In roots of adult plants, expressed
CC in cells closely associated with the stele (PubMed:32612621). In
CC flowering stalks, expressed in parenchyma cells associated with the
CC phloem or the xylem (PubMed:32612621). {ECO:0000269|PubMed:24608865,
CC ECO:0000269|PubMed:32612621}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19597944}.
CC -!- SIMILARITY: Belongs to the LeuD family. {ECO:0000305}.
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DR EMBL; AL163527; CAB86927.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79857.1; -; Genomic_DNA.
DR EMBL; AY065366; AAL38807.1; -; mRNA.
DR EMBL; BT006060; AAP04045.1; -; mRNA.
DR PIR; T47781; T47781.
DR RefSeq; NP_191458.1; NM_115761.3.
DR AlphaFoldDB; Q9LYT7; -.
DR SMR; Q9LYT7; -.
DR STRING; 3702.AT3G58990.1; -.
DR PaxDb; Q9LYT7; -.
DR PRIDE; Q9LYT7; -.
DR ProteomicsDB; 238656; -.
DR EnsemblPlants; AT3G58990.1; AT3G58990.1; AT3G58990.
DR GeneID; 825068; -.
DR Gramene; AT3G58990.1; AT3G58990.1; AT3G58990.
DR KEGG; ath:AT3G58990; -.
DR Araport; AT3G58990; -.
DR TAIR; locus:2077685; AT3G58990.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_081378_1_0_1; -.
DR InParanoid; Q9LYT7; -.
DR OMA; PKFYNER; -.
DR OrthoDB; 1358801at2759; -.
DR PhylomeDB; Q9LYT7; -.
DR BioCyc; ARA:AT3G58990-MON; -.
DR BRENDA; 4.2.1.170; 399.
DR BRENDA; 4.2.1.33; 399.
DR UniPathway; UPA00048; UER00071.
DR PRO; PR:Q9LYT7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYT7; baseline and differential.
DR Genevisible; Q9LYT7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.19.10; -; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR Pfam; PF00694; Aconitase_C; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Leucine biosynthesis; Lyase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..253
FT /note="3-isopropylmalate dehydratase small subunit 3"
FT /id="PRO_0000425811"
SQ SEQUENCE 253 AA; 27208 MW; A99AB88C4656B0DA CRC64;
MATSQQFLNP TLFKSLASSN KNSCTLCPSP FLQLKSASTI FNYKPLTSSS ATIITRVAAS
SSDSGESITR ETFHGLCFVL KDNIDTDQII PAEYGTLIPS IPEDREKLGS FALNGLPKFY
NERFVVPGEM KSKYSVIIGG DNFGCGSSRE HAPVCLGAAG AKAVVAESYA RIFFRNCVAT
GEIFPLESEV RICDECKTGD VVTIEHKEDG SSLLINHTTR KEYKLKPLGD AGPVIDAGGI
FAYARKAGMI PSA
