LEUD3_ARATH
ID LEUD3_ARATH Reviewed; 251 AA.
AC Q9ZW85;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=3-isopropylmalate dehydratase small subunit 1 {ECO:0000305};
DE EC=4.2.1.33 {ECO:0000269|PubMed:19597944};
DE AltName: Full=AtLEUD3 {ECO:0000303|PubMed:20663849};
DE AltName: Full=Isopropylmalate isomerase small subunit 1 {ECO:0000303|PubMed:19597944};
DE Short=IPMI SSU1 {ECO:0000303|PubMed:19597944};
DE Flags: Precursor;
GN Name=SSU1 {ECO:0000303|PubMed:19597944};
GN Synonyms=LEUD3 {ECO:0000303|PubMed:20663849};
GN OrderedLocusNames=At2g43090 {ECO:0000312|Araport:AT2G43090};
GN ORFNames=MFL8.15;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [7]
RP FUNCTION, AND 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 [8]
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
CC (PubMed:19597944). Plays an essential role in leucine biosynthesis
CC (PubMed:19597944, PubMed:20663849, PubMed:24608865, PubMed:32612621).
CC Functions in both the biosynthesis of leucine, and in the methionine
CC chain elongation pathway of aliphatic glucosinolate formation
CC (PubMed:24608865). Plays an essential role in female gametophyte
CC development (PubMed:19597944, PubMed:20663849, PubMed:24608865).
CC {ECO:0000269|PubMed:19597944, ECO:0000269|PubMed:20663849,
CC ECO:0000269|PubMed:24608865, ECO:0000269|PubMed:32612621,
CC ECO:0000305|PubMed:19597944, 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: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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZW85-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, root tips, at the
CC basis of the hypocotyls, and in emerging leaves (PubMed:24608865). In
CC young seedlings, expressed in cotyledon epidermal cells
CC (PubMed:32612621). In hypocotyls, expressed in peripheral cells
CC (PubMed:32612621). In seedling roots, expressed in the epidermis,
CC including root hairs, and throughout the cortex (PubMed:32612621). In
CC rosette leaves, expressed in the upper and lower epidermis
CC (PubMed:32612621). In roots of adult plants, expressed in the root tips
CC and cortex of the mature root enclosing the stele (PubMed:32612621). In
CC flowering stalks, expressed in the epidermis (PubMed:32612621).
CC Expressed in the carpel epidermis (PubMed:32612621).
CC {ECO:0000269|PubMed:24608865, ECO:0000269|PubMed:32612621}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:19597944, ECO:0000269|PubMed:20663849}.
CC -!- MISCELLANEOUS: Plants silencing SSU1 exhibit stunted growth, narrow
CC pale leaf blades with green vasculature, abnormal leaf adaxial-abaxial
CC patterning, and abnormal flower morphology.
CC {ECO:0000269|PubMed:24608865}.
CC -!- SIMILARITY: Belongs to the LeuD family. {ECO:0000305}.
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DR EMBL; AC004450; AAC64298.1; -; Genomic_DNA.
DR EMBL; AC006224; AAM15163.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10207.1; -; Genomic_DNA.
DR EMBL; AY035158; AAK59662.1; -; mRNA.
DR EMBL; AY063029; AAL34203.1; -; mRNA.
DR EMBL; AY087084; AAM64645.1; -; mRNA.
DR PIR; H84861; H84861.
DR RefSeq; NP_181837.1; NM_129870.3. [Q9ZW85-1]
DR AlphaFoldDB; Q9ZW85; -.
DR SMR; Q9ZW85; -.
DR BioGRID; 4248; 6.
DR STRING; 3702.AT2G43090.1; -.
DR iPTMnet; Q9ZW85; -.
DR MetOSite; Q9ZW85; -.
DR PaxDb; Q9ZW85; -.
DR PRIDE; Q9ZW85; -.
DR ProteomicsDB; 250743; -. [Q9ZW85-1]
DR EnsemblPlants; AT2G43090.1; AT2G43090.1; AT2G43090. [Q9ZW85-1]
DR GeneID; 818911; -.
DR Gramene; AT2G43090.1; AT2G43090.1; AT2G43090. [Q9ZW85-1]
DR KEGG; ath:AT2G43090; -.
DR Araport; AT2G43090; -.
DR TAIR; locus:2041081; AT2G43090.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_081378_1_0_1; -.
DR InParanoid; Q9ZW85; -.
DR OMA; AKHAFEG; -.
DR PhylomeDB; Q9ZW85; -.
DR BioCyc; ARA:AT2G43090-MON; -.
DR BioCyc; MetaCyc:AT2G43090-MON; -.
DR BRENDA; 4.2.1.170; 399.
DR BRENDA; 4.2.1.33; 399.
DR UniPathway; UPA00048; UER00071.
DR PRO; PR:Q9ZW85; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW85; baseline and differential.
DR Genevisible; Q9ZW85; 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:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0009098; P:leucine biosynthetic process; IMP:UniProtKB.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR Pfam; PF00694; Aconitase_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Leucine biosynthesis;
KW Lyase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..251
FT /note="3-isopropylmalate dehydratase small subunit 1"
FT /id="PRO_0000425812"
SQ SEQUENCE 251 AA; 26790 MW; 62EBB1B6059ED272 CRC64;
MAASLQSANP TLSRTLASPN KPSSFATFRS PFLRFNSTSV ASNFKPLVSR EASSSFVTRS
AAEPQERKTF HGLCYVVGDN IDTDQIIPAE FLTLVPSNPE EYEKLGSYAL VGLPASYKER
FVQPGEMKTK YSIIIGGENF GCGSSREHAP VCLGAAGAKA VVAQSYARIF FRNSVATGEV
YPLDSEVRVC DECTTGDVAT VELREGDSIL INHTTGKEYK LKPIGDAGPV IDAGGIFAYA
RKAGMIPSAA A
