LEUD1_ARATH
ID LEUD1_ARATH Reviewed; 256 AA.
AC Q9ZW84;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=3-isopropylmalate dehydratase small subunit 2 {ECO:0000305};
DE EC=4.2.1.33 {ECO:0000305|PubMed:19597944};
DE AltName: Full=2-(omega-methylthio)alkylmalate dehydratase small subunit 2 {ECO:0000305};
DE EC=4.2.1.170 {ECO:0000269|PubMed:19597944};
DE AltName: Full=AtLEUD1 {ECO:0000303|PubMed:20663849};
DE AltName: Full=Isopropylmalate isomerase 2 {ECO:0000305};
DE AltName: Full=Isopropylmalate isomerase small subunit 2 {ECO:0000303|PubMed:19597944};
DE Short=IPMI SSU2 {ECO:0000303|PubMed:19597944};
DE AltName: Full=Methylthioalkylmalate isomerase small subunit {ECO:0000305};
DE Short=MAM-IS {ECO:0000305};
DE Flags: Precursor;
GN Name=SSU2 {ECO:0000303|PubMed:19597944};
GN Synonyms=IPMI2 {ECO:0000305}, LEUD1 {ECO:0000303|PubMed:20663849};
GN OrderedLocusNames=At2g43100 {ECO:0000312|Araport:AT2G43100};
GN ORFNames=MFL8.14;
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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 LEUD2 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:19597944, ECO:0000269|PubMed:20663849}. Plastid
CC {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 young seedlings, expressed in cotyledon epidermal
CC cells and vasculare bundles (PubMed:32612621). In hypocotyls, expressed
CC in parenchyma cells surrounding the vasculature and further peripheral
CC cells (PubMed:32612621). In seedling roots, expressed in cells along
CC the vasculature (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). Expressed in the vasculature of
CC sepals and petals (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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004450; AAC64299.1; -; Genomic_DNA.
DR EMBL; AC006224; AAM15160.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10209.1; -; Genomic_DNA.
DR EMBL; AY060594; AAL31219.1; -; mRNA.
DR EMBL; AY063828; AAL36184.1; -; mRNA.
DR EMBL; AY117208; AAM51283.1; -; mRNA.
DR PIR; A84862; A84862.
DR RefSeq; NP_181838.1; NM_129871.3.
DR AlphaFoldDB; Q9ZW84; -.
DR SMR; Q9ZW84; -.
DR STRING; 3702.AT2G43100.1; -.
DR iPTMnet; Q9ZW84; -.
DR PaxDb; Q9ZW84; -.
DR PRIDE; Q9ZW84; -.
DR ProteomicsDB; 250755; -.
DR EnsemblPlants; AT2G43100.1; AT2G43100.1; AT2G43100.
DR GeneID; 818912; -.
DR Gramene; AT2G43100.1; AT2G43100.1; AT2G43100.
DR KEGG; ath:AT2G43100; -.
DR Araport; AT2G43100; -.
DR TAIR; locus:2040996; AT2G43100.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_081378_1_0_1; -.
DR InParanoid; Q9ZW84; -.
DR OMA; FAYARMM; -.
DR OrthoDB; 1358801at2759; -.
DR PhylomeDB; Q9ZW84; -.
DR BioCyc; ARA:AT2G43100-MON; -.
DR BioCyc; MetaCyc:AT2G43100-MON; -.
DR BRENDA; 4.2.1.33; 399.
DR UniPathway; UPA00048; UER00071.
DR PRO; PR:Q9ZW84; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZW84; baseline and differential.
DR Genevisible; Q9ZW84; AT.
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 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 Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; Leucine biosynthesis; Lyase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..256
FT /note="3-isopropylmalate dehydratase small subunit 2"
FT /id="PRO_0000425810"
SQ SEQUENCE 256 AA; 27043 MW; 56845DC3F4F90A65 CRC64;
MAYSLPTFPQ ALPCSSTKTS SSLATFRSPF LRFNGSTSLI PSSISITSRG TSSPTIIPRA
AASESDSNEA LANTTFHGLC YVLKDNIDTD QIIPAGAACT FPSNQQERDE IAAHALSGLP
DFHKTRFIEP GENRSKYSII IGGENFGCGS SREHAPVCLG AAGAKAIVAE SYARIFFRNS
VATGEVFPLE SEVRVCEECK TGDTVTIELS DSGGLLTNHT TGKNYKLKSI GDAGPVIDAG
GIFAYARMMG MIPSLA
