ID   LEU32_ARATH             Reviewed;         405 AA.
AC   P93832; Q540Z4; Q8W4P6;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 168.
DE   RecName: Full=3-isopropylmalate dehydrogenase 2, chloroplastic {ECO:0000303|PubMed:15849421};
DE            Short=3-IPM-DH 2 {ECO:0000303|PubMed:15849421};
DE            Short=AtIMDH2 {ECO:0000303|PubMed:15849421};
DE            Short=AtIMDH3 {ECO:0000303|PubMed:19674406};
DE            Short=IMDH 2 {ECO:0000303|PubMed:15849421};
DE            EC=1.1.1.85 {ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:20840499};
DE   AltName: Full=Beta-IPM dehydrogenase 2 {ECO:0000303|PubMed:15849421};
DE   AltName: Full=Isopropylmalate dehydrogenase 2 {ECO:0000303|PubMed:19493961};
DE            Short=AtIMD2 {ECO:0000303|PubMed:19493961};
DE   Flags: Precursor;
GN   Name=IMDH2 {ECO:0000303|PubMed:15849421};
GN   Synonyms=IMD2 {ECO:0000303|PubMed:19493961}, IMDH {ECO:0000303|Ref.1},
GN   IPMDH2 {ECO:0000303|PubMed:20840499};
GN   OrderedLocusNames=At1g80560 {ECO:0000312|Araport:AT1G80560};
GN   ORFNames=T21F11.11 {ECO:0000312|EMBL:AAF27137.1};
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 [MRNA].
RC   STRAIN=cv. Columbia;
RA   Salchert K.D.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP   SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=15849421; DOI=10.1271/bbb.69.806;
RA   Nozawa A., Takano J., Miwa K., Nakagawa Y., Fujiwara T.;
RT   "Cloning of cDNAs encoding isopropylmalate dehydrogenase from Arabidopsis
RT   thaliana and accumulation patterns of their transcripts.";
RL   Biosci. Biotechnol. Biochem. 69:806-810(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
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   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19493961; DOI=10.1093/pcp/pcp079;
RA   Sawada Y., Kuwahara A., Nagano M., Narisawa T., Sakata A., Saito K.,
RA   Hirai M.Y.;
RT   "Omics-based approaches to methionine side chain elongation in Arabidopsis:
RT   characterization of the genes encoding methylthioalkylmalate isomerase and
RT   methylthioalkylmalate dehydrogenase.";
RL   Plant Cell Physiol. 50:1181-1190(2009).
RN   [8]
RP   GENE FAMILY.
RX   PubMed=19674406; DOI=10.1111/j.1365-313x.2009.03990.x;
RA   He Y., Mawhinney T.P., Preuss M.L., Schroeder A.C., Chen B., Abraham L.,
RA   Jez J.M., Chen S.;
RT   "A redox-active isopropylmalate dehydrogenase functions in the biosynthesis
RT   of glucosinolates and leucine in Arabidopsis.";
RL   Plant J. 60:679-690(2009).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP   ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=20840499; DOI=10.1111/j.1469-8137.2010.03460.x;
RA   He Y., Chen L., Zhou Y., Mawhinney T.P., Chen B., Kang B.-H., Hauser B.A.,
RA   Chen S.;
RT   "Functional characterization of Arabidopsis thaliana isopropylmalate
RT   dehydrogenases reveals their important roles in gametophyte development.";
RL   New Phytol. 189:160-175(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), FUNCTION, MUTAGENESIS OF LEU-133,
RP   TISSUE SPECIFICITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Columbia;
RX   PubMed=21697089; DOI=10.1074/jbc.m111.262519;
RA   He Y., Galant A., Pang Q., Strul J.M., Balogun S.F., Jez J.M., Chen S.;
RT   "Structural and functional evolution of isopropylmalate dehydrogenases in
RT   the leucine and glucosinolate pathways of Arabidopsis thaliana.";
RL   J. Biol. Chem. 286:28794-28801(2011).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; NAD AND
RP   SUBSTRATE, SITE, MUTAGENESIS OF LEU-132; LEU-133; ARG-136; ARG-146;
RP   ARG-174; TYR-181; LYS-232; ASN-234; VAL-235; ASP-264; ASP-288 AND ASP-292,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=27137927; DOI=10.1074/jbc.m116.730358;
RA   Lee S.G., Nwumeh R., Jez J.M.;
RT   "Structure and Mechanism of Isopropylmalate Dehydrogenase from Arabidopsis
RT   thaliana: INSIGHTS ON LEUCINE AND ALIPHATIC GLUCOSINOLATE BIOSYNTHESIS.";
RL   J. Biol. Chem. 291:13421-13430(2016).
CC   -!- FUNCTION: Involved in leucine biosynthesis; catalyzes the oxidative
CC       decarboxylation step in leucine biosynthesis (primary metabolism)
CC       (PubMed:21697089). Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate, 3-IPM) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate
CC       (PubMed:15849421, PubMed:20840499). Required during pollen development
CC       and involved in embryo sac development (PubMed:20840499).
CC       {ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:20840499,
CC       ECO:0000269|PubMed:21697089}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:20840499};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:27137927};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P50455};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000250|UniProtKB:P50455};
CC   -!- ACTIVITY REGULATION: Regulated by a thiol-based redox modification.
CC       {ECO:0000250|UniProtKB:Q9FMT1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.5 uM for 3-isopropylmalate (at pH 7.5 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:27137927};
CC         KM=10.9 uM for 3-isopropylmalate (at pH 7.5)
CC         {ECO:0000269|PubMed:20840499, ECO:0000269|PubMed:21697089};
CC         KM=435 uM for 3-(2'-methylthio)ethylmalate (at pH 7.5)
CC         {ECO:0000269|PubMed:21697089};
CC         Vmax=4.05 umol/min/mg enzyme with 3-isopropylmalate as substrate (at
CC         pH 7.5) {ECO:0000269|PubMed:20840499};
CC         Note=kcat is 373 min(-1) with 3-isopropylmalate as substrate (at pH
CC         7.5) (PubMed:20840499, PubMed:21697089). kcat is 274 min(-1) with
CC         3-isopropylmalate as substrate (at pH 7.5 and 25 degrees Celsius)
CC         (PubMed:27137927). kcat is 1 min(-1) with
CC         3-(2'-methylthio)ethylmalate as substrate (at pH 7.5)
CC         (PubMed:21697089). {ECO:0000269|PubMed:20840499,
CC         ECO:0000269|PubMed:21697089, ECO:0000269|PubMed:27137927};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000269|PubMed:15849421,
CC       ECO:0000269|PubMed:20840499}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21697089}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:Q9FMT1}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, cotyledons,
CC       hypocotyls, flowers, roots, pollen, leaves and stems.
CC       {ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:20840499,
CC       ECO:0000269|PubMed:21697089}.
CC   -!- DISRUPTION PHENOTYPE: No discernible vegetative or reproductive
CC       phenotypes except a slight reduction of both male and female
CC       transmission efficiency, but decreased leucine biosynthetic enzyme
CC       activities and lower free leucine concentrations. The double mutant
CC       ipmdh2 ipmdh3 is lethal in male gametophytes (small aborted pollen
CC       grains abnormal in cellular structure, and arrested in germination) and
CC       had reduced transmission through female gametophytes (slow embryo sacs
CC       development). {ECO:0000269|PubMed:20840499}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; Y10216; CAA71268.1; -; mRNA.
DR   EMBL; AC018849; AAF27137.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36420.1; -; Genomic_DNA.
DR   EMBL; OZ408683; CAO7034096.1; -; Genomic_DNA.
DR   EMBL; AY062441; AAL32519.1; -; mRNA.
DR   EMBL; AY114627; AAM47946.1; -; mRNA.
DR   PIR; F96837; F96837.
DR   RefSeq; NP_178171.1; NM_106704.4.
DR   PDB; 3R8W; X-ray; 2.25 A; A/B/C/D=1-405.
DR   PDB; 5J32; X-ray; 1.93 A; A/B/C/D=39-405.
DR   PDB; 5J33; X-ray; 3.49 A; A/B/C/D/E/F/G/H=1-405.
DR   PDB; 5J34; X-ray; 1.83 A; A/B/C/D=1-405.
DR   AlphaFoldDB; P93832; -.
DR   MDposit; P93832; -.
DR   SMR; P93832; -.
DR   BioGRID; 29613; 22.
DR   FunCoup; P93832; 1302.
DR   IntAct; P93832; 1.
DR   STRING; 3702.P93832; -.
DR   iPTMnet; P93832; -.
DR   PaxDb; 3702-P93832; -.
DR   ProteomicsDB; 237162; -.
DR   GeneID; 844395; -.
DR   KEGG; ath:AT1G80560; -.
DR   Araport; AT1G80560; -.
DR   TAIR; AT1G80560; IMD2.
DR   eggNOG; KOG0786; Eukaryota.
DR   HOGENOM; CLU_031953_0_3_1; -.
DR   InParanoid; P93832; -.
DR   OMA; EYDLGAR; -.
DR   PhylomeDB; P93832; -.
DR   BRENDA; 1.1.1.85; 399.
DR   UniPathway; UPA00048; UER00072.
DR   EvolutionaryTrace; P93832; -.
DR   PRO; PR:P93832; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P93832; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; ISS:TAIR.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0009553; P:embryo sac development; IMP:UniProtKB.
DR   GO; GO:0009098; P:L-leucine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR   FunFam; 3.40.718.10:FF:000004; 3-isopropylmalate dehydrogenase; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   NCBIfam; TIGR00169; leuB; 1.
DR   PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
DR   PDBsum; 3R8W; -.
DR   PDBsum; 5J32; -.
DR   PDBsum; 5J33; -.
DR   PDBsum; 5J34; -.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Chloroplast; Leucine biosynthesis;
KW   Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..405
FT                   /note="3-isopropylmalate dehydrogenase 2, chloroplastic"
FT                   /id="PRO_0000014454"
FT   BINDING         114..129
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J33"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32"
FT   BINDING         234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J33"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32, ECO:0007744|PDB:5J33,
FT                   ECO:0007744|PDB:5J34"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32"
FT   BINDING         265
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J33"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32, ECO:0007744|PDB:5J33,
FT                   ECO:0007744|PDB:5J34"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J32, ECO:0007744|PDB:5J33,
FT                   ECO:0007744|PDB:5J34"
FT   BINDING         318..334
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000269|PubMed:27137927,
FT                   ECO:0007744|PDB:5J33"
FT   SITE            133
FT                   /note="Confers substrate specificity"
FT                   /evidence="ECO:0000269|PubMed:21697089"
FT   SITE            181
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   SITE            228
FT                   /note="Essential for redox regulation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FMT1"
FT   SITE            232
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   SITE            386
FT                   /note="Essential for redox regulation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FMT1"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FMT1"
FT   MUTAGEN         132
FT                   /note="L->A: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         133
FT                   /note="L->A: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         133
FT                   /note="L->F: Enhanced activity toward
FT                   3-(2'-methylthio)-ethylmalate, but reduced catalytic
FT                   efficiency with 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:21697089"
FT   MUTAGEN         136
FT                   /note="R->A: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         136
FT                   /note="R->K: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         146
FT                   /note="R->A: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         146
FT                   /note="R->K: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         174
FT                   /note="R->A: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         174
FT                   /note="R->K: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         181
FT                   /note="Y->A,F,H: Reduced activity toward
FT                   3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         232
FT                   /note="K->M: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         234
FT                   /note="N->A,D: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         235
FT                   /note="V->A: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         264
FT                   /note="D->N: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         288
FT                   /note="D->N: Loss of activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   MUTAGEN         292
FT                   /note="D->N: Reduced activity toward 3-isopropylmalate."
FT                   /evidence="ECO:0000269|PubMed:27137927"
FT   CONFLICT        177
FT                   /note="T -> K (in Ref. 6; AAL32519/AAM47946)"
FT                   /evidence="ECO:0000305"
FT   STRAND          42..51
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           54..70
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           85..90
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           128..138
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           152..157
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          169..175
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:5J33"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          196..205
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           206..221
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          225..231
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           237..249
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           250..252
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          256..262
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           263..272
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          278..282
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           284..298
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           301..303
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          307..309
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          311..313
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          315..317
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   TURN            328..331
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           336..344
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           345..350
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           353..368
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:5J34"
FT   HELIX           386..398
FT                   /evidence="ECO:0007829|PDB:5J34"
SQ   SEQUENCE   405 AA;  43371 MW;  D5E22968F19FC7DC CRC64;
     MAAALQTNIR TVKVPATFRA VSKQSLAPFR VRCAVASPGK KRYTITLLPG DGIGPEVVSI
     AKNVLQQAGS LEGVEFNFRE MPIGGAALDL VGVPLPEETI SAAKESDAVL LGAIGGYKWD
     NNEKHLRPEK GLLQIRAALK VFANLRPATV LPQLVDASTL KREVAEGVDL MVVRELTGGI
     YFGEPRGIKT NENGEEVGFN TEVYAAHEID RIARVAFETA RKRRGKLCSV DKANVLEASI
     LWRKRVTALA SEYPDVELSH MYVDNAAMQL VRDPKQFDTI VTNNIFGDIL SDEASMITGS
     IGMLPSASLS DSGPGLFEPI HGSAPDIAGQ DKANPLATIL SAAMLLKYGL GEEKAAKRIE
     DAVLVALNNG FRTGDIYSAG TKLVGCKEMG EEVLKSVDSQ VPASV
//