LEU32_ARATH
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 03-AUG-2022, entry version 154.
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 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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 3-
CC isopropylmalate as substrate (at pH 7.5 and 25 degrees Celsius)
CC (PubMed:27137927). kcat is 1 min(-1) with 3-(2'-
CC methylthio)ethylmalate as substrate (at pH 7.5) (PubMed:21697089).
CC {ECO:0000269|PubMed:20840499, ECO:0000269|PubMed:21697089,
CC 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; 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 PDBsum; 3R8W; -.
DR PDBsum; 5J32; -.
DR PDBsum; 5J33; -.
DR PDBsum; 5J34; -.
DR AlphaFoldDB; P93832; -.
DR SMR; P93832; -.
DR BioGRID; 29613; 22.
DR IntAct; P93832; 1.
DR STRING; 3702.AT1G80560.1; -.
DR iPTMnet; P93832; -.
DR PaxDb; P93832; -.
DR PRIDE; P93832; -.
DR ProteomicsDB; 237162; -.
DR EnsemblPlants; AT1G80560.1; AT1G80560.1; AT1G80560.
DR GeneID; 844395; -.
DR Gramene; AT1G80560.1; AT1G80560.1; AT1G80560.
DR KEGG; ath:AT1G80560; -.
DR Araport; AT1G80560; -.
DR TAIR; locus:2198893; AT1G80560.
DR eggNOG; KOG0786; Eukaryota.
DR HOGENOM; CLU_031953_0_3_1; -.
DR InParanoid; P93832; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; P93832; -.
DR BRENDA; 1.1.1.85; 399.
DR UniPathway; UPA00048; UER00072.
DR PRO; PR:P93832; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93832; baseline and differential.
DR Genevisible; P93832; AT.
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:leucine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
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 PANTHER; PTHR42979; PTHR42979; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00169; leuB; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
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 3-(2'-methylthio)-
FT ethylmalate, but reduced catalytic efficiency with 3-
FT 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 3-
FT 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. 5; 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..348
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
