ID D7KX44_ARALL Unreviewed; 405 AA.
AC D7KX44;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
DE EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
GN ORFNames=ARALYDRAFT_477193 {ECO:0000313|EMBL:EFH65545.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC {ECO:0000256|RuleBase:RU004445}.
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:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC {ECO:0000256|RuleBase:RU004445}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004445}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; GL348714; EFH65545.1; -; Genomic_DNA.
DR RefSeq; XP_002889286.1; XM_002889240.1.
DR AlphaFoldDB; D7KX44; -.
DR STRING; 81972.D7KX44; -.
DR EnsemblPlants; fgenesh2_kg.2__2323__AT1G80560.1; fgenesh2_kg.2__2323__AT1G80560.1; fgenesh2_kg.2__2323__AT1G80560.1.
DR Gramene; fgenesh2_kg.2__2323__AT1G80560.1; fgenesh2_kg.2__2323__AT1G80560.1; fgenesh2_kg.2__2323__AT1G80560.1.
DR eggNOG; KOG0786; Eukaryota.
DR HOGENOM; CLU_031953_0_3_1; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0070403; F:NAD+ binding; IEA:EnsemblPlants.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0009553; P:embryo sac development; IEA:EnsemblPlants.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009555; P:pollen development; IEA:EnsemblPlants.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU004445};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW ECO:0000256|RuleBase:RU004445}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004445};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004445};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT DOMAIN 44..393
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 405 AA; 43325 MW; 8F733788B43DE871 CRC64;
MAAALQTNIP PVKVPATFRA VKKQSFAPFR VRCAVASPGN KRYNITLLPG DGIGPEVVSI
AKNVLQQAGS LEGVEFSFRE MPIGGAALDL VGVPLPEETI AAAKESDALL LGAIGGYKWD
NNEKHLRPET GLLQIRAALK VFANLRPATV LPQLVDASTL KRQVAEGVDL MVVRELTGGI
YFGEPRGIKT NENGEEVGFN TEVYAAHEID RIARVAFETA RKRRGKLCSV DKANVLEASI
LWRKRVTALA SEYPDVELSH MYVDNAAMQL VRDPKQFDTI VTNNIFGDIL SDEASMITGS
IGMLPSASLS DSGPGLFEPI HGSAPDIAGQ DKANPLATIL SAAMLLKYGL GEEKAAKRIE
DAVLVALNNG FRTGDIYSAG TKLVGCKEMG EEVLKSVDSQ VPASV
//
