ID LEU33_ARATH Reviewed; 409 AA. AC Q9FMT1; Q8VXU4; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=3-isopropylmalate dehydrogenase 3, chloroplastic; DE Short=3-IPM-DH 3; DE Short=IMDH 3; DE EC=1.1.1.85; DE AltName: Full=Beta-IPM dehydrogenase 3; DE Flags: Precursor; GN Name=IMDH3; OrderedLocusNames=At5g14200; ORFNames=MUA22.20; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98162728; PubMed=9501997; DOI=10.1093/dnares/4.6.401; RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. RT Sequence features of the regions of 1,191,918 bp covered by seventeen RT physically assigned P1 clones."; RL DNA Res. 4:401-414(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). 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 CC oxopentanoate. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By CC similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). 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=Q9FMT1-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB007650; BAB08299.1; -; Genomic_DNA. DR EMBL; AY074587; AAL67125.1; -; mRNA. DR IPI; IPI00548301; -. DR RefSeq; NP_196924.1; -. DR UniGene; At.6515; -. DR HSSP; Q56268; 1A05. DR PRIDE; Q9FMT1; -. DR GeneID; 831270; -. DR GenomeReviews; BA000015_GR; AT5G14200. DR NMPDR; fig|3702.1.peg.23549; -. DR TAIR; At5g14200; -. DR OMA; Q9FMT1; ASECHAV. DR BRENDA; 1.1.1.85; 302. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IGI:TAIR. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0009098; P:leucine biosynthetic process; IGI:TAIR. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009651; P:response to salt stress; IEP:TAIR. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR004429; Isopropylmalate_DH. DR Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1. DR PANTHER; PTHR11835; IDH_IMDH_dimeric; 1. DR PANTHER; PTHR11835:SF13; IPMDH; 1. DR Pfam; PF00180; Iso_dh; 1. DR TIGRFAMs; TIGR00169; leuB; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Chloroplast; KW Complete proteome; Leucine biosynthesis; Magnesium; Manganese; KW Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide. FT TRANSIT 1 37 Chloroplast (Potential). FT CHAIN 38 409 3-isopropylmalate dehydrogenase 3, FT chloroplastic. FT /FTId=PRO_0000014455. FT NP_BIND 120 133 NAD (By similarity). FT NP_BIND 326 338 NAD (By similarity). FT METAL 268 268 Magnesium or manganese (By similarity). FT METAL 292 292 Magnesium or manganese (By similarity). FT METAL 296 296 Magnesium or manganese (By similarity). FT BINDING 140 140 Substrate (By similarity). FT BINDING 150 150 Substrate (By similarity). FT BINDING 178 178 Substrate (By similarity). FT BINDING 268 268 Substrate (By similarity). FT SITE 185 185 Important for catalysis (By similarity). FT SITE 236 236 Important for catalysis (By similarity). FT CONFLICT 251 251 T -> A (in Ref. 2; AAL67125). SQ SEQUENCE 409 AA; 44162 MW; 471293D4C3FB55DD CRC64; MAAFLQTNIS LNAIKIVPGK YSSLTDHQFR APYRIRCAAA SPGKKRYNIA LLPGDGIGPE VISVAKNVLQ KAGSLEGLEF DFKEMPVGGA ALDLVGVPLP EETFTAAKLS DAILLGAIGG YKWDKNEKHL RPEMALFYLR RDLKVFANLR PATVLPQLVD ASTLKKEVAE GVDMMIVREL TGGIYFGEPR GITINENGEE VGVSTEIYAA HEIDRIARVA FETARKRRGK LCSVDKANVL DASILWRKRV TALASEYPDV ELSHMYVDNA AMQLIRDPKQ FDTIVTNNIF GDILSDEASM ITGSIGMLPS ASLGESGPGL FEPIHGSAPD IAGQDKANPL ATILSAAMLL KYGLGEEKAA KRIEDAVVDA LNKGFRTGDI YSPGNKLVGC KEMGEEVLKS VESKVPATV //