ID LEU3_AGRT5 Reviewed; 370 AA. AC P24404; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 04-NOV-2008, entry version 70. DE RecName: Full=3-isopropylmalate dehydrogenase; DE EC=1.1.1.85; DE AltName: Full=Beta-IPM dehydrogenase; DE Short=IMDH; DE AltName: Full=3-IPM-DH; GN Name=leuB; OrderedLocusNames=Atu2791; ORFNames=AGR_C_5067; OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium. OX NCBI_TaxID=176299; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Strizhov N.I., Kryukov V.M., Bur'Yanov Y.I., Beav A.A.; RT "Beta-isopropyl malate dehydrogenase gene of Agrobacterium tumefaciens RT C58: coding and primary structure."; RL Dokl. Akad. Nauk SSSR 288:481-486(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. LeuB type 1 subfamily. 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; M38670; AAA22089.1; -; Genomic_DNA. DR EMBL; AE007869; AAK88504.1; -; Genomic_DNA. DR PIR; AF2919; AF2919. DR PIR; G97693; G97693. DR RefSeq; NP_355719.1; -. DR HSSP; Q56268; 1A05. DR GeneID; 1134829; -. DR GenomeReviews; AE007869_GR; Atu2791. DR KEGG; atc:AGR_C_5067; -. DR KEGG; atu:Atu2791; -. DR HOGENOM; P24404; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:HAMAP. 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:0009098; P:leucine biosynthetic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01033; -; 1. DR InterPro; IPR004429; 3-isopropylmalate_DHase. DR InterPro; IPR001804; IsoCit_IM_DHase. 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 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; KW Manganese; Metal-binding; NAD; Oxidoreductase. FT CHAIN 1 370 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000083627. FT NP_BIND 77 90 NAD (By similarity). FT NP_BIND 290 302 NAD (By similarity). FT METAL 226 226 Magnesium or manganese (By similarity). FT METAL 250 250 Magnesium or manganese (By similarity). FT METAL 254 254 Magnesium or manganese (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 107 107 Substrate (By similarity). FT BINDING 135 135 Substrate (By similarity). FT BINDING 226 226 Substrate (By similarity). FT SITE 142 142 Important for catalysis (By similarity). FT SITE 193 193 Important for catalysis (By similarity). FT CONFLICT 6 6 L -> V (in Ref. 1; AAA22089). SQ SEQUENCE 370 AA; 39659 MW; BB4138D257849E0B CRC64; MTVRSLFLLP GDGIGPEAMT EVRKLIEYMN SAHNAGFTVS EGLVGGSAYD AHGVAISDAD MEKALAADAI LFGAVGGPKW DGVPYEHRPE AGLLRLRKDL ELFANLRPAI CYPALAAASS LKPELVEGLD ILIVRELTGG VYFGEPKQII DLGNGQKRGI DTQIYDTFEI ERIASVAFEL ARSRDNRVCS MEKRNVMKSG VLWNQVVTET HAAKYKDVQL EHMLADAGGM QLVRKPKQFD VIVTDNLFGD MLSDVAAMLT GSLGMLPSAS LGAPDAKTGK RKAMYEPVHG SAPDIAGKSI ANPIAMIASF AMCLRYSFNM VDEATKLEAA IANVLDKGIR TADIMADGCR QVGTSDMGDA VLAEFKALSA //