ID LEU3_CHRVO Reviewed; 354 AA. AC Q7NUC2; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 04-NOV-2008, entry version 44. 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=CV_2778; OS Chromobacterium violaceum. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Chromobacterium. OX NCBI_TaxID=536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131; RX MEDLINE=22882880; PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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: Cytoplasm (By similarity). 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; AE016825; AAQ60446.1; -; Genomic_DNA. DR RefSeq; NP_902448.1; -. DR GeneID; 2547144; -. DR GenomeReviews; AE016825_GR; CV_2778. DR KEGG; cvi:CV_2778; -. DR NMPDR; fig|243365.1.peg.2778; -. DR HOGENOM; Q7NUC2; -. DR BioCyc; CVIO243365:CV_2778-MON; -. 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 1 354 3-isopropylmalate dehydrogenase. FT /FTId=PRO_0000083679. FT NP_BIND 73 86 NAD (By similarity). FT NP_BIND 279 291 NAD (By similarity). FT METAL 221 221 Magnesium or manganese (By similarity). FT METAL 245 245 Magnesium or manganese (By similarity). FT METAL 249 249 Magnesium or manganese (By similarity). FT BINDING 93 93 Substrate (By similarity). FT BINDING 103 103 Substrate (By similarity). FT BINDING 131 131 Substrate (By similarity). FT BINDING 221 221 Substrate (By similarity). FT SITE 138 138 Important for catalysis (By similarity). FT SITE 189 189 Important for catalysis (By similarity). SQ SEQUENCE 354 AA; 38544 MW; 3DA41DB62D0E15B6 CRC64; MKIAILPGDG IGPEIIAQAE RVLEVLRRDG LKIETEHAPL GGAAYDQYGV PYPEATQKLA READAVLLGA VGGPAYDKLD RPLRPERGLL AIRKDLNLFA NLRPAILYPE LANASTLKPE VVAGLDIMIV RELTGDIYFG QPRGIAVNEL GEREAYNTMR YSESEVRRIA HVAFGIAMKR NRKLCSVDKA NVLETTEFWK EIMIEVAKEY PQVELSHMYV DNAAMQLVRN PKQFDVMVTG NIFGDILSDE ASMLTGSIGM LPSASLDQNN KGLYEPSHGS APDIAGQNLA NPLATILSAA MMLRYSFGQE AAARRVEDAV KKVLAQGYRT ADIYEAGCEK VSCSGMGDAV VAAM //