ID   LEU3_CLAM3              Reviewed;         355 AA.
AC   A5CPZ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   04-NOV-2008, entry version 13.
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=CMM_1104;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O.,
RA   Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S.,
RA   Rueckert C., Schneiker S., Zellermann E.-M., Puehler A.,
RA   Eichenlaub R., Kaiser O., Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island
RT   involved in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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 (By similarity).
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 2 subfamily.
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DR   EMBL; AM711867; CAN01147.1; -; Genomic_DNA.
DR   RefSeq; YP_001221845.1; -.
DR   GeneID; 5175261; -.
DR   GenomeReviews; AM711867_GR; CMM_1104.
DR   KEGG; cmi:CMM_1104; -.
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_01035; -; 1.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 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    355       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_1000063869.
FT   NP_BIND     283    295       NAD (By similarity).
FT   METAL       223    223       Magnesium or manganese (By similarity).
FT   METAL       247    247       Magnesium or manganese (By similarity).
FT   METAL       251    251       Magnesium or manganese (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     108    108       Substrate (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     223    223       Substrate (By similarity).
FT   SITE        139    139       Important for catalysis (By similarity).
FT   SITE        190    190       Important for catalysis (By similarity).
SQ   SEQUENCE   355 AA;  37179 MW;  E2BD12E685D06224 CRC64;
     MPRTISLAVV PGDGIGPEVV HEALRVLREA VPADVSLDTT QYPFGAGHFL ETGEILTDSD
     LAALAQHDAI LLGAVGGDPR DARLAGGIIE RGLLLKLRFA FDHYINLRPT TLLPGVTSPL
     ASPGEVDFVV VREGTEGPYA GNGGVLRRGT EHEIATEVSV NTAHGVERTV RFAFDLASKR
     ERKRVTLVHK TNVLTFAGSL WQRTVDRVAA EHPDVAVDYL HVDATMIFLV TDPSRFDVIV
     SDNLFGDIIT DLAAAISGGI GLAASGNVNP TGAFPSMFEP VHGSAPDIAG QQKADPTAAI
     LSVSLLLDHL GLPEAAARVT AAVSADLAAR AAGDPAPRST AEVGDAVIRA LSTNH
//