ID   LEU3_CLAMS              Reviewed;         355 AA.
AC   B0RIP4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 9.
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=CMS1424;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / JCM
OS   9667).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18192393; DOI=10.1128/JB.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis
RT   subsp. sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(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; AM849034; CAQ01535.1; -; Genomic_DNA.
DR   RefSeq; YP_001710151.1; -.
DR   GeneID; 6157256; -.
DR   GenomeReviews; AM849034_GR; CMS1424.
DR   KEGG; cms:CMS_1424; -.
DR   OMA; B0RIP4; ATRGNER.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0051287; F:NAD or NADH binding; IEA:InterPro.
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; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
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_1000084277.
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;  37195 MW;  7D22C084DF79E199 CRC64;
     MPRTISLAVV PGDGIGPEVV HEALRVLREA VPADVSLDTT QYPFGAGHFL ETGQILTDSD
     LAALAQHDAI LLGAVGGDPR DARLAGGIIE RGLLLKLRFA FDHYINLRPT ALLPGVASPL
     AAPGQVDFVV VREGTEGPYA GNGGVLRRGT EHEIATEVSV NTAHGVERTV RFAFELAEKR
     DRKRVTLVHK TNVLTFAGSL WQRTVDRVAA EHPDVTVDYL HVDATMIFLV TDPSRFDVIV
     SDNLFGDIIT DLAAAISGGI GLAASGNVNP TGAFPSMFEP VHGSAPDIAG QQKADPTAAI
     LSVALLLDHL GLSEAAARVS AAVSDDLAAR ATGDAAPRST AEVGDAILRA LSTNH
//