ID   LEU3_BACCA              Reviewed;         366 AA.
AC   P05644;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   04-NOV-2008, entry version 62.
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;
OS   Bacillus caldotenax.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87146398; PubMed=3547331; DOI=10.1093/nar/15.2.853;
RA   Sekiguchi T., Suda M., Ishii T., Nosoh Y., Tsuda K.;
RT   "The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from
RT   Bacillus caldotenax.";
RL   Nucleic Acids Res. 15:853-853(1987).
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.
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DR   EMBL; X04762; CAA28455.1; -; Genomic_DNA.
DR   PIR; A26447; A26447.
DR   HSSP; P12010; 2AYQ.
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   Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    366       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083633.
FT   NP_BIND      77     90       NAD (By similarity).
FT   NP_BIND     280    292       NAD (By similarity).
FT   METAL       223    223       Magnesium or manganese (By similarity).
FT   METAL       246    246       Magnesium or manganese (By similarity).
FT   METAL       250    250       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     223    223       Substrate (By similarity).
FT   SITE        142    142       Important for catalysis (By similarity).
FT   SITE        191    191       Important for catalysis (By similarity).
SQ   SEQUENCE   366 AA;  39636 MW;  530C88B3A60C630D CRC64;
     MGNYRIAVLP GDGIGKEVTS GAVEVLKAVG IRFGHEFTFE YGLIGGAAID EAGTPLPEET
     VRLCRESDAV LLGAVGGPKW DDNPPHLRPE KGLLAIRKQL DLYANLRPVV CYDSLVSRSP
     LKPDLVQGVD FVIVRELTGG IYFGQPSAVV ENGEEKAVDT LLYKKEEIER IVRMAFELAR
     GRRKKVTSVD KANVLSSSRL WREVAEEVAN EFPDVTLEHM LVDMRMQLIR APKQFDVIVT
     ENMFGDILSD EASMLSGSLG MLPSASLSAS GPSLYEPVHG SAPDIAGMNK ANPIAAILSA
     AMMLRLSFGL TAEAGGRARV WQALALGSGS RLGQRRPHLS TNEMVEEIKA AVLDYTAIAQ
     IMTVYA
//