ID   LEU3_AZOSE              Reviewed;         350 AA.
AC   Q5P1J6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 34.
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=AZOSEA26930; ORFNames=ebA4760;
OS   Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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.
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DR   EMBL; CR555306; CAI08818.1; -; Genomic_DNA.
DR   RefSeq; YP_159719.1; -.
DR   GeneID; 3182723; -.
DR   GenomeReviews; CR555306_GR; AZOSEA26930.
DR   KEGG; eba:ebA4760; -.
DR   NMPDR; fig|76114.4.peg.2590; -.
DR   HOGENOM; Q5P1J6; -.
DR   OMA; Q5P1J6; EAFDTMR.
DR   BioCyc; ASP76114:EBA4760-MON; -.
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_01033; -; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004429; Isopropylmalate_DH.
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    350       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083630.
FT   NP_BIND      70     83       NAD (By similarity).
FT   NP_BIND     275    287       NAD (By similarity).
FT   METAL       217    217       Magnesium or manganese (By similarity).
FT   METAL       241    241       Magnesium or manganese (By similarity).
FT   METAL       245    245       Magnesium or manganese (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     128    128       Substrate (By similarity).
FT   BINDING     217    217       Substrate (By similarity).
FT   SITE        135    135       Important for catalysis (By similarity).
FT   SITE        185    185       Important for catalysis (By similarity).
SQ   SEQUENCE   350 AA;  37964 MW;  6A1DA475C7D1AF1E CRC64;
     MKICILPGDG IGPEITAEAV RVIEALDLKF EMEEALLGGA AVDATGDPYP EATRKLAREA
     DAVLLGAVGG PKWDTLPREQ RPERGLLGIR KDLGLFANLR PAILYPELAN ASSLKPEVVA
     GLDILIVREL TGDIYFGQPR GLEVRDGERF GFNTMHYSES EIRRIGRVAF EAARKRNRRL
     CSVDKMNVLE TTQLWRDVMI ELAAEYPDVE LSHMLVDNAA MQLVRAPKQF DVMVTGNMFG
     DILSDEASML TGSIGMLPSA SLDANNKGLY EPSHGSAPDI AGQGIANPLA TILSVAMMLR
     YTFNQENGAL RIENAVKKVL AQGLRTGDIF EPGTTKVGTK QMGDAVLAAL
//