ID LEU3_NOVAD Reviewed; 352 AA.
AC Q2G4X5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE EC=1.1.1.85;
DE AltName: Full=3-IPM-DH;
DE AltName: Full=Beta-IPM dehydrogenase;
DE Short=IMDH;
GN Name=leuB; OrderedLocusNames=Saro_2662;
OS Novosphingobium aromaticivorans (strain DSM 12444).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12444;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 1 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD27098.1; Type=Erroneous initiation;
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DR EMBL; CP000248; ABD27098.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_497932.1; NC_007794.1.
DR HSSP; Q9WZ26; 1VLC.
DR ProteinModelPortal; Q2G4X5; -.
DR SMR; Q2G4X5; 2-352.
DR STRING; 279238.Saro_2662; -.
DR EnsemblBacteria; ABD27098; ABD27098; Saro_2662.
DR GeneID; 3918436; -.
DR KEGG; nar:Saro_2662; -.
DR PATRIC; 22788132; VBINovAro50627_2725.
DR eggNOG; COG0473; -.
DR HOGENOM; HOG000021112; -.
DR KO; K00052; -.
DR OMA; MSYQIAV; -.
DR ProtClustDB; PRK00772; -.
DR BioCyc; NARO279238:GHBU-3354-MONOMER; -.
DR UniPathway; UPA00048; UER00072.
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:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.718.10; -; 1.
DR HAMAP; MF_01033; LeuB_type1; 1; -.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR11835; PTHR11835; 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 1 352 3-isopropylmalate dehydrogenase.
FT /FTId=PRO_0000250123.
FT NP_BIND 281 293 NAD (By similarity).
FT METAL 218 218 Magnesium or manganese (By similarity).
FT METAL 242 242 Magnesium or manganese (By similarity).
FT METAL 246 246 Magnesium or manganese (By similarity).
FT BINDING 91 91 Substrate (By similarity).
FT BINDING 101 101 Substrate (By similarity).
FT BINDING 129 129 Substrate (By similarity).
FT BINDING 218 218 Substrate (By similarity).
FT SITE 136 136 Important for catalysis (By similarity).
FT SITE 186 186 Important for catalysis (By similarity).
SQ SEQUENCE 352 AA; 37476 MW; 6DD4B37720CE6889 CRC64;
MKIAVLPGDG IGPEVTREAV RVIEALGLGD IEMKEAPVGG AAYKAYGHPL PPETLEIARL
SDGILFGAVG DPDCDSLERH LRPEQAILGL RKALTLFANL RPARVFKGME DFSALRPEVA
GAIDLLIVRE LNGDVYFGEK GFRTAANGDR EGYDVMSYSE SEVRRIAHVA FRAAMGRKKR
LCSVDKANVL ETSQLWRDVM LEVAKDYPEV ALEHMYVDNA AMQLVRAPGN FDVVVTGNLF
GDILSDQASM CVGSIGLLAS ASLGERETEY GTFGLYEPIH GSAPDIAGKG LANPMATILS
AAMLLRHSLG LEVAADRIEA AVAKALADGV LGRDLGGTAG TTEIGDAVLA RL
//
