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Database: UniProt
Entry: Q2G4X5
LinkDB: Q2G4X5
Original site: Q2G4X5 
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   26-NOV-2014, entry version 68.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000255|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000255|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000255|HAMAP-Rule:MF_01033};
GN   OrderedLocusNames=Saro_2662;
OS   Novosphingobium aromaticivorans (strain DSM 12444 / F199).
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 / F199;
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. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
CC       2-oxopentanoate + CO(2) + NADH. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01033};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01033};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01033}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD27098.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000248; ABD27098.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_497932.1; NC_007794.1.
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; FEMESAL; -.
DR   OrthoDB; EOG65N1BN; -.
DR   BioCyc; NARO279238:GHBU-2726-MONOMER; -.
DR   UniPathway; UPA00048; UER00072.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-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:UniProtKB-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; Reference proteome.
FT   CHAIN         1    352       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000250123.
FT   NP_BIND     281    293       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       218    218       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       242    242       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       246    246       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   BINDING      91     91       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     101    101       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     218    218       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   SITE        136    136       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   SITE        186    186       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
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
//
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