(data stored in ACNUC7421 zone)

SWISSPROT: LEU3_ECO57

ID   LEU3_ECO57              Reviewed;         363 AA.
AC   Q8X9Z9;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-JUL-2017, entry version 109.
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=Z0082, ECs0077;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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=AAG54377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB33500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54377.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33500.1; ALT_INIT; Genomic_DNA.
DR   PIR; E85489; E85489.
DR   PIR; E90638; E90638.
DR   RefSeq; NP_308104.2; NC_002695.1.
DR   RefSeq; WP_000042351.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q8X9Z9; -.
DR   SMR; Q8X9Z9; -.
DR   STRING; 155864.Z0082; -.
DR   EnsemblBacteria; AAG54377; AAG54377; Z0082.
DR   EnsemblBacteria; BAB33500; BAB33500; BAB33500.
DR   GeneID; 913510; -.
DR   KEGG; ece:Z0082; -.
DR   KEGG; ecs:ECs0077; -.
DR   PATRIC; fig|386585.9.peg.177; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X9Z9.
DR   SWISS-2DPAGE; Q8X9Z9.
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium;
KW   Manganese; Metal-binding; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    363       3-isopropylmalate dehydrogenase.
FT                                /FTId=PRO_0000083692.
FT   NP_BIND      78     91       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   NP_BIND     285    297       NAD. {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       227    227       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   METAL       255    255       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   BINDING      99     99       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     109    109       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   BINDING     227    227       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01033}.
FT   SITE        145    145       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
FT   SITE        195    195       Important for catalysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   363 AA;  39515 MW;  B5C3E87A8BB0E5D9 CRC64;
     MSKNYHIAVL PGDGIGPEVM TQALKVLDAV RNRFAMRITT SHYDVGGAAI DNHGQPLPPA
     TVEGCEQADA VLFGSVGGPK WEHLPPDQQP ERGALLPLRK HFKLFSNLRP AKLYQGLEAF
     CPLRADIAAN GFDILCVREL TGGIYFGQPK GREGSGQYEK AFDTEVYHRF EIERIARIAF
     ESARKRRHKV TSIDKANVLQ SSILWREIVN EIATEYPDIE LAHMYIDNAT MQLIKDPSQF
     DVLLCSNLFG DILSDECAMI TGSMGMLPSA SLNEQGFGLY EPAGGSAPDI AGKNIANPIA
     QILSLALLLR YSLDADDAAS AIERAINRAL EEGIRTGDLA RGAAAVSTDE MGDIIARYVA
     EGV
//

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