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LEU3_PSEU2
ID   LEU3_PSEU2              Reviewed;         360 AA.
AC   Q4ZUZ4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=Psyr_1985;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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 oxopentanoate.
CC       {ECO:0000255|HAMAP-Rule:MF_01033}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85; Evidence={ECO:0000255|HAMAP-
CC         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-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; CP000075; AAY37028.1; -; Genomic_DNA.
DR   RefSeq; WP_011267364.1; NC_007005.1.
DR   RefSeq; YP_235066.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZUZ4; -.
DR   SMR; Q4ZUZ4; -.
DR   STRING; 205918.Psyr_1985; -.
DR   World-2DPAGE; 0008:Q4ZUZ4; -.
DR   EnsemblBacteria; AAY37028; AAY37028; Psyr_1985.
DR   KEGG; psb:Psyr_1985; -.
DR   PATRIC; fig|205918.7.peg.2028; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_3_6; -.
DR   OMA; EYDLGAR; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000000426; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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   PANTHER; PTHR42979; PTHR42979; 1.
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;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW   Oxidoreductase.
FT   CHAIN           1..360
FT                   /note="3-isopropylmalate dehydrogenase"
FT                   /id="PRO_0000083731"
FT   BINDING         76..89
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   BINDING         282..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   SITE            141
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT   SITE            192
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
SQ   SEQUENCE   360 AA;  38877 MW;  F93467358EF42C90 CRC64;
     MSKQILILPG DGIGPEIMTE AVKVLELANE KYQLGFELTH DVIGGAAIDK HGVPLADETL
     ERARAADAVL LGAVGGPKWD TIERDIRPER GLLKIRSQLG LFGNLRPAIL YPQLADASSL
     KPEIVAGLDI MIVRELTGGI YFGAPRGTRV LDNGERQAYD TLPYSESEIR RIAKVGFDMA
     MVRGKKLCSV DKANVLASSQ LWREIVEQVA RDYPEVELSH MYVDNAAMQL VRAPKQFDVI
     VTDNLFGDIL SDQASMLTGS IGMLPSASLD TANKGMYEPC HGSAPDIAGK GIANPLATIL
     SVSMMLRYSF NLTDAADAIE KAVSLVLDQG IRTGDIWSEG KVKVGTQEMG DAVVAALRNL
 
 
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