LEU3_PSEAE
ID LEU3_PSEAE Reviewed; 360 AA.
AC Q51375; O87012; Q51343; Q9HZA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=PA3118;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9108278; DOI=10.1007/s004380050404;
RA Hoang T.T., Schweizer H.P.;
RT "Identification and genetic characterization of the Pseudomonas aeruginosa
RT leuB gene encoding 3-isopropylmalate dehydrogenase.";
RL Mol. Gen. Genet. 254:166-170(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Semmler A., Whitchurch C.B., Mattick J.S.;
RT "Pseudomonas aeruginosa twitching motility gene fimV.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
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DR EMBL; U29655; AAC45419.1; -; Genomic_DNA.
DR EMBL; U11055; AAB51625.1; -; Genomic_DNA.
DR EMBL; U93274; AAC23938.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06506.1; -; Genomic_DNA.
DR PIR; D83255; D83255.
DR RefSeq; NP_251808.1; NC_002516.2.
DR RefSeq; WP_003091395.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; Q51375; -.
DR SMR; Q51375; -.
DR STRING; 287.DR97_4815; -.
DR PaxDb; Q51375; -.
DR PRIDE; Q51375; -.
DR DNASU; 882812; -.
DR EnsemblBacteria; AAG06506; AAG06506; PA3118.
DR GeneID; 882812; -.
DR KEGG; pae:PA3118; -.
DR PATRIC; fig|208964.12.peg.3270; -.
DR PseudoCAP; PA3118; -.
DR HOGENOM; CLU_031953_0_3_6; -.
DR InParanoid; Q51375; -.
DR OMA; EYDLGAR; -.
DR PhylomeDB; Q51375; -.
DR BioCyc; PAER208964:G1FZ6-3174-MON; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..360
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083727"
FT BINDING 76..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 282..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 192
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 95
FT /note="I -> F (in Ref. 1; AAC45419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39121 MW; 94D8756E33383B2D CRC64;
MSKQILVLPG DGIGPEIMAE AVKVLELAND RFQLGFELAE DVIGGAAIDK HGVPLADQTL
QRARQADAVL LGAVGGPKWD RIERDIRPER GLLKIRSQLG LFANLRPAIL YPQLAAASSL
KPEVVAGLDI LIVRELTGGI YFGQPREQRV LENGERQAYD TLPYSESEIR RIARVGFDMA
RVRNNRLCSV DKANVLASSQ LWREVVEEVA KDYPDVELSH MYVDNAAMQL VRAPKQFDVM
VTDNMFGDIL SDEASMLTGS IGMLPSASLD ANNKGMYEPC HGSAPDIAGQ GIANPLATIL
SVSMMLRYSF SQATAADAIE QAVSKVLDQG LRTGDIWSEG CRKVGTREMG DAVVAALKNL
