LEU3_BUCAI
ID LEU3_BUCAI Reviewed; 363 AA.
AC P56933; Q9EVG0; Q9KGP9; Q9R6R4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=BUpL05;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OG Plasmid pLeu (pBAp1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10688696; DOI=10.1007/s002849910052;
RA Soler T., Latorre A., Sabater B., Silva F.J.;
RT "Molecular characterization of the Leucine plasmid from Buchnera
RT aphidicola, primary endosymbiont of the aphid Acyrthosiphon pisum.";
RL Curr. Microbiol. 40:264-268(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11133977; DOI=10.1128/jb.183.2.785-790.2001;
RA Wernegreen J.J., Moran N.A.;
RT "Vertical transmission of biosynthetic plasmids in aphid endosymbionts
RT (Buchnera).";
RL J. Bacteriol. 183:785-790(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(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; AJ006878; CAB56191.1; -; Genomic_DNA.
DR EMBL; AF197457; AAG31405.1; -; Genomic_DNA.
DR EMBL; AP001071; BAA95424.1; -; Genomic_DNA.
DR RefSeq; NP_057969.1; NC_002253.1.
DR RefSeq; WP_010892295.1; NC_002253.1.
DR AlphaFoldDB; P56933; -.
DR SMR; P56933; -.
DR EnsemblBacteria; BAA95424; BAA95424; BAA95424.
DR KEGG; buc:BUpL05; -.
DR PATRIC; fig|107806.10.peg.11; -.
DR HOGENOM; CLU_031953_0_3_6; -.
DR OMA; EYDLGAR; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000001806; Plasmid pLeu.
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; Plasmid; Reference proteome.
FT CHAIN 1..363
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083655"
FT BINDING 78..91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 285..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 145
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 101
FT /note="H -> Y (in Ref. 1; CAB56191)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="R -> K (in Ref. 1; CAB56191)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Q -> R (in Ref. 1; CAB56191)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..207
FT /note="RE -> GK (in Ref. 1; CAB56191)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="E -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40479 MW; AB7D6DCF8FFD8D70 CRC64;
MKKNYRIAVL SGDGIGPEVM QEACKILNVL KKYFFLSLEI QKFNIGGIAI EREGVALPKT
TLLGCENSDS ILLGSVGGKK WDNLPVEQRP ERAALLPLRK HFNLFSNLRP AKLYPELKCL
SPLRSDIVKN GFDILCVREL TGGIYFGEPK GFVNKNNTKY AFDTEIYHEY EIIRIAHLAF
KLARSRKKKV CSIDKSNVLQ SSILWREVVE SVSKKYPDVH LSHLYIDNAA MQIIKDPNQF
DVLLCSNLFG DIISDECATI TGSIGMLPSA SFNEKNFGLY EPAGGSAPDI EGKNIANPIA
QILSLSMLVR YGMNLNQIAD KIDKAVNNVL KKGYRTSDIS HDNNFLKTDE MGDLIVDSLI
NGE
