LEU3_BUCUM
ID LEU3_BUCUM Reviewed; 365 AA.
AC Q9EVG9; Q99Q96; Q99QE7; Q9AJ51; Q9AJ53; Q9AJ54;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
OS Buchnera aphidicola subsp. Uroleucon ambrosiae.
OG Plasmid pLeu (pBAp1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118117;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 245-365.
RC STRAIN=AL.012, AZ.023, AZ.026, AZ.065, AZ.180, DC.005, GA.039, GA2181,
RC IL.014, IL2.17, IN.018, KY.172, KY2.37, LA.013, MI.035, MN.001, MNb027,
RC MS.040, NY.016, OH.036, TN.173, TN2.38, UT.002, and VA.015;
RX PubMed=11156972; DOI=10.1093/genetics/157.2.477;
RA Funk D.J., Wernegreen J.J., Moran N.A.;
RT "Intraspecific variation in symbiont genomes: bottlenecks and the aphid-
RT Buchnera association.";
RL Genetics 157:477-489(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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF197454; AAG31396.1; -; Genomic_DNA.
DR EMBL; AF196403; AAK21724.1; -; Genomic_DNA.
DR EMBL; AF196404; AAK21725.1; -; Genomic_DNA.
DR EMBL; AF196407; AAK21730.1; -; Genomic_DNA.
DR EMBL; AF196408; AAK21732.1; -; Genomic_DNA.
DR EMBL; AF196410; AAK21736.1; -; Genomic_DNA.
DR EMBL; AF196412; AAK21740.1; -; Genomic_DNA.
DR EMBL; AF196413; AAK21742.1; -; Genomic_DNA.
DR EMBL; AF196414; AAK21744.1; -; Genomic_DNA.
DR EMBL; AF196415; AAK21746.1; -; Genomic_DNA.
DR EMBL; AF196417; AAK21750.1; -; Genomic_DNA.
DR EMBL; AF196418; AAK21752.1; -; Genomic_DNA.
DR EMBL; AF196419; AAK21754.1; -; Genomic_DNA.
DR EMBL; AF196420; AAK21756.1; -; Genomic_DNA.
DR EMBL; AF196421; AAK21758.1; -; Genomic_DNA.
DR EMBL; AF196422; AAK21760.1; -; Genomic_DNA.
DR EMBL; AF196423; AAK21762.1; -; Genomic_DNA.
DR EMBL; AF196424; AAK21764.1; -; Genomic_DNA.
DR EMBL; AF196402; AAK21722.1; -; Genomic_DNA.
DR EMBL; AF196406; AAK21728.1; -; Genomic_DNA.
DR EMBL; AF196416; AAK21748.1; -; Genomic_DNA.
DR EMBL; AF196425; AAK21766.1; -; Genomic_DNA.
DR EMBL; AF196409; AAK21734.1; -; Genomic_DNA.
DR EMBL; AF196411; AAK21738.1; -; Genomic_DNA.
DR EMBL; AF196405; AAK21727.1; -; Genomic_DNA.
DR UniPathway; UPA00048; UER00072.
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.
FT CHAIN 1..365
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083664"
FT BINDING 78..91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 287..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 146
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 197
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT VARIANT 255
FT /note="V -> I (in strain: GA2181)"
SQ SEQUENCE 365 AA; 40759 MW; 14F1E76B771C5764 CRC64;
MKTKYRISVL PGDGIGPEVM REAYKILNIL KNHFSLPLEI KEFNIGGAAI DQEGVALPKK
TLLGCENSDA ILFGSVGGKK WDHLPIDKRP ERASLLPLRK HFNLFANLRP AQLYSELKYL
SPLRSDIXIK NGFNILCIRE LTGGIYFGKP TGRXLKKNNI EYAFDTEIYY DYEINRIAHL
AFQLAQTRNY KVCSIDKSNV LNSSVLWRET VQKVSKNYPD VHLSHLYIDN ATMQIIKDPN
QFDILLCSNL FGDIVSDECA IITGSIGMLP SASLNEKKFG LYEPAGGSAP DIEGKNIANP
IAQILSVSML VRYGMNLKKI ADKIDQSVIS VLKKGYRTAD ISNNNNYLKT NEMGDVIANT
LISGE
