LEU3_BURTA
ID LEU3_BURTA Reviewed; 355 AA.
AC Q2T7H6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=BTH_II0674;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(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; CP000085; ABC35976.1; -; Genomic_DNA.
DR RefSeq; WP_009895843.1; NZ_CP008786.1.
DR PDB; 4IWH; X-ray; 1.75 A; A/B=1-355.
DR PDB; 4XXV; X-ray; 1.70 A; A/B=1-355.
DR PDBsum; 4IWH; -.
DR PDBsum; 4XXV; -.
DR AlphaFoldDB; Q2T7H6; -.
DR SMR; Q2T7H6; -.
DR PRIDE; Q2T7H6; -.
DR EnsemblBacteria; ABC35976; ABC35976; BTH_II0674.
DR KEGG; bte:BTH_II0674; -.
DR HOGENOM; CLU_031953_0_3_4; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 1551125at2; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000001930; Chromosome II.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis;
KW Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..355
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000250109"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 280..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 135
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 190
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 11..25
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4IWH"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4XXV"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4XXV"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 164..179
FT /evidence="ECO:0007829|PDB:4XXV"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4XXV"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4XXV"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:4XXV"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4XXV"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:4XXV"
SQ SEQUENCE 355 AA; 38242 MW; CE8C13AF0007C5E4 CRC64;
MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEHAPVGGA GYEASGHPLP DATLALAKEA
DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA
GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGEREGFDTM RYSEPEVRRI AHVAFQAAQK
RAKKLLSVDK SNVLETSQFW RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT
GNMFGDILSD EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA
AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCR QVGTAAMGDA VVAAL
