LEU3_THETH
ID LEU3_THETH Reviewed; 345 AA.
AC P61495; P00351;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 95.
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;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
RX PubMed=9086278; DOI=10.1006/jmbi.1996.0797;
RA Wallon G., Kryger G., Lovett S.T., Oshima T., Ringe D., Petsko G.A.;
RT "Crystal structures of Escherichia coli and Salmonella typhimurium 3-
RT isopropylmalate dehydrogenase and comparison with their thermophilic
RT counterpart from Thermus thermophilus.";
RL J. Mol. Biol. 266:1016-1031(1997).
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;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. LeuB type 1 subfamily. {ECO:0000305}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1WAL. {ECO:0000305}.
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DR PDB; 1WAL; X-ray; 2.27 A; A=1-345.
DR PDBsum; 1WAL; -.
DR AlphaFoldDB; P61495; -.
DR SASBDB; P61495; -.
DR SMR; P61495; -.
DR BRENDA; 1.1.1.85; 2305.
DR UniPathway; UPA00048; UER00072.
DR EvolutionaryTrace; P61495; -.
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..345
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083773"
FT BINDING 74..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 274..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 139
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 185
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:1WAL"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1WAL"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:1WAL"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1WAL"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 288..302
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1WAL"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:1WAL"
SQ SEQUENCE 345 AA; 36651 MW; 3521F7363A0550C5 CRC64;
MKVAVLPGDG IGPEVTEAAL KVLRALDEAE GLGLAYEVFP FGGAAIDAFG EPFPEPTRKG
VEEAEAVLLG SVGGPKWDGL PRKISPETGL LSLRKSQDLF ANLRPAKVFP GLERLSPLKE
EIARGVDVLI VRELTGGIYF GEPRGMSEAE AWNTERYSKP EVERVARVAF EAARKRRKHV
VSVDKANVLE VGEFWRKTVE EVGRGYPDVA LEHQYVDAAA MHLVRSPARF DVVVTGNIFG
DILSDLASVL PGSLGLLPSA SLGRGTPVFE PVHGSAPDIA GKGIANPTAA ILSAAMMLEH
AFGLVELARK VEDAVAKALL ETPPPDLGGS AGTEAFTATV LRHLA
