LEU3_WEICA
ID LEU3_WEICA Reviewed; 366 AA.
AC P12010;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
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;
OS Weizmannia coagulans (Bacillus coagulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Weizmannia.
OX NCBI_TaxID=1398;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sekiguchi T., Ortega-Cesena J., Nosoh Y., Ohashi S., Tsuda K., Kanaya S.;
RT "DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of
RT Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae
RT and Thermus thermophilus.";
RL Biochim. Biophys. Acta 867:36-44(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=9498551; DOI=10.1093/oxfordjournals.jbchem.a021867;
RA Tsuchiya D., Sekiguchi T., Takenaka A.;
RT "Crystal structure of 3-isopropylmalate dehydrogenase from the moderate
RT facultative thermophile, Bacillus coagulans: two strategies for
RT thermostabilization of protein structures.";
RL J. Biochem. 122:1092-1104(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. {ECO:0000269|PubMed:9498551}.
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; M33099; AAA22554.1; ALT_SEQ; Genomic_DNA.
DR PIR; A24537; DEBSIC.
DR RefSeq; WP_029141661.1; NZ_QRUW01000015.1.
DR PDB; 1V53; X-ray; 2.85 A; A/B=1-366.
DR PDB; 1V5B; X-ray; 2.95 A; A/B/C/D/E/F/G/H=1-366.
DR PDB; 2AYQ; X-ray; 3.00 A; A/B=1-366.
DR PDBsum; 1V53; -.
DR PDBsum; 1V5B; -.
DR PDBsum; 2AYQ; -.
DR AlphaFoldDB; P12010; -.
DR SMR; P12010; -.
DR STRING; 1398.AB434_0291; -.
DR GeneID; 29815080; -.
DR UniPathway; UPA00048; UER00072.
DR EvolutionaryTrace; P12010; -.
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..366
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083638"
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 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 280..292
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 190
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:2AYQ"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 164..180
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1V5B"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1V53"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:2AYQ"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:1V53"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:1V53"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:1V53"
SQ SEQUENCE 366 AA; 39809 MW; 05958B786718408E CRC64;
MKMKLAVLPG DGIGPEVMDA AIRVLKTVLD NDGHEAVFEN ALIGGAAIDE AGTPLPEETL
DICRRSDAIL LGAVGGPKWD HNPASLRPEK GLLGLRKEMG LFANLRPVKA YATLLNASPL
KRERVENVDL VIVRELTGGL YFGRPSERRG PGENEVVDTL AYTREEIERI IEKAFQLAQI
RRKKLASVDK ANVLESSRMW REIAEETAKK YPDVELSHML VDSTSMQLIA NPGQFDVIVT
ENMFGDILSD EASVITGSLG MLPSASLRSD RFGMYEPVHG SAPDIAGQGK ANPLGTVLSA
ALMLRYSFGL EKEAAAIEKA VDDVLQDGYC TGDLQVANGK VVSTIELTDR LIEKLNNSAA
RPRIFQ
