LEU3_SHEON
ID LEU3_SHEON Reviewed; 364 AA.
AC Q8E9N3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=SO_4235;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; 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; AE014299; AAN57206.1; -; Genomic_DNA.
DR RefSeq; NP_719762.1; NC_004347.2.
DR RefSeq; WP_011073915.1; NZ_CP053946.1.
DR PDB; 3VKZ; X-ray; 1.84 A; A=2-364.
DR PDB; 3VL2; X-ray; 2.06 A; A=2-364.
DR PDB; 3VL3; X-ray; 1.80 A; A=2-364.
DR PDB; 3VL4; X-ray; 1.88 A; A=2-364.
DR PDB; 3VL6; X-ray; 2.07 A; A=2-364.
DR PDB; 3VL7; X-ray; 2.20 A; A=2-364.
DR PDB; 3VMJ; X-ray; 1.56 A; A=2-364.
DR PDB; 3VML; X-ray; 1.56 A; A=2-68, A=329-364.
DR PDB; 3WZV; X-ray; 1.90 A; A=2-364.
DR PDB; 3WZW; X-ray; 1.80 A; A=2-364.
DR PDB; 3WZX; X-ray; 1.90 A; A=2-364.
DR PDB; 3WZY; X-ray; 1.55 A; A=2-364.
DR PDBsum; 3VKZ; -.
DR PDBsum; 3VL2; -.
DR PDBsum; 3VL3; -.
DR PDBsum; 3VL4; -.
DR PDBsum; 3VL6; -.
DR PDBsum; 3VL7; -.
DR PDBsum; 3VMJ; -.
DR PDBsum; 3VML; -.
DR PDBsum; 3WZV; -.
DR PDBsum; 3WZW; -.
DR PDBsum; 3WZX; -.
DR PDBsum; 3WZY; -.
DR AlphaFoldDB; Q8E9N3; -.
DR SMR; Q8E9N3; -.
DR STRING; 211586.SO_4235; -.
DR PaxDb; Q8E9N3; -.
DR KEGG; son:SO_4235; -.
DR PATRIC; fig|211586.12.peg.4094; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_3_6; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 1551125at2; -.
DR PhylomeDB; Q8E9N3; -.
DR BioCyc; SONE211586:G1GMP-3912-MON; -.
DR BRENDA; 1.1.1.85; 5706.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..364
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083744"
FT BINDING 76..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 283..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 143
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT SITE 193
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01033"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 14..32
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3WZY"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:3WZY"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3WZY"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3WZY"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:3WZY"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:3WZY"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:3WZY"
SQ SEQUENCE 364 AA; 39368 MW; 3DB9FA335E8F72C9 CRC64;
MSYQIAVLAG DGIGPEVMAE ARKVLKAVEA RFGLNIEYTE YDVGGIAIDN HGCPLPEATL
KGCEAADAIL FGSVGGPKWE KLPPNEQPER GALLPLRGHF ELFCNLRPAK LHDGLEHMSP
LRSDISARGF DVLCVRELTG GIYFGKPKGR QGEGESEEAF DTMRYSRREI SRIARIAFEA
ARGRRKKVTS VDKANVLACS VLWRQVVEEV AVDFPDVELE HIYIDNATMQ LLRRPDEFDV
MLCSNLFGDI LSDEIAMLTG SMGLLSSASM NSTGFGLFEP AGGSAPDIAG KGIANPIAQI
LSAALMLRHS LKQEEAASAI ERAVTKALNS GYLTGELLSS DQRHKAKTTV QMGDFIADAV
KAGV
