LEU3_THEMA
ID LEU3_THEMA Reviewed; 354 AA.
AC Q9WZ26;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
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; OrderedLocusNames=TM_0556;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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:0000250}.
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; AE000512; AAD35641.1; -; Genomic_DNA.
DR PIR; B72363; B72363.
DR RefSeq; NP_228366.1; NC_000853.1.
DR RefSeq; WP_004081326.1; NZ_CP011107.1.
DR PDB; 1VLC; X-ray; 1.90 A; A=1-354.
DR PDBsum; 1VLC; -.
DR AlphaFoldDB; Q9WZ26; -.
DR SMR; Q9WZ26; -.
DR STRING; 243274.THEMA_01895; -.
DR EnsemblBacteria; AAD35641; AAD35641; TM_0556.
DR KEGG; tma:TM0556; -.
DR eggNOG; COG0473; Bacteria.
DR InParanoid; Q9WZ26; -.
DR OMA; EYDLGAR; -.
DR OrthoDB; 1551125at2; -.
DR UniPathway; UPA00048; UER00072.
DR EvolutionaryTrace; Q9WZ26; -.
DR Proteomes; UP000008183; 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..354
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083771"
FT BINDING 74..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275..287
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 187
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 11..30
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:1VLC"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1VLC"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1VLC"
FT STRAND 260..274
FT /evidence="ECO:0007829|PDB:1VLC"
FT TURN 278..284
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 306..321
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1VLC"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:1VLC"
SQ SEQUENCE 354 AA; 39190 MW; 2C93ACBF888A0D38 CRC64;
MKIAVLPGDG IGPEVVREAL KVLEVVEKKT GKTFEKVFGH IGGDAIDRFG EPLPEETKKI
CLEADAIFLG SVGGPKWDDL PPEKRPEIGG LLALRKMLNL YANIRPIKVY RSLVHVSPLK
EKVIGSGVDL VTVRELSYGV YYGQPRGLDE EKGFDTMIYD RKTVERIART AFEIAKNRRK
KVTSVDKANV LYSSMLWRKV VNEVAREYPD VELTHIYVDN AAMQLILKPS QFDVILTTNM
FGDILSDESA ALPGSLGLLP SASFGDKNLY EPAGGSAPDI AGKNIANPIA QILSLAMMLE
HSFGMVEEAR KIERAVELVI EEGYRTRDIA EDPEKAVSTS QMGDLICKKL EEIW
