LEU3_NEUCR
ID LEU3_NEUCR Reviewed; 368 AA.
AC P34738; Q7RVH7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=3-isopropylmalate dehydrogenase;
DE Short=3-IPM-DH;
DE Short=IMDH;
DE EC=1.1.1.85;
DE AltName: Full=Beta-IPM dehydrogenase;
GN Name=leu-1; ORFNames=NCU06232;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8294021; DOI=10.1016/0378-1119(93)90484-k;
RA Li Q., Jarai G., Yaghmai B., Marzluf G.A.;
RT "The leu-1 gene of Neurospora crassa: nucleotide and deduced amino acid
RT sequence comparisons.";
RL Gene 136:301-305(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
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. {ECO:0000305}.
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DR EMBL; U01061; AAD10616.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA33847.1; -; Genomic_DNA.
DR PIR; T46607; T46607.
DR RefSeq; XP_963083.1; XM_957990.2.
DR AlphaFoldDB; P34738; -.
DR SMR; P34738; -.
DR STRING; 5141.EFNCRP00000005960; -.
DR EnsemblFungi; EAA33847; EAA33847; NCU06232.
DR GeneID; 3879238; -.
DR KEGG; ncr:NCU06232; -.
DR VEuPathDB; FungiDB:NCU06232; -.
DR HOGENOM; CLU_031953_0_3_1; -.
DR InParanoid; P34738; -.
DR OMA; MATHNIV; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..368
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083613"
FT BINDING 79..91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 291..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 144
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="G -> C (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="P -> S (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="F -> C (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="L -> W (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="G -> V (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="G -> C (in Ref. 1; AAD10616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 38661 MW; EC590007A1E3FF48 CRC64;
MATHNIVVFG GDHCGPEVVL EAIKVLKAIE TNSPSAGKFN LQNHLLGGAS IDKHNDPLTD
EALNAAKAAD AVLLGAIGGP EWGTSSTVRP EQGLLKLRKE LGTYGNLRPC NFASESLVDS
SPLKAEVCRG TDFIVVRELT GGIYFGDRTE DDGSGYACDT EPYSRAEIVR IARLAGFLAL
AKNPPAKVWS LDKANVLATS RLWRKTVTDV ISKEFPQLQL EHQLIDSAAM LLVKNPRALN
GVVITSNLFG DIISDEASVI PGSIGLLPSA SLGGIPDGKG KCNGIYEPIH GSAPDISGKG
IVNPVGTILS VAMMLRYSLN LPKEADAVEA AVKAAIDNGT KTKDLGGNAT TSDMGNAVVA
ELEKILKA
