LEU3_PHACH
ID LEU3_PHACH Reviewed; 380 AA.
AC O59930;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=LEU2;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 34541 / NBRC 31249 / ME-446 / PRL 2750;
RX PubMed=9647839; DOI=10.1128/aem.64.7.2624-2629.1998;
RA Zapanta L.S., Hattori T., Rzetskaya M., Tien M.;
RT "Cloning of Phanerochaete chrysosporium leu2 by complementation of
RT bacterial auxotrophs and transformation of fungal auxotrophs.";
RL Appl. Environ. Microbiol. 64:2624-2629(1998).
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; AF050668; AAC26195.1; -; mRNA.
DR AlphaFoldDB; O59930; -.
DR SMR; O59930; -.
DR PRIDE; O59930; -.
DR VEuPathDB; FungiDB:AGR57_2264; -.
DR UniPathway; UPA00048; UER00072.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:EnsemblFungi.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD;
KW Oxidoreductase.
FT CHAIN 1..380
FT /note="3-isopropylmalate dehydrogenase"
FT /id="PRO_0000083614"
FT BINDING 80..92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 300..312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 145
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 196
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 40643 MW; 70724990A2AD3A95 CRC64;
MSKRTFKIVI LPGDGIGPEV VAEATRVLEV VSASSSDVEI KLETHDFGGC SIDKHGEPLT
AATLEACKLA DAILLGAIGG PKWGVNSKVR PEQALLALRK ALGLYANIRP ANFASDSLLA
YSPLKPSVAR GVDIIVIREL IGGAYFGERK ELGARAQEDA AWDTMIYSVP EVQRITRSRR
QVASPDPPLP VHSIDKANVL ASSRLWRKVA TETIQNEFPQ LKLDHHLVDS ASMLIVANPK
KLNGVILTEN LFGDILSDES SVIPGSLGLL PSASLAARPL WPNTAHRRSS PRRVYEPIHG
SAPDIAGQGI ANPIGTILSA AMLCGTRSVW RSPAKAIEAA VEGARRQGDR REGLRTADLG
GSSKTKDIGH KVVEILKATL
