LEU3A_ASPNG
ID LEU3A_ASPNG Reviewed; 363 AA.
AC P87256;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=3-isopropylmalate dehydrogenase A;
DE Short=3-IPM-DH A;
DE Short=IMDH A;
DE EC=1.1.1.85;
DE AltName: Full=Beta-IPM dehydrogenase A;
GN Name=leu2A;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A733;
RX PubMed=8781173; DOI=10.1007/s002940050137;
RA Williams B.A., Sillaots S., Tsang A., Storms R.;
RT "Isolation by genetic complementation of two differentially expressed genes
RT for beta-isopropylmalate dehydrogenase from Aspergillus niger.";
RL Curr. Genet. 30:305-311(1996).
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; S83228; AAB50827.1; -; mRNA.
DR EMBL; U51130; AAD10278.1; -; mRNA.
DR PIR; S72209; S72209.
DR AlphaFoldDB; P87256; -.
DR SMR; P87256; -.
DR STRING; 5061.CADANGAP00001364; -.
DR PRIDE; P87256; -.
DR VEuPathDB; FungiDB:An01g14130; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1118079; -.
DR VEuPathDB; FungiDB:ATCC64974_12090; -.
DR VEuPathDB; FungiDB:M747DRAFT_262474; -.
DR eggNOG; KOG0786; Eukaryota.
DR BRENDA; 1.1.1.85; 518.
DR UniPathway; UPA00048; UER00072.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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..363
FT /note="3-isopropylmalate dehydrogenase A"
FT /id="PRO_0000083599"
FT BINDING 78..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 135
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 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 287..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Important for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 38670 MW; 20AC729774C646B7 CRC64;
MPAYNIVVFA GDHWGPEVTA EAIKVLRVIE KSRDDITLNL QDHLLGGASI DATANPLTDE
ALAAAKNADA VLLGAIGGPK WGTGAVRPEQ GLLNVRKEMG TFGNLRPCNF AAPSLVEHSP
LKASVCEGVD FNIIRELTGG IYFGDRKKMT AAATMDTEPY SRAEIERITP RAHLALQHNP
PLPVWSLDKA NVLATSRLWR KTVTEIMAKE FPQLKIEHQL IDSAAMIMVK NPRQLNGIIV
TSNLFGDIIS DEASVIPGSL GLLPSASLSG IPDGKGRVNG IYEPIHGSAP DIAGKGIVNP
VAAILSVAMM MQYSFGRFDE ARAIEAAVRN VLESGVRTGD IGGKATTSEV GDAVAAELEK
LLK
