ID Q2UQS4_ASPOR Unreviewed; 364 AA.
AC Q2UQS4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 13-SEP-2023, entry version 110.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
DE EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
GN ORFNames=AO090005001122 {ECO:0000313|EMBL:BAE56091.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE56091.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE56091.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 {ECO:0000256|RuleBase:RU004445}.
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 Evidence={ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004445};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|RuleBase:RU004445};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4.
CC {ECO:0000256|RuleBase:RU004445}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004445}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|RuleBase:RU004443}.
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DR EMBL; AP007151; BAE56091.1; -; Genomic_DNA.
DR RefSeq; XP_001818093.1; XM_001818041.2.
DR AlphaFoldDB; Q2UQS4; -.
DR SMR; Q2UQS4; -.
DR STRING; 510516.Q2UQS4; -.
DR EnsemblFungi; BAE56091; BAE56091; AO090005001122.
DR GeneID; 5990038; -.
DR KEGG; aor:AO090005001122; -.
DR VEuPathDB; FungiDB:AO090005001122; -.
DR HOGENOM; CLU_031953_0_3_1; -.
DR OMA; MVKNPRQ; -.
DR OrthoDB; 2606404at2759; -.
DR UniPathway; UPA00048; UER00072.
DR Proteomes; UP000006564; Chromosome 1.
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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR NCBIfam; TIGR00169; leuB; 1.
DR PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU004445};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW ECO:0000256|RuleBase:RU004445}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004445};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004445};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004443};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 5..355
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 364 AA; 38555 MW; 37D67301363AE872 CRC64;
MSSYNIVVFG GDHCGPEVTA EAIKVLRAVE KNCDVTFNLQ DHLLGGASID ATGSPLTDEA
LNAAKNADAV LLGAIGGPKW GTGAVRPEQG ILKLRKEMGT FGNLRPCNFA APSLVESSPL
RADVCRGVNF NIIRELTGGI YFGERKEDDG SGYAMDTEPY SRAEIERIIR LAAHLALQHD
PPLPVWSLDK ANVLATSRLW RKVVTEVMAK EFPQLKIEHQ LIDSAAMIMV KNPRQLNGIV
VTSNLFGDII SDEASVIPGS LGLLPSASLS GIPDGNSKVN GIYEPIHGSA PDIAGKGIVN
PVAAILSVAM MMQYSFGLFA EARAIEQAVS NVIESGVRTG DIGGKATTAE VGDAVAAELE
KLLK
//