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Database: UniProt
Entry: R7T1Y6_DICSQ
LinkDB: R7T1Y6_DICSQ
Original site: R7T1Y6_DICSQ 
ID   R7T1Y6_DICSQ            Unreviewed;       385 AA.
AC   R7T1Y6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-SEP-2023, entry version 46.
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=DICSQDRAFT_85316 {ECO:0000313|EMBL:EJF62396.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF62396.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF62396.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF62396.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH719406; EJF62396.1; -; Genomic_DNA.
DR   RefSeq; XP_007365108.1; XM_007365046.1.
DR   AlphaFoldDB; R7T1Y6; -.
DR   GeneID; 18844593; -.
DR   KEGG; dsq:DICSQDRAFT_85316; -.
DR   HOGENOM; CLU_031953_0_3_1; -.
DR   OMA; EYDLGAR; -.
DR   OrthoDB; 2606404at2759; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000053319; Unassembled WGS sequence.
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   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:UP000053319}.
FT   DOMAIN          7..377
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   385 AA;  40136 MW;  D55A0662A74BC62E CRC64;
     MAKKSFRVVV LPGDGIGPEV VAEAVRVLEV ISAASQDVEL KLESHEFGGC AIDSTGEPLP
     ASTLKACQEA DAILMGSIGG PKWGVNSKVR PEQGLLGLRK ALGLYANIRP ANFASDSLLA
     NSPLKPSVAE GVDIIVVREL IGGVYFGARQ ELGAGAGPEA ETAWDTMVYS VQEVQRITRV
     AAQIALQANP PLPIHSIDKA NVLASSRLWR KVVIETLQAE YPQLTLDHHL VDSASMLIVA
     NPKKLNGVIV TENLFGDILS DEASVIPGSL GLLPSASLAG APSVADATSP GFKPTPGLYE
     PIHGSAPDIA GKGIANPVGT ILSAAMLLRY SLGLEKYAQA IESAVRKALD TQATGGLELR
     TADLGGKVTT KELGDKVVEI LKGLV
//
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