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Database: UniProt
Entry: G8WT07_STREN
LinkDB: G8WT07_STREN
Original site: G8WT07_STREN 
ID   G8WT07_STREN            Unreviewed;       327 AA.
AC   G8WT07;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:AEW96713.1};
GN   OrderedLocusNames=SCATT_43420 {ECO:0000313|EMBL:AEW96713.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW96713.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000624};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP003219; AEW96713.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8WT07; -.
DR   STRING; 1003195.SCATT_43420; -.
DR   KEGG; scy:SCATT_43420; -.
DR   PATRIC; fig|1003195.29.peg.4335; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_11; -.
DR   Proteomes; UP000007842; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT   DOMAIN          1..321
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   327 AA;  34806 MW;  C99935BEC6835D95 CRC64;
     MAEGLKVLRA VLDEDVKLET TEYDFGARRY HATGDTLTDA DLAALKGHDA ILLGAIGDPS
     VPSGVLERGF LLKLRFAFDH YVNLRPGKLF PNVASPLAGS PRIDFVVVRE GTEGPYTGNG
     GSLRTGTPHE VATEVSVNTA YGIERVVRDA YARAQARPRK KLTLVHKNNV LVHAGHLWKS
     VFDRVGREFP EVTTDYLHVD AATIFFVTQP ERFDVIVTDN LFGDILTDLA AAVTGGIGLA
     ASGNINPAGE FPSMFEPVHG SAPDIAGQGK ADPTATVLSV ALLLDHLGHR EQAARVEEAV
     AADLAGRTGE PRTTAEIGDA LAARVSG
//
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