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Database: UniProt/TrEMBL
Entry: G8ZQ45_TORDC
LinkDB: G8ZQ45_TORDC
Original site: G8ZQ45_TORDC 
ID   G8ZQ45_TORDC            Unreviewed;       414 AA.
AC   G8ZQ45;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUL-2017, entry version 32.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   Name=TDEL0B06100 {ECO:0000313|EMBL:CCE90739.1};
GN   ORFNames=TDEL_0B06100 {ECO:0000313|EMBL:CCE90739.1};
OS   Torulaspora delbrueckii (strain ATCC 10662 / CBS 1146 / NBRC 0425 /
OS   NCYC 2629 / NRRL Y-866) (Yeast) (Candida colliculosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Torulaspora.
OX   NCBI_TaxID=1076872 {ECO:0000313|Proteomes:UP000005627};
RN   [1] {ECO:0000313|EMBL:CCE90739.1, ECO:0000313|Proteomes:UP000005627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10662 / CBS 1146 / NBRC 0425 / NCYC 2629 / NRRL Y-866
RC   {ECO:0000313|Proteomes:UP000005627};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH. {ECO:0000256|PIRNR:PIRNR000108}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|PIRNR:PIRNR000108}.
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DR   EMBL; HE616743; CCE90739.1; -; Genomic_DNA.
DR   RefSeq; XP_003679950.1; XM_003679902.1.
DR   STRING; 4950.XP_003679950.1; -.
DR   EnsemblFungi; CCE90739; CCE90739; TDEL_0B06100.
DR   GeneID; 11505055; -.
DR   KEGG; tdl:TDEL_0B06100; -.
DR   InParanoid; G8ZQ45; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000005627; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) 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:0006102; P:isocitrate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11822; PTHR11822; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005627};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000108};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005627};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN        8    398       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      74     76       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     309    314       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       93     99       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       274    274       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      76     76       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      81     81       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     108    108       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     131    131       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     259    259       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     327    327       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        138    138       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        211    211       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   414 AA;  46730 MW;  AC163493E89DD731 CRC64;
     MKVTVKSPIV EMDGDEQTRI IWQLIKDKLI LPFLDVDLKY YDLSVTNRDD TNDQVTVDSA
     NATLKYGVAV KCATITPDEA RVEEFKLKKM WRSPNGTIRN ILGGTVFREP IVIPRIPRLV
     PQWEKAIIIG RHAFGDQYRA TDVVIPGEGE LRLVFKSKDG KSDQDLHVFD FPKDGGVGMA
     MYNTTESITG FAKASFELAL ERKLPLYSTT KNTILKKYDG KFKDVFEQMY ADQYQSRFEE
     LGIWYEHRLI DDMVAQMLKS KGGFIIAMKN YDGDVESDIV AQGFGSLGLM TSVLVTPDGK
     TFESEAAHGT VTRHFRQHQQ GKETSTNSIA SIFAWTRGVI QRGKLDDTPE VVRFGELLEK
     ATVDTVQVDG IMTKDLALIL GKTDRSSYTT TEGFIDSVEH RLVKEFQHAF PSRL
//
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