(data stored in SCRATCH zone)

SWISSPROT: Q757F2_ASHGO

ID   Q757F2_ASHGO            Unreviewed;       425 AA.
AC   Q757F2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=AGOS_AER061C {ECO:0000313|EMBL:AAS52745.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52745.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52745.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:16087, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC         Evidence={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; AE016818; AAS52745.1; -; Genomic_DNA.
DR   RefSeq; NP_984921.1; NM_210275.1.
DR   STRING; 33169.AAS52745; -.
DR   EnsemblFungi; AAS52745; AAS52745; AGOS_AER061C.
DR   GeneID; 4621124; -.
DR   KEGG; ago:AGOS_AER061C; -.
DR   HOGENOM; HOG000019858; -.
DR   InParanoid; Q757F2; -.
DR   KO; K00031; -.
DR   OMA; HGTVQRH; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
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;
DR   PRODOM; Q757F2.
DR   SWISS-2DPAGE; Q757F2.
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000108, 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:UP000000591};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN          27..416
FT                   /note="Iso_dh"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   NP_BIND         93..95
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   NP_BIND         327..332
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   REGION          112..118
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   METAL           269
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   METAL           292
FT                   /note="Magnesium or manganese"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   BINDING         95
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         100
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         127
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         150
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         277
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         345
FT                   /note="NADP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   SITE            157
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT   SITE            229
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ   SEQUENCE   425 AA;  47064 MW;  9A6E7CCE800A8812 CRC64;
     MLGRGRMLGR RLFSGSRAAA RIRVKTPVVE LDGDEMTRII WERIKQQLVL PHVDVELKYY
     DLSITSRDAT SDQVTVDAAH AIKQYGVGVK CATITPDEAR VREFGLKKMW RSPNGTIRNI
     LGGTVFREPI VIPRIPRLVP GWEKPIIIGR HAHGDQYKAT DAVVPGAGTL DLVFRPADGS
     APTSLHVYDF AGPGVALAMY NTEESIRGFA HASFRLALAK QLNLFLSTKN TILKQYDGRF
     KDVFEELYQA QYKAEFERLG IYYEHRLIDD MVAQMVKSKG GFIMALKNYD GDVQSDIVAQ
     GFGSLGLMTS VLVTPDGKTF ESEAAHGTVT RHFRQHQAGK ETSTNSIASI FAWTRGLAKR
     GELDNTPDVV NFAHALEAAT TNTVQLDGIM TKDLALACGR SDRSAYVNTN EFIDAVEARL
     KKELA
//

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