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Database: UniProt/TrEMBL
Entry: E6QZC0_CRYGW
LinkDB: E6QZC0_CRYGW
Original site: E6QZC0_CRYGW 
ID   E6QZC0_CRYGW            Unreviewed;       449 AA.
AC   E6QZC0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   07-JUN-2017, entry version 43.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   OrderedLocusNames=CGB_A2040C {ECO:0000313|EMBL:ADV19527.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV19527.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV19527.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T.,
RA   Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q.,
RA   Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A.,
RA   Meyer W., Carter D., Schein J., Krzywinski M., Kwon-Chung K.J.,
RA   Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F., Siddiqui A.,
RA   Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T.,
RA   Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q.,
RA   Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A.,
RA   Meyer W., Carter D., Schein J., Krzywinski M., Kwong-Chung K.J.,
RA   Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F.F., Siddiqui A.,
RA   Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(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; CP000286; ADV19527.1; -; Genomic_DNA.
DR   RefSeq; XP_003191314.1; XM_003191266.1.
DR   STRING; 367775.XP_003191314.1; -.
DR   EnsemblFungi; ADV19527; ADV19527; CGB_A2040C.
DR   GeneID; 10188754; -.
DR   KEGG; cgi:CGB_A2040C; -.
DR   EuPathDB; FungiDB:CGB_A2040C; -.
DR   eggNOG; KOG1526; Eukaryota.
DR   eggNOG; COG0538; LUCA.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000007805; Chromosome A.
DR   GO; GO:0005739; C:mitochondrion; 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:InterPro.
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:UP000007805};
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   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       45    436       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     111    113       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     345    350       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      130    136       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       287    287       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       310    310       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     113    113       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     118    118       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     145    145       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     168    168       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     295    295       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     363    363       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        175    175       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        247    247       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   449 AA;  50278 MW;  6DB937016E5EC419 CRC64;
     MLARSTSAFT RSSLLRSTRP LAFAMASRNY ASTPAGIERI KVKNPVVEID GDEMTRIIWK
     KIREELILPY VDVDLKYYDL GMESRDATND QITIDSAEAI KKYSVGVKCA TITPDEARVK
     EFNLKEMWRS PNGTIRNILG GTVFREPIIL DKIPKPVPGW TKPICIGRHA FGDQYRSTDF
     LAPGPGKLTL TYTPADGGAP TELNVYDFKG KGVALAMYNT DESIYGFAHA SFKMALSKKM
     PLFMSTKNTI LKKYDGRFKD IFQEVYESTY KTEFEKLGLY YEHRLIDDMV AQAIKSSGGF
     VWACKNYDGD VMSDILAQGF GSLGMMTSEL ITPDGKTMES EAAHGTVTRH YRQYQAGHET
     STNPVASIFA WTRGLAFRAK LDETPALEAF AKDLEAACVE VIDKDGIMTK DLALAMKGKD
     MTRDDWVTTD VYMKKVNERL VEKLKARSA
//
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