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Database: UniProt/TrEMBL
Entry: E9EB02_METAQ
LinkDB: E9EB02_METAQ
Original site: E9EB02_METAQ 
ID   E9EB02_METAQ            Unreviewed;       458 AA.
AC   E9EB02;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   07-JUN-2017, entry version 36.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=MAC_07050 {ECO:0000313|EMBL:EFY86933.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY86933.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY86933.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z.,
RA   Hu X., Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W.,
RA   Wang S., Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y.,
RA   Feng M.G., Xia Y., Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(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; GL698536; EFY86933.1; -; Genomic_DNA.
DR   RefSeq; XP_007813390.1; XM_007815199.1.
DR   ProteinModelPortal; E9EB02; -.
DR   EnsemblFungi; EFY86933; EFY86933; MAC_07050.
DR   GeneID; 19251361; -.
DR   KEGG; maw:MAC_07050; -.
DR   InParanoid; E9EB02; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
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:UP000002499};
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:UP000002499};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       57    446       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     123    125       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     357    362       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      142    148       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       299    299       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       322    322       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     125    125       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     130    130       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     157    157       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     180    180       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     307    307       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     375    375       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        187    187       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        259    259       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   458 AA;  51358 MW;  4BFDB4F66E9BE921 CRC64;
     MNSAARLLSS PLPLRRVPIA SVRASSSRFA PSFGAVRTFS VSARNMAAAR KIKVKNPVVE
     LDGDEMTRII WQTIKDKFIY PYLDIDLKYY DLGLEYRDKT NDQVTIDAAE AIKKYSVGVK
     CATITPDEAR VEEFKLKQMW LSPNGTIRNA LGGTVFREPI VIPRIPRLVP GWEKPIIIGR
     HAFGDQYRAK DLVAPGPGKL SMVYTPEGGE PQEVEVFQFK NGGGVAQAQY NTDESITGFA
     HASFKLALDK GLPLYMSTKN TILKKYDGRF KDIFQELYDT QYKKDFEAKK IWYEHRLIDD
     MVAQMIKSKG GYIMALKNYD GDVQSDIVAQ GFGSLGLMTS VLITPDGKTF ESEAAHGTVT
     RHYREHQKGK ETSTNPIASI FAWTRGLTQR GKLDNTPELV AFAESLEQAC IDTVDKDGVM
     TKDLALACGK NERSDYVTTN EYLNAVERRM KTILKEKL
//
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