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Database: UniProt/TrEMBL
Entry: A0A010QLN7_9PEZI
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ID   A0A010QLN7_9PEZI        Unreviewed;       452 AA.
AC   A0A010QLN7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=CFIO01_12107 {ECO:0000313|EMBL:EXF80957.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF80957.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF80957.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF80957.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EXF80957.1}.
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DR   EMBL; JARH01000412; EXF80957.1; -; Genomic_DNA.
DR   RefSeq; XP_007595412.1; XM_007595350.1.
DR   EnsemblFungi; EXF80957; EXF80957; CFIO01_12107.
DR   GeneID; 19041957; -.
DR   KEGG; cfj:CFIO01_12107; -.
DR   KO; K00031; -.
DR   Proteomes; UP000020467; 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:UP000020467};
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:UP000020467};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       51    440       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     117    119       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     351    356       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      136    142       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       293    293       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       316    316       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     119    119       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     124    124       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     151    151       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     174    174       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     301    301       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     369    369       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        181    181       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        253    253       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   452 AA;  50692 MW;  FE4B8E0E99C56007 CRC64;
     MNAARFLRRP ATFALRPSFI VPQSSASFSS SASFNFARTM AAAAKIKVKN PVVELDGDEM
     TRIIWQTIKD KFIHPYLDID LKYYDLGLPY RDETNDKVTL DAAEAIKKYS VGVKCATITP
     DEQRVEEFKL KQMWLSPNGT IRNHLGGTVF REPIVIPRVP RLVPGWKKPI IIGRHAFGDQ
     YRAKDAVLPG NGTLKMVYTP EGGEPQEIEV YKFKNGGGVA QTQYNTDESI TGFAHASFKL
     ALTKKLPLYM STKNTILKKY DGRFKDIFQE LYETKYKAEF EAAGIWYEHR LIDDMVAQMV
     KSSGGYIMAL KNYDGDVQSD IVAQGFGSLG LMTSVLITPD GKTFESEAAH GTVTRHYREH
     QKGNETSTNP IASIFAWTRG LIQRGKLDET PEVVAFAESL EKACIDTVDV DGIMTKDLAL
     ACGKTARSDY VTTNEYLNAV ERRMKNILKE KL
//
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