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Database: UniProt/TrEMBL
Entry: W6YS85_COCMI
LinkDB: W6YS85_COCMI
Original site: W6YS85_COCMI 
ID   W6YS85_COCMI            Unreviewed;       486 AA.
AC   W6YS85;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   07-JUN-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=COCMIDRAFT_108688 {ECO:0000313|EMBL:EUC40485.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC40485.1, ECO:0000313|Proteomes:UP000054032};
RN   [1] {ECO:0000313|EMBL:EUC40485.1, ECO:0000313|Proteomes:UP000054032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC40485.1,
RC   ECO:0000313|Proteomes:UP000054032};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
RA   Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
RA   Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
RA   Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
RA   Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
RA   Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector
RT   coding capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KI964161; EUC40485.1; -; Genomic_DNA.
DR   RefSeq; XP_007692991.1; XM_007694801.1.
DR   EnsemblFungi; EUC40485; EUC40485; COCMIDRAFT_108688.
DR   GeneID; 19119292; -.
DR   KEGG; bor:COCMIDRAFT_108688; -.
DR   KO; K00031; -.
DR   Proteomes; UP000054032; 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:UP000054032};
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       85    474       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     151    153       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     385    390       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      170    176       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       327    327       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       350    350       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     153    153       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     158    158       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     185    185       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     208    208       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     335    335       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     403    403       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        215    215       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        287    287       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   486 AA;  54211 MW;  2AA8B42665DAEB90 CRC64;
     MRPAIAAPAA IRHASSIAHL SRRQTCAFAT RCLASHSPAT SAQLLSPRRP ATVTARTTPT
     SLYTLAAQHR MASSSPVKKI KVKNPVVELD GDEMTRIIWQ VIKDKFIHPY LDIDLKYYDL
     GLPYRDETDD QVTLDAAEAI KKYSVGVKCA TITPDEQRVE EFKLKKMWLS PNGTIRNHLG
     GTVFRAPIVI PTIPRLVPGW KQPIIIGRHA FGDQYRAKDR VIPGEGTLEM VFTPKGGKPE
     VIKVYDFPAE GGVAQTQYNT TESISGFAHA SFKMALDKKL PLYMSTKNTI LKAYDGKFKD
     VFQEIYDTQY KKDFEAANIW YEHRLIDDMV AQMIKSEGGY VIAMKNYDGD VQSDIVAQGF
     GSLGLMTSTL ITPDGKTFEA EAAHGTVTRH YREHQKGKET STNPIASIFA WTQGLAKRGE
     LDNTPELVVF AETLEKACID TVDVDKIMTK DLALACGKKD RASWVTTNEY LDAVERRLKS
     SLKEKL
//
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