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Database: UniProt/TrEMBL
Entry: M2TN57_COCSN
LinkDB: M2TN57_COCSN
Original site: M2TN57_COCSN 
ID   M2TN57_COCSN            Unreviewed;       486 AA.
AC   M2TN57;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   07-JUN-2017, entry version 23.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=COCSADRAFT_132669 {ECO:0000313|EMBL:EMD70117.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot
OS   and spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD70117.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD70117.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
RA   Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
RA   Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
RA   Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
RA   Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
RA   de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in
RT   the genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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; KB445637; EMD70117.1; -; Genomic_DNA.
DR   RefSeq; XP_007695249.1; XM_007697059.1.
DR   EnsemblFungi; EMD70117; EMD70117; COCSADRAFT_132669.
DR   GeneID; 19130860; -.
DR   KEGG; bsc:COCSADRAFT_132669; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000016934; 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:UP000016934};
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:UP000016934};
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;  54249 MW;  575A52AE622E915E CRC64;
     MKPAVAASAT IRHASSIAHL SRRQTCAFAT RCLASHSPAT SAQLLSPRRP ATITARTTPT
     SLYTLVAQHR MASSSPVKKI KVKNPVVELD GDEMTRIIWQ VIKDKFIHPY LDIDLKYYDL
     GLPYRDETDD QVTLDAAEAI KKYSVGVKCA TITPDEQRVE EFKLKKMWLS PNGTIRNHLG
     GTVFRAPIVI PTIPRLVPGW KQPIIIGRHA FGDQYRAKDR VIPGEGTLEM VFTPKGGKPE
     VIKVYDFPAE GGVAQTQYNT TESISGFAHA SFKMALDKKM 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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