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Database: UniProt/TrEMBL
Entry: M2N1P3_BAUCO
LinkDB: M2N1P3_BAUCO
Original site: M2N1P3_BAUCO 
ID   M2N1P3_BAUCO            Unreviewed;       414 AA.
AC   M2N1P3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   07-JUN-2017, entry version 21.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=BAUCODRAFT_78276 {ECO:0000313|EMBL:EMC92550.1};
OS   Baudoinia compniacensis (strain UAMH 10762) (Angels' share fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Teratosphaeriaceae;
OC   Baudoinia.
OX   NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC92550.1, ECO:0000313|Proteomes:UP000011761};
RN   [1] {ECO:0000313|EMBL:EMC92550.1, ECO:0000313|Proteomes:UP000011761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC92550.1,
RC   ECO:0000313|Proteomes:UP000011761};
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).
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; KB445562; EMC92550.1; -; Genomic_DNA.
DR   RefSeq; XP_007680504.1; XM_007682314.1.
DR   EnsemblFungi; EMC92550; EMC92550; BAUCODRAFT_78276.
DR   GeneID; 19117160; -.
DR   KEGG; bcom:BAUCODRAFT_78276; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000011761; 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:UP000011761};
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:UP000011761};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       13    402       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      79     81       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     315    320       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       98    104       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       257    257       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       280    280       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      81     81       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      86     86       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     113    113       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     136    136       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     265    265       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     333    333       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        143    143       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        217    217       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   414 AA;  46609 MW;  E9844A5A21BEBCFC CRC64;
     MATSIPKIKV KNPVVELDGD EMTRIIWQDI KDKFIHPYLD IDLKYYDLGL PYRDETNDQV
     TIDAAEAIKK YSVGVKCATI TPDEARVEEF KLKQMWLSPN GTLRNALGGT VFREPIVIPK
     IPRLVPGWKK PIVIGRHAFG DQYRAKDRVI DGPGTLEMVF TPKGGQPERI KVFEFDEHHQ
     GGVAQTQYNT AESITGFAHA SFKHALSLKY PMYMTTKNTI LKKYDGRFKD IFQDIYEKEY
     RKDFEAAGIW YEHRLIDDMV AQMIKSEGGM VIAMKNYDGD VQSDIVAQGF GSLGLMTSVL
     ITPDGKTFEA EAAHGTVTRH FREHQKGNPT STNPIASIFA WTRGLAKRGE LDGTPEVVKF
     AESLEEACIH VVDQQGIMTK DLAISCGKKD DYVTTTEYLD AVEKRMKAVL SAKL
//
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