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Database: UniProt/TrEMBL
Entry: B8N000_ASPFN
LinkDB: B8N000_ASPFN
Original site: B8N000_ASPFN 
ID   B8N000_ASPFN            Unreviewed;       499 AA.
AC   B8N000;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-JUL-2017, entry version 55.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=AFLA_086400 {ECO:0000313|EMBL:EED57942.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM
OS   12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED57942.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED57942.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167
RC   {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963472; EED57942.1; -; Genomic_DNA.
DR   RefSeq; XP_002373554.1; XM_002373513.1.
DR   STRING; 5059.CADAFLAP00001419; -.
DR   PRIDE; B8N000; -.
DR   EnsemblFungi; EED57942; EED57942; AFLA_086400.
DR   GeneID; 7909786; -.
DR   KEGG; afv:AFLA_086400; -.
DR   EuPathDB; FungiDB:AFLA_086400; -.
DR   HOGENOM; HOG000019858; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000001875; 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:UP000001875};
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:UP000001875};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       99    487       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     165    167       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     398    403       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      184    190       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       340    340       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       363    363       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     167    167       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     172    172       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     199    199       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     222    222       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     348    348       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     416    416       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        229    229       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        300    300       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   499 AA;  55826 MW;  19D7C2C137E10B00 CRC64;
     MMNSLRLHSA SVRRAVASPL SAPLSSSAYR SISCTSSSYI SSSSSSSFST AATPRAQRPL
     ASSQLPRIVS PRQTGIYPLQ WTQARTMATE GPKIKVKNPV VELDGDEMTR IIWQEIREKL
     ILPYLDIDLK YYDLGLEYRD QTDDQVTVEA AEAIKKYGVG VKCATITPDE ARVEEFKLKK
     MWLSPNGTIR NILGGTVFRE PIIIPRVPRL VPGWTKPIII GRHAFGDQYR ATDRVIPGPG
     KLELVYTPVN GEPETVKVYD FQGGGVTQTQ YNTDESIQGF AHASFQMALL KGLPLYMSTK
     NTILKKYDGR FKDIFQEIYE STYKKDFEAK NIWYEHRLID DMVAQMIKSE GGFVMALKNY
     DGDVQSDIVA QGFGSLGLMT STLTTPSGEA FESEAAHGTV TRHYREHQKG RETSTNPIAS
     IFAWTRGLVQ RGKLDETPDV VAFAEELERA CIEVVNDEGI MTKDLALACG RKDRDAWVTT
     KEYMAAVERK LKTNLKSRL
//
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