GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0D2XM79_FUSO4
LinkDB: A0A0D2XM79_FUSO4
Original site: A0A0D2XM79_FUSO4 
ID   A0A0D2XM79_FUSO4        Unreviewed;       462 AA.
AC   A0A0D2XM79;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=FOXG_05055 {ECO:0000313|EMBL:KNB01983.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC
OS   9935 / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EnsemblFungi:FOXG_05055P0, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNB01983.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB01983.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J.,
RA   Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E., Brockman W., MacCallum I.A., Young S., LaButti K.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Larson L., White J., O'Leary S., Kodira C.,
RA   Zeng Q., Yandava C., Alvarado L., Kistler C., Shim W.-B., Kang S.,
RA   Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNB01983.1, ECO:0000313|EnsemblFungi:FOXG_05055P0, ECO:0000313|Proteomes:UP000009097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB01983.1}, and 4287 / CBS 123668 /
RC   FGSC 9935 / NRRL 34936 {ECO:0000313|EnsemblFungi:FOXG_05055P0,
RC   ECO:0000313|Proteomes:UP000009097};
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J.,
RA   Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M.,
RA   Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C.,
RA   Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A.,
RA   Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M.,
RA   Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S.,
RA   Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K.,
RA   Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M.,
RA   Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y.,
RA   Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S.,
RA   Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O.,
RA   Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C.,
RA   Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3] {ECO:0000313|EnsemblFungi:FOXG_05055P0}
RP   IDENTIFICATION.
RC   STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC   {ECO:0000313|EnsemblFungi:FOXG_05055P0};
RG   EnsemblFungi;
RL   Submitted (MAR-2015) to UniProtKB.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DS231700; KNB01983.1; -; Genomic_DNA.
DR   EMBL; DS231700; KNB01984.1; -; Genomic_DNA.
DR   EMBL; DS231700; KNB01985.1; -; Genomic_DNA.
DR   RefSeq; XP_018240028.1; XM_018383146.1.
DR   RefSeq; XP_018240029.1; XM_018383147.1.
DR   RefSeq; XP_018240030.1; XM_018383148.1.
DR   STRING; 5507.FOXG_05055P0; -.
DR   EnsemblFungi; FOXG_05055T0; FOXG_05055P0; FOXG_05055.
DR   GeneID; 28947058; -.
DR   KEGG; fox:FOXG_05055; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   Proteomes; UP000009097; Chromosome 7.
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:UP000009097};
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:UP000009097};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       61    450       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     127    129       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     361    366       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      146    152       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       303    303       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       326    326       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     129    129       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     134    134       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     161    161       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     184    184       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     311    311       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     379    379       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        191    191       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        263    263       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   462 AA;  51772 MW;  57D569141C901C21 CRC64;
     MPAAVFASSI QRSLLSSSLR RVAITSSAVR PVRASFGAIQ TISPFAVRTM ASHQKIKVKN
     PVVELDGDEM TRIIWQVIKD KLILPYLDID LKYYDLGLEY RDETNDQVTI DAAEAIKKYS
     VGVKCATITP DEARVEEFKL KQMWLSPNGT IRNALGGTVF REPIVIPRIP RLVPGWKKPI
     IIGRHAFGDQ YRAKDAVLPG PGKLSMVYTP EGGQPQEIEV FQFKNGGGVA QTQYNTDESI
     TGFAHASFKL ALDKELPLYM STKNTILKKY DGRFKDIFQE IYESTYKKDF EAKKIWYEHR
     LIDDMVAQMI KSSGGYIMAL KNYDGDVQSD IVAQGFGSLG LMTSVLITPD GKTFESEAAH
     GTVTRHYREH QKGNETSTNP IASIFAWTRG LVQRGKLDDT PEVVAFAESL EQACIDTVDI
     DGIMTKDLAL ATGKSERKDY VTTNEYMDAV ERRLKRTLKE KL
//
DBGET integrated database retrieval system