ID C7YSA6_FUSV7 Unreviewed; 466 AA. AC C7YSA6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN ORFNames=NECHADRAFT_100651 {ECO:0000313|EMBL:EEU45600.1}; OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL OS 45880 / 77-13-4) (Fusarium solani subsp. pisi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium solani species complex; Fusarium vanettenii. OX NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU45600.1, ECO:0000313|Proteomes:UP000005206}; RN [1] {ECO:0000313|EMBL:EEU45600.1, ECO:0000313|Proteomes:UP000005206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4 RC {ECO:0000313|Proteomes:UP000005206}; RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618; RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C., RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C., RA Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M., RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M., RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L., RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E., RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E., RA Vanetten H.D.; RT "The genome of Nectria haematococca: contribution of supernumerary RT chromosomes to gene expansion."; RL PLoS Genet. 5:E1000618-E1000618(2009). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; CC Evidence={ECO:0000256|ARBA:ARBA00023554, CC 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769, CC ECO:0000256|PIRNR:PIRNR000108}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG698899; EEU45600.1; -; Genomic_DNA. DR RefSeq; XP_003051313.1; XM_003051267.1. DR AlphaFoldDB; C7YSA6; -. DR STRING; 660122.C7YSA6; -. DR EnsemblFungi; NechaT100651; NechaP100651; NechaG100651. DR GeneID; 9666174; -. DR KEGG; nhe:NECHADRAFT_100651; -. DR VEuPathDB; FungiDB:NECHADRAFT_100651; -. DR eggNOG; KOG1526; Eukaryota. DR HOGENOM; CLU_023296_1_1_1; -. DR InParanoid; C7YSA6; -. DR OMA; HGTVQRH; -. DR OrthoDB; 423at2759; -. DR Proteomes; UP000005206; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00127; nadp_idh_euk; 1. DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1. DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 3: Inferred from homology; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000108}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000108}; KW Reference proteome {ECO:0000313|Proteomes:UP000005206}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT DOMAIN 65..454 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 131..133 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 133 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 138 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 150..156 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 165 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 188 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 307 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 315 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 330 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3" FT BINDING 365..370 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 383 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT SITE 195 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" FT SITE 267 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" SQ SEQUENCE 466 AA; 52027 MW; A7923FEAA03157C7 CRC64; MPAVAFASAV PRSLLSSSLR RVAFASSSPI AVRPIRASFG AVQTISPFAV RTMASAIPKI KVKNPVVELD GDEMTRIIWQ SIKDKFIYPY LDIDLKYYDL GLEYRDETND QVTIDAAEAI KKYQVGVKCA TITPDEARVE EFKLKQMWLS PNGTIRNALG GTVFREPIVI PRIPRLVPGW KKPIIIGRHA FGDQYRAKDA VLPGPGKLSM VYTPEGGEPQ EIEVYQFKNG GGVAQTQYNT DESITGFAHA SFKLALDKGL PLYMSTKNTI LKKYDGRFKD IFQELYDTQY KPEFEAKKIW YEHRLIDDMV AQMVKSSGGY IMALKNYDGD VQSDIVAQGF GSLGLMTSVL ITPDGKTFES EAAHGTVTRH YREHQKGNET STNPIASIFA WTRGLIQRGK LDDQPEVVSF AESLEQACID TVDIDGVMTK DLALACGKTG REDYVTTTEY LNAVERRMKN ILKEKL //