ID A6R400_AJECN Unreviewed; 363 AA. AC A6R400; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 90. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108}; DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108}; GN ORFNames=HCAG_04358 {ECO:0000313|EMBL:EDN07848.1}; OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus) OS (Histoplasma capsulatum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma. OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN07848.1, ECO:0000313|Proteomes:UP000009297}; RN [1] {ECO:0000313|Proteomes:UP000009297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297}; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T., RA Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens Coccidioides RT and their relatives."; RL Genome Res. 19:1722-1731(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 Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRNR:PIRNR000108}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000256|PIRNR:PIRNR000108}; 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; CH476658; EDN07848.1; -; Genomic_DNA. DR AlphaFoldDB; A6R400; -. DR STRING; 339724.A6R400; -. DR VEuPathDB; FungiDB:HCAG_04358; -. DR HOGENOM; CLU_023296_1_1_1; -. DR OMA; HGTVQRH; -. DR OrthoDB; 423at2759; -. DR Proteomes; UP000009297; Unassembled WGS sequence. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; 2. 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; 2. DR PIRSF; PIRSF000108; IDH_NADP; 2. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 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|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-4}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000108}; KW Reference proteome {ECO:0000313|Proteomes:UP000009297}; KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}. FT DOMAIN 13..350 FT /note="Isopropylmalate dehydrogenase-like" FT /evidence="ECO:0000259|SMART:SM01329" FT BINDING 64..66 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 66 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 71 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 83..89 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 98 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 121 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2" FT BINDING 247 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 261..266 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT BINDING 279 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4" FT SITE 128 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" FT SITE 199 FT /note="Critical for catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1" SQ SEQUENCE 363 AA; 41159 MW; D25A8C9FC6A06D0D CRC64; MTGSRRKIKV KNPVVELDGD EMTRIIWQDI KDKGLEYRDQ TNDQVTIDSA EAIKKYGVGV KCATITPDEA RVEEFKLKQM WLSPNGTIRN ILGGTVFREP IVIPRIPRLV PGWKKPIIIG RHAFGDQYRA KDLVVPGPGT LELVYTPKGG QPEHIKVFDF EGGGVAMSQY NTDDSIAGFA HASFKLALLK EMPLYMSTKN TILKKYDGRF KDIFQEIFEA NYKKDFDAKG IWYEHRLIDD MVAQMIKSDG GFVIAMKTAH GTVTRHYREY QKGNETSTNP IASIFAWTRG LIRRGQLDNT PDVVVWAEQL ERACIDVVDE DGVMTKDLAL ACGRKDRAAW VTTREYLEAV ERRLQKNLAN AKL //