ID   A4UQJ4_TOXGO            Unreviewed;       621 AA.
AC   A4UQJ4;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN   Name=ICDH2 {ECO:0000313|EMBL:ABO93633.1};
OS   Toxoplasma gondii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=5811 {ECO:0000313|EMBL:ABO93633.1};
RN   [1] {ECO:0000313|EMBL:ABO93633.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17784785; DOI=10.1371/journal.ppat.0030115;
RA   Pino P., Foth B.J., Kwok L.Y., Sheiner L., Schepers R., Soldati T.,
RA   Soldati-Favre D.;
RT   "Dual targeting of antioxidant and metabolic enzymes to the mitochondrion
RT   and the apicoplast of Toxoplasma gondii.";
RL   PLoS Pathog. 3:E115-E115(2007).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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DR   EMBL; EF467321; ABO93633.1; -; mRNA.
DR   AlphaFoldDB; A4UQJ4; -.
DR   VEuPathDB; ToxoDB:TGARI_313140; -.
DR   VEuPathDB; ToxoDB:TGCAST_313140; -.
DR   VEuPathDB; ToxoDB:TGCOUG_313140A; -.
DR   VEuPathDB; ToxoDB:TGCOUG_313140B; -.
DR   VEuPathDB; ToxoDB:TGDOM2_313140; -.
DR   VEuPathDB; ToxoDB:TGFOU_313140; -.
DR   VEuPathDB; ToxoDB:TGGT1_313140; -.
DR   VEuPathDB; ToxoDB:TGMAS_313140; -.
DR   VEuPathDB; ToxoDB:TGME49_313140; -.
DR   VEuPathDB; ToxoDB:TGP89_313140A; -.
DR   VEuPathDB; ToxoDB:TGP89_313140B; -.
DR   VEuPathDB; ToxoDB:TGPRC2_313140; -.
DR   VEuPathDB; ToxoDB:TGRH88_052270; -.
DR   VEuPathDB; ToxoDB:TGRUB_313140; -.
DR   VEuPathDB; ToxoDB:TGVAND_313140; -.
DR   VEuPathDB; ToxoDB:TGVEG_313140; -.
DR   HOGENOM; CLU_023296_1_1_1; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   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   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          181..571
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   REGION          602..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68289 MW;  E0EEFA791E3F196D CRC64;
     MRAENSGFSQ KSVRFWTPLE SVQPRTACSF SLCLLWKVCL LSCGVLRTHL RTRSASISRV
     GGAFQTFPTN RPCVFSKKMA SALRRITARA ASPAFPFTSV QSSTFARALS TKSACVRPQL
     LSSALCNTVS STSSSASSGL AVSPVQKSGN PDASPRFFAS AASVATGGAF NLEGKIHVAN
     PVVEMDGDEM TRILWAWIKE KLLFPYVEIP LEYYDLSVTN RDQTEDKVTL EAAEAIKKCH
     VGIKCATITP DEGRVKEFNL KKMWKSPNGT IRNILDGTVF RAPILISNVP RLVPGWKKPI
     VIGRHAYGDQ YKAESLVCDG PGDFTISFTP AGGSRVEKKV FSFSGPGVML GMYNTEDSIR
     GFALSSFKFA LQQNMPLYLS TKNTILKQYD GMFKDIFQSY YDEQFKPLFE KQGIWYEHRL
     IDDMVAQALK SEGGFVWACK NYDGDVQSDI VAQGYGSLGL MTSILVCPDG KTVVSEAAHG
     TVTRHYRQHQ KGQKTSTNPI ASIFAWTRGL AHRAKLDGND RLGQFCLALE HACIQTVENG
     AMPKDLALCV KGADKVTASD YLTTEEFMDA ISDTLKMNLI TRQAPHADQG VGGKLSNSSW
     EHYAASEHNS SVDDHDDNQR R
//