ID S9WIC8_9TRYP Unreviewed; 419 AA.
AC S9WIC8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN ORFNames=ADEAN_000286300 {ECO:0000313|EMBL:CAD2215408.1};
OS Angomonas deanei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Angomonas.
OX NCBI_TaxID=59799 {ECO:0000313|EMBL:CAD2215408.1, ECO:0000313|Proteomes:UP000515908};
RN [1] {ECO:0000313|EMBL:CAD2215408.1, ECO:0000313|Proteomes:UP000515908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Crithidia deanei Carvalho (ATCC PRA-265)
RC {ECO:0000313|Proteomes:UP000515908};
RA Newling K., Davey J., Forrester S.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; LR877149; CAD2215408.1; -; Genomic_DNA.
DR AlphaFoldDB; S9WIC8; -.
DR EnsemblProtists; EPY39061; EPY39061; AGDE_04868.
DR EnsemblProtists; EPY41085; EPY41085; AGDE_02840.
DR VEuPathDB; TriTrypDB:ADEAN_000286300; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000515908; Chromosome 05.
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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000515908};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 19..415
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT COILED 251..280
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 419 AA; 45498 MW; 6D466C8B14EC4B67 CRC64;
MGDIIRIQDG KLIVPDEVII PFIEGDGVGK EISLETQKII DAAVAKAYPN RKIHWREVLA
GEKGQAQCGS YLPDETLEVL RSHLVSIKGP LGTPVGGGMR SINVTLRQTL DLYVCQRPVR
HFRGVSSPVL HPEQVDMVVF RENTEDIYSG IEWQQGTPEA EKFYRFLSEE MGVTKVRFPT
TSAFGVKPVS IEGTERLVRA AIEHALAHQL PSVTLVHKGN IMKFTEGGFR NWGYALAERE
FGDKTFCWTT YEAVKKEKGK AEAEKLLAEA KANKKLIIKD CIADAFLQNI LLKPKDYSVV
ATLNLNGDYV SDALAAMVGG IGIAPGANIN YQTGHALFEA THGTAPDIAG EGKANPTSLL
LSAVMLCDYL GWTKVGEAVF GALEKCFGEG KATADLSSQM ANGTPLSTSA FAQAVIDNL
//
