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Database: UniProt
Entry: A0A163F2I1_DIDRA
LinkDB: A0A163F2I1_DIDRA
Original site: A0A163F2I1_DIDRA 
ID   A0A163F2I1_DIDRA        Unreviewed;       518 AA.
AC   A0A163F2I1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN   ORFNames=ST47_g4786 {ECO:0000313|EMBL:KZM24100.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM24100.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM24100.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM24100.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM24100.1}.
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DR   EMBL; JYNV01000176; KZM24100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163F2I1; -.
DR   STRING; 5454.A0A163F2I1; -.
DR   Proteomes; UP000076837; 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   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   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          117..506
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  56892 MW;  6E618044BC7B10AC CRC64;
     MRPPSSPSAA LRTATTASTA TTAAIAATAA TAATAATAAT AATAATASPL TRLPRRPFAT
     RALARPPPAN PARFSHARPS TTARTPAAFL SSTRFGQQLR MASTPASAIK KIKVVNPVVE
     LDGDEMTRII WQTIKDKFIH PYLDIDLKYY DLGLEYRDET NDQVTLDAAE AIQKYSVGVK
     CATITPDEQR VEEFKLKKMW LSPNGTIRNH LGGTVFRAPI VIPRIPRLVP SWKQPIIIGR
     HAFGDQYRAK DRVIDGEGTL EMVFTPKGGE PQTIKVYDFP AGGGVAQTQY NTTESISGFA
     HASMKLALDK KLPLYMSTKN TILKAYDGKF KDVFQDIYDN QYKKDFDAAG IWYEHRLIDD
     MVAQMIKSEG GYIIAMKNYD GDVQSDIVAQ GFGSLGLMTS VLITPDGKTF EAEAAHGTVT
     RHYREHQKGN ETSTNPIASI YAWTQGLSKR GELDNTPELV VFAEQLEKAC VDTVDVDGIM
     TKDLALACGK KDRASWVTTN EYLDAVERRL KTSLKEKL
//
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