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Database: UniProt
Entry: A0A061HMA4_BLUGR
LinkDB: A0A061HMA4_BLUGR
Original site: A0A061HMA4_BLUGR 
ID   A0A061HMA4_BLUGR        Unreviewed;       403 AA.
AC   A0A061HMA4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=isocitrate dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00013012};
DE            EC=1.1.1.41 {ECO:0000256|ARBA:ARBA00013012};
DE   AltName: Full=Isocitric dehydrogenase {ECO:0000256|ARBA:ARBA00030683};
DE   AltName: Full=NAD(+)-specific ICDH {ECO:0000256|ARBA:ARBA00030631};
GN   ORFNames=BGT96224_1191 {ECO:0000313|EMBL:EPQ66890.1},
GN   BGT96224V2_LOCUS1242 {ECO:0000313|EMBL:SUZ08084.1};
OS   Blumeria graminis f. sp. tritici 96224.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria.
OX   NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ08084.1};
RN   [1] {ECO:0000313|Proteomes:UP000053110}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX   PubMed=23852167; DOI=10.1038/ng.2704;
RA   Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA   Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA   Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA   Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT   "The wheat powdery mildew genome shows the unique evolution of an obligate
RT   biotroph.";
RL   Nat. Genet. 45:1092-1096(2013).
RN   [2] {ECO:0000313|EMBL:EPQ66890.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=96224 {ECO:0000313|EMBL:EPQ66890.1};
RA   Oberhaensli S., Wicker T., Keller B.;
RT   "The wheat powdery mildew genome reveals unique evolution of an obligate
RT   biotroph.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SUZ08084.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=96224 {ECO:0000313|EMBL:SUZ08084.1};
RA   Quirk P.G., Krulwich T.A.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC         Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00000837};
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   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2.
CC       {ECO:0000256|ARBA:ARBA00011567}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; KE374664; EPQ66890.1; -; Genomic_DNA.
DR   EMBL; UIGY01000009; SUZ08084.1; -; Genomic_DNA.
DR   HOGENOM; CLU_031953_0_1_1; -.
DR   OrthoDB; 143577at2759; -.
DR   Proteomes; UP000053110; Unassembled WGS sequence.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) 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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00175; mito_nad_idh; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053110};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          74..399
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   403 AA;  43569 MW;  411D5B28B633B8FF CRC64;
     MISVATPTGR LCLLAKSQAT KRFALQASKR RSAENTLRSI TSLSQSGRSY SGNSSPIGKI
     ASFYGQKDSE GCYTASLIEG DGIGPEISRS VIDIFKAAKA PIKWEPVDVT PQLKDGKTTI
     LPETIKSIEK NKVALKGPLA TPIGKGHVSL NLTLRRTFNL FANVRPCRSI AGYKTPYDGV
     ETVIIRENTE GEYSGIEHVV VDGVVQSIKL ITREASERVL RFAFLYAQNI GKPKVRVVHK
     ATIMKMSDGL FLATAERVSK DFPDIEFDAE LLDNTCLKIV TDPVPYNDKV LVMPNLYGDI
     LSDMCSGLIG GLGLTPSGNI GDSCSIFEAV HGSAPDIAGK GLANPTALLL SSVMMLRHMQ
     LNEHALKIEN AIFDTLKEGK SLTGDLGGKA KTHEFAEAIM KRL
//
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