ID A0A094G3G2_9PEZI Unreviewed; 385 AA.
AC A0A094G3G2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=V498_01953 {ECO:0000313|EMBL:KFY97649.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY97649.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY97649.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY97649.1}.
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DR EMBL; JPKA01000289; KFY97649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094G3G2; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR Proteomes; UP000029270; 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 Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 56..381
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 385 AA; 41593 MW; EFBB6A89689884B6 CRC64;
MLAIRSIAAP ARRQCLRANG VAMLSSLQTR TYAAGASTHD KVAKFHGKKG SDGLYTVSLI
EGDGIGPEIA QSVKDIFKAA NTPIKWEPVD VTPQLKDGKT VIPDETIESI ERNKVALKGP
LATPIGKGHV SLNLTLRRTF NLFANVRPCR SIAGFKTPYD GVDTVLIREN TEGEYSGIEH
VVIDGVVQSI KLITREASER VCKYAFQYAE EIGKLKVRAV HKATIMKMSD GLFLSTAQRV
AKDFPKVEFD AELIDNTCLK IVTDPTPYND KVLVMPNLYG DILSDTCAGL IGGLGLTPSA
NIGDECSIFE AVHGSAPDIA GKALANPTAL LLSSIMMLRH MGLEEQAVRI EKAIFETLAE
GKYLTGDLHG TAKTHEYAGA IISRL
//
