ID A0A0G4M5R2_9PEZI Unreviewed; 376 AA.
AC A0A0G4M5R2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BN1708_005023 {ECO:0000313|EMBL:CRK29606.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK29606.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK29606.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK29606.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQH01021195; CRK29606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4M5R2; -.
DR STRING; 100787.A0A0G4M5R2; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000044602; 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:UP000044602};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 53..372
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 376 AA; 40325 MW; EA1ED7EBA8861F6E CRC64;
MLAARAFSAP IGRQSLRVAP RAAGVVAFQR FYSAQGDRVA KFNGVKDASG KYPVSLIEGD
GIGPEISDAV KNIFAAAKPI DVTPILKDGK TAIPDAAIES IKRNKIALKG PLATPIGKGH
VSLNLTLRRT FNLFANLRPC RSIAGYKTPY DGVDTVLIRE NTEGEYSGIE HVVVDGVVQS
IKLITREASE RVLRYAFQHA ESIGRKKVRV VHKATIMKMS DGLFLNVARE VAKDFPNIEF
DAELLDNSCL KMVTDPLPYN DKVLVMPNLY GDILSDMCAG LIGGLGLTPS GNIGDECSIF
EAVHGSAPDI AGQGLANPTA LLLSSMMMLR HMNLTEYADR IEKAAFATLA EGKALTGDLG
GKAKTHEFAS AIISKL
//
