ID A0A0L6UYJ6_9BASI Unreviewed; 390 AA.
AC A0A0L6UYJ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=VP01_31g5 {ECO:0000313|EMBL:KNZ53569.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ53569.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ53569.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ53569.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-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}.
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:KNZ53569.1}.
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DR EMBL; LAVV01008169; KNZ53569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6UYJ6; -.
DR STRING; 27349.A0A0L6UYJ6; -.
DR VEuPathDB; FungiDB:VP01_31g5; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000037035; 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 Oxidoreductase {ECO:0000313|EMBL:KNZ53569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 60..385
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 390 AA; 42290 MW; 6AFF7387E04BEF9A CRC64;
MIAFSRGLRA SSHSIARGQA QAKSFGTSVS SQLPAIPAAQ PSSAQTGAFK GFKLPNQTYK
VTLIPGDGIG PEISESVKAI YAAAKVPITW EERDVTPVIV DGRSTIPQDA IDSIHQTTVA
LKGPLATPIG KGHVSLNLTL RRTFKLFANV RPCRSIVGFK TPYDDVNSVL IRENTEGEYS
GIEHEVVDGV VQSIKLITMD ASERVARYAF QYARLNKRPH VTAVHKASIM KMSDGMFLQA
CRRVKEDFPD IKYDEDILDR VCLRIVQNPA PYSDRVMVMP NLYGDILSDM CAGLIGGLGL
TPSGNIGRDA SIFEAVHGSA PDIAGQGKAN PTALLLSSLM MLRHMNLPQY ADRIEKATLE
TIAEGKHITG DLGGKASTQQ YTEAILKRLK
//