ID A0A0D1XAF9_9PEZI Unreviewed; 381 AA.
AC A0A0D1XAF9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=PV09_09133 {ECO:0000313|EMBL:KIV99180.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99180.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV99180.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99180.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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 -!- 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; KN847582; KIV99180.1; -; Genomic_DNA.
DR RefSeq; XP_016209050.1; XM_016363130.1.
DR AlphaFoldDB; A0A0D1XAF9; -.
DR STRING; 253628.A0A0D1XAF9; -.
DR GeneID; 27317106; -.
DR VEuPathDB; FungiDB:PV09_09133; -.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; A0A0D1XAF9; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000053259; 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:SF42; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT GAMMA, 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 Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 47..374
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 381 AA; 41516 MW; CDC6E399B234CB60 CRC64;
MLPVQRTMLA ARALSKASRP AAVAAARSYA TVQSDIFKPT KFGGKYTATL IPGDGIGAEV
TEAVKAIFKA DNVPIEWEQV DVSGVETGDK NSEQLFREAI ASLKRNKLGL KGILYTPLER
SGHQSFNVAL RQELDIYASI VLIKNIPGYE TRHKNVDLCI IRENTEGEYS GLEHQSVAGV
VESLKIITRA KSERIAKFAF AFALANNRKK VTCIHKANIM KLADGLFRNT FKKVAEEYPT
LEANDMIVDN ASMQCVSRPQ QFDVMVMPNL YGGILSNIGA GLVGGPGIVP GCNIGRDIAV
FEPGCRHVGL DIKGKDQANP SALLLSASMM LRHVGLDDHA NRISKAVYDV IADGKVRTRD
MGGNATTHEF TRAILDQMEK Q
//
