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Database: UniProt
Entry: A0A1G4JEA1_9SACH
LinkDB: A0A1G4JEA1_9SACH
Original site: A0A1G4JEA1_9SACH 
ID   A0A1G4JEA1_9SACH        Unreviewed;       361 AA.
AC   A0A1G4JEA1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-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=LADA_0E10814G {ECO:0000313|EMBL:SCU88549.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU88549.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Devillers H.;
RL   Submitted (MAR-2016) 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; LT598455; SCU88549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JEA1; -.
DR   STRING; 1266660.A0A1G4JEA1; -.
DR   OrthoDB; 143577at2759; -.
DR   Proteomes; UP000190274; Chromosome E.
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:UP000190274};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          31..354
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   361 AA;  38834 MW;  4E63C26682AC7882 CRC64;
     MFKNGIGMSK RSLASVAAEQ LLPKKYGGRY TVTLIPGDGV GKEVTDSVVS IFDAENVPVD
     WESVEISGLE NQEGVQKAVD SLKRNKIGLK GIWHTPVDQS GFGSLNVALR KQLDIFANVA
     LFKSVPGVQT RHSNVDLVVI RENTEGEYSG LEHESVPGVV ESLKIMTKTK SERIGRFAFD
     FAVKNNRKSV CAVHKANIMK LGDGLFRNCI NEVGAKEYPE IDVKNIIVDN ASMQAAAKPQ
     QFDVLVTPNL YGSILGNIGA ALIGGPGLVP GANFGREYAV FEPGSRHVGL DIKGQNLANP
     TAMILSSTLM LRHLGLNAYA DRISKATYDV IAEGKTTTQD IGGSSSTTDF TNAIIEKLKA
     L
//
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