ID   IDH1_AJECA              Reviewed;         388 AA.
AC   O13302;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase;
DE   AltName: Full=NAD(+)-specific ICDH;
DE   Flags: Precursor;
GN   Name=IDH1;
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 26032 / G217B;
RX   PubMed=10398348;
RX   DOI=10.1002/(sici)1097-0061(19990630)15:9<799::aid-yea419>3.0.co;2-n;
RA   Johnson C.H., McEwen J.E.;
RT   "Isolation of a Histoplasma capsulatum cDNA that complements a
RT   mitochondrial NAD(+)-isocitrate dehydrogenase subunit I-deficient mutant of
RT   Saccharomyces cerevisiae.";
RL   Yeast 15:799-804(1999).
CC   -!- FUNCTION: Performs an essential role in the oxidative function of the
CC       citric acid cycle. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
CC   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AF009036; AAB63461.1; -; mRNA.
DR   AlphaFoldDB; O13302; -.
DR   SMR; O13302; -.
DR   PRIDE; O13302; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   2: Evidence at transcript level;
KW   Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..388
FT                   /note="Isocitrate dehydrogenase [NAD] subunit 1,
FT                   mitochondrial"
FT                   /id="PRO_0000014428"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P50213"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            175
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            222
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42222 MW;  7E80888D17CEBEF7 CRC64;
     MFSLRTAQPA QSLFRAATNT YSTSLPRSAI AARSFATVQS DIFKPTKYGG KYTVTLIPGD
     GIGTEVAESV KTIFKADNVP IEWEQVDVSG LDAGNKHSED LFKESIASLK RNKLGLKGIL
     HTPVERSGHQ SFNVALRQEL DIYASIVLIK NIPGYKTRHD NVDLCIIREN TEGEYSGLEH
     QSVSGVVESL KIITRAKSER IAKFAFSFAL ANNRKKVTCI HKANIMKLAD GLFRSTFHKV
     AESYPTLETN DMIVDNASMQ AVARPQQFDV MVMPNLYGGI LSNVGAALVG GPGIVPGCNM
     GRDVAVFEPG CRHVGLDIKG KDQANPTALI LSGSMLLRHL GLDEHANRIS KAVYDVIGEG
     VTRTRDMGGQ ASTHEFTRAV LDKMESAL