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   16-JUN-2009, entry version 55.
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 capsulata (Darling's disease fungus) (Histoplasma
OS   capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces.
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>3.3.CO;2-E;
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
RT   mutant of Saccharomyces cerevisiae.";
RL   Yeast 15:799-804(1999).
CC   -!- FUNCTION: Performs an essential role in the oxidative function of
CC       the citric acid cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit.
CC   -!- SUBUNIT: Octamer of two non-identical subunits IDH1 and IDH2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AF009036; AAB63461.1; -; mRNA.
DR   HSSP; P08200; 1ISO.
DR   BRENDA; 1.1.1.41; 266116.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD_mit.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; 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;
KW   Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     35       Mitochondrion (Potential).
FT   CHAIN        36    388       Isocitrate dehydrogenase [NAD] subunit 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000014428.
FT   METAL       255    255       Magnesium or manganese (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     168    168       Substrate (By similarity).
FT   BINDING     255    255       Substrate (By similarity).
FT   SITE        175    175       Critical for catalysis (By similarity).
FT   SITE        222    222       Critical for catalysis (By similarity).
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
//