ID   IDH3B_BOVIN             Reviewed;         385 AA.
AC   O77784; O77785; Q3MI01;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase;
DE   AltName: Full=NAD(+)-specific ICDH;
DE   AltName: Full=NAD(+)-isocitrate dehydrogenase subunit 1;
DE            Short=IDH1;
DE   Flags: Precursor;
GN   Name=IDH3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX   PubMed=10677231; DOI=10.1021/bi991691i;
RA   Weiss C., Zeng Y., Huang J., Sobocka M.B., Rushbrook J.I.;
RT   "Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing
RT   and tissue-dependent expression of subunit 1.";
RL   Biochemistry 39:1807-1816(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-385 (ISOFORM B).
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the
CC       apparent ratio of 2:1:1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=O77784-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=O77784-2; Sequence=VSP_002461;
CC   -!- TISSUE SPECIFICITY: Isoform A is predominant in heart muscle; also
CC       found in brain, kidney and liver. Isoform B is present in kidney
CC       and liver.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AF090321; AAC83166.1; -; mRNA.
DR   EMBL; AF090322; AAC83167.1; -; mRNA.
DR   EMBL; BC104502; AAI04503.1; -; mRNA.
DR   IPI; IPI00705072; -.
DR   IPI; IPI00708762; -.
DR   PIR; S58432; S58432.
DR   RefSeq; XP_869155.1; -.
DR   UniGene; Bt.13324; -.
DR   UniGene; Bt.56156; -.
DR   HSSP; P39126; 1HQS.
DR   Ensembl; ENSBTAG00000018813; Bos taurus.
DR   GeneID; 613338; -.
DR   KEGG; bta:613338; -.
DR   HOVERGEN; O77784; -.
DR   OMA; O77784; TTTDFIK.
DR   BRENDA; 1.1.1.41; 251.
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   Alternative splicing; Magnesium; Manganese; Metal-binding;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     33       Mitochondrion (By similarity).
FT   CHAIN        34    385       Isocitrate dehydrogenase [NAD] subunit
FT                                beta, mitochondrial.
FT                                /FTId=PRO_0000014443.
FT   METAL       251    251       Magnesium or manganese (By similarity).
FT   BINDING     133    133       Substrate (By similarity).
FT   BINDING     164    164       Substrate (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
FT   SITE        171    171       Critical for catalysis (By similarity).
FT   SITE        218    218       Critical for catalysis (By similarity).
FT   VAR_SEQ     361    385       RDMGGYSTTTDFIKSVIGHLHPYGG -> SDMGGYATCQDF
FT                                TEAVIGALSNP (in isoform A).
FT                                /FTId=VSP_002461.
SQ   SEQUENCE   385 AA;  42497 MW;  8E974AD550F5D50D CRC64;
     MAALSRVRWL TRALVAAPNP GAWRSLCTST VAQASSRTQG EDVRVEGAFP VTMLPGDGVG
     PELMHAVKEV FKAASVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME
     YKGELASYDM RLRRKLDLFA NVVHVKSLPG YKTRHNNLDL VIIREQTEGE YSSLEHESAR
     GVIECLKIVT RTKSQRIAKF AFDYATKKGR GKVTAVHKAN IMKLGDGLFL QCCEEVAELY
     PKIKFEKMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY
     AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEH HSNMIAEAVK KVIKVGKVRT
     RDMGGYSTTT DFIKSVIGHL HPYGG
//