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   03-AUG-2022, entry version 144.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial;
DE   AltName: Full=Isocitric dehydrogenase subunit beta;
DE   AltName: Full=NAD(+)-isocitrate dehydrogenase subunit 1;
DE            Short=IDH1;
DE   AltName: Full=NAD(+)-specific ICDH subunit beta;
DE   Flags: Precursor;
GN   Name=IDH3B;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   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 and
RT   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   -!- FUNCTION: Plays a structural role to facilitate the assembly and ensure
CC       the full activity of the enzyme catalyzing the decarboxylation of
CC       isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of
CC       the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer
CC       composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have
CC       considerable basal activity but the full activity of the heterotetramer
CC       (containing two subunits of IDH3A, one of IDH3B and one of IDH3G)
CC       requires the assembly and cooperative function of both heterodimers.
CC       {ECO:0000250|UniProtKB:O43837}.
CC   -!- ACTIVITY REGULATION: The heterotetramer and the heterodimer composed of
CC       IDH3A and IDH3G subunits can be allosterically activated by citrate
CC       (CIT) or/and ADP, and the two activators can act independently or
CC       synergistically. The heterodimer composed of IDH3A and IDH3B subunits
CC       cannot be allosterically regulated and the allosteric regulation of the
CC       heterotetramer is through the IDH3G subunit and not the IDH3B subunit.
CC       The IDH3G subunit contains the allosteric site which consists of a CIT-
CC       binding site and an ADP-binding site, and the binding of CIT and ADP
CC       causes conformational changes at the allosteric site which are
CC       transmitted to the active site in the catalytic subunit (IDH3A) through
CC       a cascade of conformational changes at the heterodimer interface,
CC       leading to stabilization of the isocitrate-binding at the active site
CC       and thus activation of the enzyme. ATP can activate the heterotetramer
CC       and the heterodimer composed of IDH3A and IDH3G subunits at low
CC       concentrations but inhibits their activities at high concentrations,
CC       whereas ATP exhibits only inhibitory effect on the heterodimer composed
CC       of IDH3A and IDH3B subunits. {ECO:0000250|UniProtKB:O43837}.
CC   -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC       gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC       containing one IDH3A and one IDH3B subunit and the heterodimer
CC       containing one IDH3A and one IDH3G subunit assemble into a
CC       heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC       one of IDH3G) and further into the heterooctamer.
CC       {ECO:0000250|UniProtKB:O43837}.
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 and
CC       liver.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AF090321; AAC83166.1; -; mRNA.
DR   EMBL; AF090322; AAC83167.1; -; mRNA.
DR   EMBL; BC104502; AAI04503.1; -; mRNA.
DR   PIR; S58432; S58432.
DR   RefSeq; NP_001139344.1; NM_001145872.1. [O77784-1]
DR   RefSeq; NP_001161346.1; NM_001167874.1. [O77784-2]
DR   AlphaFoldDB; O77784; -.
DR   SMR; O77784; -.
DR   BioGRID; 541068; 1.
DR   STRING; 9913.ENSBTAP00000025044; -.
DR   PaxDb; O77784; -.
DR   PRIDE; O77784; -.
DR   Ensembl; ENSBTAT00000025044; ENSBTAP00000025044; ENSBTAG00000018813. [O77784-1]
DR   Ensembl; ENSBTAT00000045446; ENSBTAP00000042833; ENSBTAG00000018813. [O77784-1]
DR   GeneID; 613338; -.
DR   KEGG; bta:613338; -.
DR   CTD; 3420; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018813; -.
DR   eggNOG; KOG0784; Eukaryota.
DR   GeneTree; ENSGT00950000182989; -.
DR   HOGENOM; CLU_031953_0_1_1; -.
DR   InParanoid; O77784; -.
DR   OMA; TCAHKAN; -.
DR   OrthoDB; 868374at2759; -.
DR   TreeFam; TF315033; -.
DR   SABIO-RK; O77784; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000018813; Expressed in corpus luteum and 104 other tissues.
DR   GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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   Acetylation; Alternative splicing; Mitochondrion; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           34..385
FT                   /note="Isocitrate dehydrogenase [NAD] subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000014443"
FT   MOD_RES         199
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43837"
FT   VAR_SEQ         361..385
FT                   /note="RDMGGYSTTTDFIKSVIGHLHPYGG -> SDMGGYATCQDFTEAVIGALSNP
FT                   (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:10677231"
FT                   /id="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