IDH3B_PONAB
ID IDH3B_PONAB Reviewed; 385 AA.
AC Q5RBT4; Q5R8E9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial;
DE AltName: Full=Isocitric dehydrogenase subunit beta;
DE AltName: Full=NAD(+)-specific ICDH subunit beta;
DE Flags: Precursor;
GN Name=IDH3B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RBT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RBT4-2; Sequence=VSP_014101;
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; CR858549; CAH90776.1; -; mRNA.
DR EMBL; CR859803; CAH91961.1; -; mRNA.
DR RefSeq; NP_001125436.1; NM_001131964.1.
DR AlphaFoldDB; Q5RBT4; -.
DR SMR; Q5RBT4; -.
DR IntAct; Q5RBT4; 1.
DR MINT; Q5RBT4; -.
DR STRING; 9601.ENSPPYP00000012103; -.
DR GeneID; 100172344; -.
DR KEGG; pon:100172344; -.
DR CTD; 3420; -.
DR eggNOG; KOG0784; Eukaryota.
DR InParanoid; Q5RBT4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IEA:UniProt.
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: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 Acetylation; Alternative splicing; Mitochondrion; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..385
FT /note="Isocitrate dehydrogenase [NAD] subunit beta,
FT mitochondrial"
FT /id="PRO_0000014446"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43837"
FT VAR_SEQ 367..385
FT /note="STTTDFIKSVIGHLHPHGS -> ATCHDFTEAVIAALPHP (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014101"
FT CONFLICT 171
FT /note="C -> Y (in Ref. 1; CAH90776)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="R -> S (in Ref. 1; CAH91961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42166 MW; 6341167AD11A7615 CRC64;
MAAVSGVRWL TRALVSAGNP GAWRGLSTSA AAHAASRSQA EDVRVEGSFP VTMLPGDGVG
PELMHAVKEV FKAAAVPVEF QEHHLSEVQN MASEEKLEQV LSSMKENKVA IIGKIHTPME
YKGELASYDM RLRRKLDLFA NVVHVKSLPG YMTRHNNLDL VIIREQTEGE CSSLEHESAR
GVIECLKIVT RAKSQRIAKF AFDYATKKGR SKVIAVHKAN IMKLGDGLFL QCCEEVAELY
PKIKFETMII DNCCMQLVQN PYQFDVLVMP NLYGNIIDNL AAGLVGGAGV VPGESYSAEY
AVFETGARHP FAQAVGRNIA NPTAMLLSAS NMLRHLNLEY HSSMIADAVK KVIKVGKVRT
RDMGGYSTTT DFIKSVIGHL HPHGS
