ID IDH3G_BOVIN Reviewed; 392 AA.
AC Q58CP0; Q148J3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial;
DE AltName: Full=Isocitric dehydrogenase subunit gamma;
DE AltName: Full=NAD(+)-specific ICDH subunit gamma;
DE Flags: Precursor;
GN Name=IDH3G;
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 [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit which plays a role in the allosteric
CC regulation of the enzyme catalyzing the decarboxylation of isocitrate
CC (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha
CC (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the
CC alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal
CC activity but the full activity of the heterotetramer (containing two
CC subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly
CC and cooperative function of both heterodimers.
CC {ECO:0000250|UniProtKB:P51553}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P51553};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P51553};
CC Note=Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in
CC presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per
CC subunit. {ECO:0000250|UniProtKB:P51553};
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:P51553}.
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:P51553}.
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; BT021907; AAX46754.1; -; mRNA.
DR EMBL; BC118275; AAI18276.1; -; mRNA.
DR RefSeq; NP_001069781.1; NM_001076313.1.
DR AlphaFoldDB; Q58CP0; -.
DR SMR; Q58CP0; -.
DR STRING; 9913.ENSBTAP00000061017; -.
DR PaxDb; 9913-ENSBTAP00000001405; -.
DR GeneID; 614145; -.
DR KEGG; bta:614145; -.
DR CTD; 3421; -.
DR eggNOG; KOG0784; Eukaryota.
DR InParanoid; Q58CP0; -.
DR OrthoDB; 143577at2759; -.
DR TreeFam; TF315033; -.
DR SABIO-RK; Q58CP0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF42; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT GAMMA, MITOCHONDRIAL; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..392
FT /note="Isocitrate dehydrogenase [NAD] subunit gamma,
FT mitochondrial"
FT /id="PRO_0000236185"
FT BINDING 119
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 132
FT /ligand="citrate"
FT /ligand_id="ChEBI:CHEBI:16947"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared with catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 311
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 312
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P51553"
FT BINDING 323
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P51553"
SQ SEQUENCE 392 AA; 42863 MW; 44F749F782E18EFD CRC64;
MALKVATAAG GAVKAALRPA LLWRPWEVLG SHEAPRRSFS QQTIPPSAKY GGRHTVTMIP
GDGIGPELML HVKSVFRHAC VPVDFEEVHV SSTADEEDIR NAIMAIRRNR VALKGNIETN
HNLPPSHKSR NNILRTSLDL YANVIHCKSL PGVVTRHRDI DILIVRENTE GEYSSLEHES
VAGVVESLKI ITKAKSLRIA EYAFQLAQES GRKKVTAVHK ANIMKLGDGL FLQCCREVAA
RYPQITFENM IVDNTTMQLV SRPQQFDVMV MPNLYGNIVN NVCAGLVGGP GLVAGANYGH
VYAVFETATR NTGKSIANKN IANPTATLLA SCMMLDHLKL HSYATSIRKA VLASMDNENM
HTPDIGGQGT TSEAIQDIIR HIRVINGRAV EA
//
