IDH3G_PIG
ID IDH3G_PIG Reviewed; 106 AA.
AC P41566;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 94.
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: Fragments;
GN Name=IDH3G;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=2252888; DOI=10.1021/bi00488a010;
RA Huang Y.C., Colman R.F.;
RT "Subunit location and sequences of the cysteinyl peptides of pig heart NAD-
RT dependent isocitrate dehydrogenase.";
RL Biochemistry 29:8266-8273(1990).
RN [2]
RP PROTEIN SEQUENCE OF 40-62.
RC TISSUE=Heart;
RX PubMed=2605193; DOI=10.1021/bi00447a023;
RA Saha A., Huang Y.C., Colman R.F.;
RT "Cysteinyl peptide labeled by 3-bromo-2-ketoglutarate in the active site of
RT pig heart NAD+-dependent isocitrate dehydrogenase.";
RL Biochemistry 28:8425-8431(1989).
RN [3]
RP PROTEIN SEQUENCE OF 76-86.
RC TISSUE=Heart;
RX PubMed=2745437; DOI=10.1016/s0021-9258(18)63842-6;
RA Huang Y.C., Colman R.F.;
RT "Aspartyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-
RT diphosphate in the allosteric ADP site of pig heart NAD+-dependent
RT isocitrate dehydrogenase.";
RL J. Biol. Chem. 264:12208-12214(1989).
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 -!- 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.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR PIR; C35834; C35834.
DR STRING; 9823.ENSSSCP00000013592; -.
DR PaxDb; P41566; -.
DR PeptideAtlas; P41566; -.
DR eggNOG; KOG0784; Eukaryota.
DR InParanoid; P41566; -.
DR SABIO-RK; P41566; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IMP:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0006102; P:isocitrate metabolic process; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Mitochondrion; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..>106
FT /note="Isocitrate dehydrogenase [NAD] subunit gamma,
FT mitochondrial"
FT /id="PRO_0000083592"
FT NON_CONS 62..63
FT /evidence="ECO:0000305"
FT NON_CONS 75..76
FT /evidence="ECO:0000305"
FT NON_CONS 86..87
FT /evidence="ECO:0000305"
FT NON_TER 106
SQ SEQUENCE 106 AA; 11334 MW; AB0A66AB845C49AB CRC64;
FSQQTIPPSA KYGGILTVTM SPGDGDGPEL MLTVXXXXXS ACVPVDFEEV VVSSNADEED
IRTSLDLYAN VIHCKLGDGL FLQCCKNIAN PTATLLASCM MLDHLK
