IDHP_BOVIN
ID IDHP_BOVIN Reviewed; 452 AA.
AC Q04467; Q3ZCD4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Isocitrate dehydrogenase [NADP], mitochondrial;
DE Short=IDH;
DE EC=1.1.1.42 {ECO:0000250|UniProtKB:P48735};
DE AltName: Full=ICD-M;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
DE Flags: Precursor;
GN Name=IDH2;
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], AND PROTEIN SEQUENCE OF 40-55.
RC TISSUE=Kidney;
RX PubMed=8318002; DOI=10.1042/bj2920705;
RA Huh T.-L., Ryu J.-H., Huh J.-W., Sung H.-C., Oh I.-U., Song B.J.,
RA Veech R.L.;
RT "Cloning of a cDNA encoding bovine mitochondrial NADP(+)-specific
RT isocitrate dehydrogenase and structural comparison with its isoenzymes from
RT different species.";
RL Biochem. J. 292:705-710(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in intermediary metabolism and energy
CC production. It may tightly associate or interact with the pyruvate
CC dehydrogenase complex. {ECO:0000250|UniProtKB:P48735}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000250|UniProtKB:P48735};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P33198};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P33198};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P33198};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P33198}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P33198}.
CC -!- PTM: Acetylation at Lys-413 dramatically reduces catalytic activity.
CC Deacetylated by SIRT3 (By similarity). {ECO:0000250|UniProtKB:P48735}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; X69432; CAA49207.1; -; mRNA.
DR EMBL; BC102509; AAI02510.1; -; mRNA.
DR PIR; S33859; S33859.
DR RefSeq; NP_786984.1; NM_175790.2.
DR AlphaFoldDB; Q04467; -.
DR SMR; Q04467; -.
DR IntAct; Q04467; 1.
DR STRING; 9913.ENSBTAP00000018741; -.
DR PaxDb; Q04467; -.
DR PeptideAtlas; Q04467; -.
DR PRIDE; Q04467; -.
DR Ensembl; ENSBTAT00000018741; ENSBTAP00000018741; ENSBTAG00000014093.
DR GeneID; 327669; -.
DR KEGG; bta:327669; -.
DR CTD; 3418; -.
DR VEuPathDB; HostDB:ENSBTAG00000014093; -.
DR VGNC; VGNC:53941; IDH2.
DR eggNOG; KOG1526; Eukaryota.
DR GeneTree; ENSGT00390000012547; -.
DR HOGENOM; CLU_023296_1_1_1; -.
DR InParanoid; Q04467; -.
DR OMA; IQKRWPL; -.
DR OrthoDB; 769322at2759; -.
DR TreeFam; TF300428; -.
DR Reactome; R-BTA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-BTA-71403; Citric acid cycle (TCA cycle).
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000014093; Expressed in cardiac ventricle and 107 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) 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:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822; PTHR11822; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW Manganese; Metal-binding; Mitochondrion; NADP; Oxidoreductase;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8318002"
FT CHAIN 40..452
FT /note="Isocitrate dehydrogenase [NADP], mitochondrial"
FT /id="PRO_0000014419"
FT BINDING 115..117
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT BINDING 117
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT BINDING 134..140
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 149
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 172
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT BINDING 349..354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT BINDING 367
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O75874"
FT SITE 179
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT SITE 251
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P33198"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 80
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 106
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 106
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 166
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 166
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 180
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 180
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 193
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 193
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 256
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 256
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 280
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 282
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 282
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 384
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 384
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54071"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT MOD_RES 442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48735"
FT CONFLICT 24
FT /note="A -> R (in Ref. 1; CAA49207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50739 MW; FAB87D3C624E0C71 CRC64;
MAGYLRVVRS LCRASGSGSA WAPAALTAPN LQEQPRRHYA DKRIKVAKPV VEMDGDEMTR
IIWQFIKEKL ILPHVDVQLK YFDLGLPNRD QTNDQVTIDS ALATQKYSVA VKCATITPDE
ARVEEFKLKK MWKSPNGTIR NILGGTVFRE PIICKNIPRL VPGWTKPITI GRHAHGDQYK
ATDFVVDRAG TFKVVFTPKD GSGPKEWEVY NFPAGGVGMG MYNTDESISG FAHSCFQYAI
QKKWPLYMST KNTILKAYDG RFKDIFQAIF EKHYKTEFDK HKIWYEHRLI DDMVAQVLKS
SGGFVWACKN YDGDVQSDIL AQGFGSLGLM TSVLVCPDGK TIEAEAAHGT VTRHYREHQK
GRPTSTNPIA SIFAWTRGLE HRGKLDGNQD LIRFAQTLEK VCVETVESGA MTKDLAGCIH
GLSNVKLNEH FLNTSDFLDT IKSNLDRALG QQ
