ID   F1PZA1_CANLF            Unreviewed;       414 AA.
AC   F1PZA1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   Name=IDH1 {ECO:0000313|EMBL:BBC43078.1,
GN   ECO:0000313|Ensembl:ENSCAFP00845032495.1,
GN   ECO:0000313|VGNC:VGNC:110512};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845032495.1, ECO:0000313|Proteomes:UP000805418};
RN   [1] {ECO:0000313|EMBL:BBC43078.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29285579; DOI=10.1007/s11259-017-9707-8;
RA   Kawakami S., Ochiai K., Azakami D., Kato Y., Michishita M., Morimatsu M.,
RA   Ishiguro-Oonuma T., Onozawa E., Watanabe M., Omi T.;
RT   "R132 mutations in canine isocitrate dehydrogenase 1 (IDH1) lead to
RT   functional changes.";
RL   Vet. Res. Commun. 42:49-56(2018).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00845032495.1}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845032495.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR000108};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC       ECO:0000256|PIRNR:PIRNR000108}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LC214936; BBC43078.1; -; mRNA.
DR   RefSeq; XP_013966568.1; XM_014111093.1.
DR   RefSeq; XP_536047.2; XM_536047.4.
DR   STRING; 9615.ENSCAFP00000020046; -.
DR   PaxDb; 9615-ENSCAFP00000020046; -.
DR   Ensembl; ENSCAFT00845041440.1; ENSCAFP00845032495.1; ENSCAFG00845023478.1.
DR   GeneID; 478889; -.
DR   KEGG; cfa:478889; -.
DR   CTD; 3417; -.
DR   VEuPathDB; HostDB:ENSCAFG00845023478; -.
DR   VGNC; VGNC:110512; IDH1.
DR   eggNOG; KOG1526; Eukaryota.
DR   GeneTree; ENSGT00390000012547; -.
DR   HOGENOM; CLU_023296_1_1_1; -.
DR   OMA; HGTVQRH; -.
DR   OrthoDB; 423at2759; -.
DR   Reactome; R-CFA-389542; NADPH regeneration.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000805418; Chromosome 37.
DR   Bgee; ENSCAFG00000013617; Expressed in jejunum and 45 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006102; P:isocitrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
DR   GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0060696; P:regulation of phospholipid catabolic process; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR   PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 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   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000108};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000108};
KW   Reference proteome {ECO:0000313|Proteomes:UP000805418};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN          9..401
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         75..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         77
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         94..100
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         109
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         132
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT   BINDING         252
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT   BINDING         310..315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   BINDING         328
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT   SITE            139
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT   SITE            212
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ   SEQUENCE   414 AA;  46807 MW;  9B607A90F0C7F387 CRC64;
     MSQKIRGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA
     AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL
     VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GSEKMTYLVH NFEEGGGVAM
     GMYNQDKSIE DFAHSSFQMA LSKSWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE
     AQNIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG
     KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELSFFAKALE
     EVCVETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLNIKLA QAKL
//