ID   ICDHC_ARATH             Reviewed;         410 AA.
AC   Q9SRZ6; Q8L9Z4; Q8RWH2; Q8RYD5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Cytosolic isocitrate dehydrogenase [NADP] {ECO:0000303|PubMed:20199623};
DE            EC=1.1.1.42 {ECO:0000269|PubMed:20199623};
GN   Name=CICDH {ECO:0000303|PubMed:20199623};
GN   OrderedLocusNames=At1g65930 {ECO:0000312|Araport:AT1G65930};
GN   ORFNames=F12P19.10 {ECO:0000312|EMBL:AAF06054.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Pistelli L., De Bellis L., Alpi A., Gonzali S.;
RT   "Molecular cloning of a full length cDNA encoding for NADP+-isocitrate
RT   dehydrogenase from Arabidopsis thaliana.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20199623; DOI=10.1111/j.1365-3040.2010.02133.x;
RA   Mhamdi A., Mauve C., Gouia H., Saindrenan P., Hodges M., Noctor G.;
RT   "Cytosolic NADP-dependent isocitrate dehydrogenase contributes to redox
RT   homeostasis and the regulation of pathogen responses in Arabidopsis
RT   leaves.";
RL   Plant Cell Environ. 33:1112-1123(2010).
CC   -!- FUNCTION: May supply 2-oxoglutarate for amino acid biosynthesis and
CC       ammonia assimilation via the glutamine synthetase/glutamate synthase
CC       (GS/GOGAT) pathway. May be involved in the production of NADPH to
CC       promote redox signaling or homeostasis in response to oxidative stress,
CC       or redox signaling linked to defense responses.
CC       {ECO:0000269|PubMed:20199623}.
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:0000269|PubMed:20199623};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19630;
CC         Evidence={ECO:0000269|PubMed:20199623};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O75874};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O75874};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000250|UniProtKB:O75874};
CC   -!- INTERACTION:
CC       Q9SRZ6; Q42403: TRX3; NbExp=2; IntAct=EBI-449319, EBI-449157;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Slight reduction in plant growth. Constitutive
CC       expression of pathogenesis-related genes and enhanced resistance to the
CC       bacterial pathogen P.syringae pv. tomato.
CC       {ECO:0000269|PubMed:20199623}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; AJ437268; CAD24782.1; -; mRNA.
DR   EMBL; AC009513; AAF06054.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34442.1; -; Genomic_DNA.
DR   EMBL; AF419575; AAL31907.1; -; mRNA.
DR   EMBL; AY045631; AAK73989.1; -; mRNA.
DR   EMBL; AY093091; AAM13090.1; -; mRNA.
DR   EMBL; AY097340; AAM19856.1; -; mRNA.
DR   EMBL; BT002400; AAO00760.1; -; mRNA.
DR   EMBL; AY088129; AAM65674.1; -; mRNA.
DR   PIR; F96683; F96683.
DR   RefSeq; NP_176768.1; NM_105265.5.
DR   AlphaFoldDB; Q9SRZ6; -.
DR   SMR; Q9SRZ6; -.
DR   BioGRID; 28126; 6.
DR   IntAct; Q9SRZ6; 2.
DR   STRING; 3702.Q9SRZ6; -.
DR   iPTMnet; Q9SRZ6; -.
DR   MetOSite; Q9SRZ6; -.
DR   PaxDb; 3702-AT1G65930-1; -.
DR   ProteomicsDB; 228756; -.
DR   EnsemblPlants; AT1G65930.1; AT1G65930.1; AT1G65930.
DR   GeneID; 842905; -.
DR   Gramene; AT1G65930.1; AT1G65930.1; AT1G65930.
DR   KEGG; ath:AT1G65930; -.
DR   Araport; AT1G65930; -.
DR   TAIR; AT1G65930; CICDH.
DR   eggNOG; KOG1526; Eukaryota.
DR   HOGENOM; CLU_023296_1_1_1; -.
DR   InParanoid; Q9SRZ6; -.
DR   OMA; EYPVYNF; -.
DR   OrthoDB; 423at2759; -.
DR   PhylomeDB; Q9SRZ6; -.
DR   BioCyc; MetaCyc:AT1G65930-MONOMER; -.
DR   BRENDA; 1.1.1.42; 399.
DR   PRO; PR:Q9SRZ6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SRZ6; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IMP:TAIR.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0006102; P:isocitrate metabolic process; IMP:TAIR.
DR   GO; GO:0006739; P:NADP metabolic process; IMP:TAIR.
DR   GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
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.
DR   Genevisible; Q9SRZ6; AT.
PE   1: Evidence at protein level;
KW   Cytoplasm; Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase;
KW   Plant defense; Reference proteome; Stress response;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..410
FT                   /note="Cytosolic isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000421963"
FT   BINDING         77..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         96..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         260
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         279
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         310..315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   BINDING         328
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   SITE            141
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   SITE            212
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:O75874"
FT   CONFLICT        181
FT                   /note="A -> V (in Ref. 1; CAD24782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="E -> K (in Ref. 5; AAM65674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="F -> L (in Ref. 1; CAD24782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="T -> S (in Ref. 1; CAD24782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="G -> A (in Ref. 5; AAM65674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="E -> D (in Ref. 4; AAM13090)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  45746 MW;  6CC3CA11AB631D28 CRC64;
     MAFEKIKVAN PIVEMDGDEM TRVIWKSIKD KLITPFVELD IKYFDLGLPH RDATDDKVTI
     ESAEATKKYN VAIKCATITP DEGRVTEFGL KQMWRSPNGT IRNILNGTVF REPIICKNVP
     KLVPGWTKPI CIGRHAFGDQ YRATDAVIKG PGKLTMTFEG KDGKTETEVF TFTGEGGVAM
     AMYNTDESIR AFADASMNTA YEKKWPLYLS TKNTILKKYD GRFKDIFQEV YEASWKSKYD
     AAGIWYEHRL IDDMVAYALK SEGGYVWACK NYDGDVQSDF LAQGFGSLGL MTSVLVCPDG
     KTIEAEAAHG TVTRHFRVHQ KGGETSTNSI ASIFAWTRGL AHRAKLDDNA KLLDFTEKLE
     AACVGTVESG KMTKDLALII HGSKLSRDTY LNTEEFIDAV AAELKERLNA
//