ICDHC_ARATH
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 03-AUG-2022, entry version 158.
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 lenght 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}.
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; 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.AT1G65930.1; -.
DR iPTMnet; Q9SRZ6; -.
DR MetOSite; Q9SRZ6; -.
DR PaxDb; Q9SRZ6; -.
DR PRIDE; Q9SRZ6; -.
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; locus:2009759; AT1G65930.
DR eggNOG; KOG1526; Eukaryota.
DR HOGENOM; CLU_023296_1_1_1; -.
DR InParanoid; Q9SRZ6; -.
DR OMA; NEHYVIT; -.
DR OrthoDB; 769322at2759; -.
DR PhylomeDB; Q9SRZ6; -.
DR BioCyc; MetaCyc:AT1G65930-MON; -.
DR BRENDA; 1.1.1.42; 399.
DR PRO; PR:Q9SRZ6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRZ6; baseline and differential.
DR Genevisible; Q9SRZ6; AT.
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:0005739; C:mitochondrion; IBA:GO_Central.
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 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 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
