ICDHX_ARATH
ID ICDHX_ARATH Reviewed; 416 AA.
AC Q9SLK0;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peroxisomal isocitrate dehydrogenase [NADP];
DE EC=1.1.1.42;
GN Name=ICDH; OrderedLocusNames=At1g54340; ORFNames=F20D21.16;
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 Kihara T., Ito N., Koyama H., Hara T.;
RT "Isolation of cDNA encoding NADP-specific isocitrate dehydrogenase from
RT Arabidopsis thaliana.";
RL Submitted (OCT-2000) 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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
CC -!- FUNCTION: May be involved in response to oxidative stresses.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17951448}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AF316501; AAK06592.1; -; mRNA.
DR EMBL; AC005287; AAD25614.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33082.1; -; Genomic_DNA.
DR EMBL; BT025983; ABG25072.1; -; mRNA.
DR PIR; A96585; A96585.
DR RefSeq; NP_175836.1; NM_104312.3.
DR AlphaFoldDB; Q9SLK0; -.
DR SMR; Q9SLK0; -.
DR BioGRID; 27100; 3.
DR STRING; 3702.AT1G54340.1; -.
DR PaxDb; Q9SLK0; -.
DR PRIDE; Q9SLK0; -.
DR ProteomicsDB; 228758; -.
DR EnsemblPlants; AT1G54340.1; AT1G54340.1; AT1G54340.
DR GeneID; 841875; -.
DR Gramene; AT1G54340.1; AT1G54340.1; AT1G54340.
DR KEGG; ath:AT1G54340; -.
DR Araport; AT1G54340; -.
DR TAIR; locus:2020128; AT1G54340.
DR eggNOG; KOG1526; Eukaryota.
DR HOGENOM; CLU_023296_1_1_1; -.
DR InParanoid; Q9SLK0; -.
DR OMA; PYLELNI; -.
DR OrthoDB; 769322at2759; -.
DR PhylomeDB; Q9SLK0; -.
DR BioCyc; ARA:AT1G54340-MON; -.
DR BRENDA; 1.1.1.42; 399.
DR PRO; PR:Q9SLK0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SLK0; baseline and differential.
DR Genevisible; Q9SLK0; AT.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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: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 Magnesium; Manganese; Metal-binding; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome; Stress response; Tricarboxylic acid cycle.
FT CHAIN 1..416
FT /note="Peroxisomal isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000421962"
FT MOTIF 414..416
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000305"
FT BINDING 77..79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 96..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 311..316
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 213
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 47234 MW; EEAAAC9E5C6B2FA5 CRC64;
MEFEKIKVIN PVVEMDGDEM TRVIWKFIKD KLIFPFLELD IKYFDLGLPN RDFTDDKVTI
ETAEATLKYN VAIKCATITP DEARVREFGL KKMWRSPNGT IRNILNGTVF REPIICRNIP
RLVPGWTKPI CIGRHAFGDQ YRATDLIVNE PGKLKLVFEP SGSSQKTEFE VFNFTGGGVA
LAMYNTDESI RAFAESSMYT AYQKKWPLYL STKNTILKIY DGRFKDIFQE VYEANWRSKY
EAAGIWYEHR LIDDMVAYAM KSEGGYVWAC KNYDGDVQSD FLAQGYGSLG MMTSVLVCPD
GKTIEAEAAH GTVTRHYRVH QKGGETSTNS IASIFAWSRG LAHRAKLDSN AALLSYTEKL
EAACMGTVES GKMTKDLALL IHGAKVRRDQ YVNTEEFIDA VAWELKRRLL GNNSRL
