ID   IDH2_ARATH              Reviewed;         367 AA.
AC   P93032; Q7XJT6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 159.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial;
DE   AltName: Full=IDH-II;
DE   AltName: Full=Isocitric dehydrogenase 2;
DE   AltName: Full=NAD(+)-specific ICDH 2;
DE   Flags: Precursor;
GN   Name=IDH2; OrderedLocusNames=At2g17130; ORFNames=F6P23.14;
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;
RX   PubMed=9526501; DOI=10.1023/a:1005923410940;
RA   Behal R.H., Oliver D.J.;
RT   "NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana.
RT   Characterization of two closely related subunits.";
RL   Plant Mol. Biol. 36:691-698(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   GENE FAMILY, FUNCTION, AND TISSUE SPECIFICITY.
RX   AGRICOLA=IND43633651; DOI=10.1016/j.plantsci.2003.12.012;
RA   Lin M., Behal R.H., Oliver D.J.;
RT   "Characterization of a mutation in the IDH-II subunit of the NAD(+)-
RT   dependent isocitrate dehydrogenase from Arabidopsis thaliana.";
RL   Plant Sci. 166:983-988(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16527867; DOI=10.1093/pcp/pcj030;
RA   Lemaitre T., Hodges M.;
RT   "Expression analysis of Arabidopsis thaliana NAD-dependent isocitrate
RT   dehydrogenase genes shows the presence of a functional subunit that is
RT   mainly expressed in the pollen and absent from vegetative organs.";
RL   Plant Cell Physiol. 47:634-643(2006).
CC   -!- FUNCTION: Performs an essential role in the oxidative function of the
CC       citric acid cycle. {ECO:0000269|Ref.7}.
CC   -!- SUBUNIT: Heterooligomer of catalytic and regulatory subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P93032-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P93032-2; Sequence=VSP_027467;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in roots, stems
CC       and leaves. {ECO:0000269|PubMed:16527867, ECO:0000269|Ref.7}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC       site. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; U81994; AAC49965.1; -; mRNA.
DR   EMBL; CP002685; AEC06588.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06589.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7035277.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7035278.1; -; Genomic_DNA.
DR   EMBL; AK228337; BAF00277.1; -; mRNA.
DR   PIR; D84548; D84548.
DR   RefSeq; NP_179304.1; NM_127267.3. [P93032-1]
DR   RefSeq; NP_849963.1; NM_179632.2. [P93032-2]
DR   AlphaFoldDB; P93032; -.
DR   SMR; P93032; -.
DR   BioGRID; 1575; 3.
DR   FunCoup; P93032; 3095.
DR   STRING; 3702.P93032; -.
DR   PaxDb; 3702-P93032; -.
DR   ProteomicsDB; 248615; -. [P93032-1]
DR   GeneID; 816218; -.
DR   KEGG; ath:AT2G17130; -.
DR   Araport; AT2G17130; -.
DR   TAIR; AT2G17130; IDH2.
DR   eggNOG; KOG0784; Eukaryota.
DR   HOGENOM; CLU_031953_0_1_1; -.
DR   InParanoid; P93032; -.
DR   OMA; FYHRIPP; -.
DR   OrthoDB; 10261637at2759; -.
DR   PhylomeDB; P93032; -.
DR   BioCyc; MetaCyc:AT2G17130-MONOMER; -.
DR   BRENDA; 1.1.1.41; 399.
DR   PRO; PR:P93032; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93032; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; ISM:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0006102; P:isocitrate metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   FunFam; 3.40.718.10:FF:000009; Isocitrate dehydrogenase [NAD] regulatory subunit 1; 1.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00175; mito_nad_idh; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF69; ISOCITRATE DEHYDROGENASE [NAD] REGULATORY SUBUNIT 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NAD; Oxidoreductase; Reference proteome; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..367
FT                   /note="Isocitrate dehydrogenase [NAD] regulatory subunit 2,
FT                   mitochondrial"
FT                   /id="PRO_0000271288"
FT   VAR_SEQ         171..174
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_027467"
FT   CONFLICT        6
FT                   /note="F -> S (in Ref. 1; AAC49965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="G -> R (in Ref. 1; AAC49965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="T -> S (in Ref. 1; AAC49965)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  39590 MW;  B5BC1C422AF757F7 CRC64;
     MSRQSFSLLK NLRSIASGSK IQTRSVTYMP RPGDGKPRPV TLIPGDGVGP LVTNAVQQVM
     EAMHAPVYFE PFEVHGDMKS LPEGLLESIK KNKVCLKGGL KTPVGGGVSS LNVNLRKELD
     LFASLVNCFN LPGLASRHEN VDIVVIRENT EGEYAGLEHE VVPGVVESLK VITKFCSERI
     AKYAFEYAYL NNRKKVTAVH KANIMKLADG LFLESCQEVA KKYPSIAYNE IIVDNCCMQL
     VARPEQFDVM VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG AEYAVFEQGA SAGNVGKDTT
     EEQKNANPVA LLLSSAMMLR HLQFPSFADR LETAVKRVIA EGNCRTEDLG GNSTTQEVVD
     AVIANLD
//