IDH6_ARATH
ID IDH6_ARATH Reviewed; 374 AA.
AC Q8LG77; Q9SF84;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Isocitrate dehydrogenase [NAD] catalytic subunit 6, mitochondrial;
DE EC=1.1.1.41 {ECO:0000305|PubMed:16527867};
DE AltName: Full=IDH-VI {ECO:0000303|PubMed:16527867};
DE AltName: Full=Isocitric dehydrogenase 6;
DE AltName: Full=NAD(+)-specific ICDH 6;
DE Flags: Precursor;
GN Name=IDH6; OrderedLocusNames=At3g09810; ORFNames=F8A24.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [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 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.
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 FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBUNIT.
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: Catalytic subunit of the NAD(+)-dependent isocitrate
CC dehydrogenase involved in the oxidative decarboxylation of isocitrate
CC to 2-oxoglutarate (Probable). Performs an essential role in the
CC oxidative function of the citric acid cycle.
CC {ECO:0000250|UniProtKB:P93032, ECO:0000305|PubMed:16527867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH;
CC Xref=Rhea:RHEA:23632, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.41;
CC Evidence={ECO:0000305|PubMed:16527867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23633;
CC Evidence={ECO:0000305|PubMed:16527867};
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 -!- SUBUNIT: Heterooligomer of catalytic and regulatory subunits.
CC {ECO:0000305|PubMed:16527867}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in leaves.
CC {ECO:0000269|PubMed:16527867}.
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; AC015985; AAF23254.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74815.1; -; Genomic_DNA.
DR EMBL; AF324664; AAG40015.1; -; mRNA.
DR EMBL; AF327427; AAG42017.1; -; mRNA.
DR EMBL; AF339723; AAK00405.1; -; mRNA.
DR EMBL; AK176269; BAD44032.1; -; mRNA.
DR EMBL; AK228113; BAF00071.1; -; mRNA.
DR EMBL; AY084425; AAM60999.1; -; mRNA.
DR RefSeq; NP_850549.1; NM_180218.2.
DR AlphaFoldDB; Q8LG77; -.
DR SMR; Q8LG77; -.
DR BioGRID; 5473; 8.
DR STRING; 3702.AT3G09810.1; -.
DR MetOSite; Q8LG77; -.
DR PaxDb; Q8LG77; -.
DR PRIDE; Q8LG77; -.
DR ProteomicsDB; 248619; -.
DR EnsemblPlants; AT3G09810.1; AT3G09810.1; AT3G09810.
DR GeneID; 820139; -.
DR Gramene; AT3G09810.1; AT3G09810.1; AT3G09810.
DR KEGG; ath:AT3G09810; -.
DR Araport; AT3G09810; -.
DR TAIR; locus:2074939; AT3G09810.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q8LG77; -.
DR OMA; IDWDEQF; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; Q8LG77; -.
DR BRENDA; 1.1.1.41; 399.
DR PRO; PR:Q8LG77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LG77; baseline and differential.
DR Genevisible; Q8LG77; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IGI:TAIR.
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; IGI:TAIR.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..374
FT /note="Isocitrate dehydrogenase [NAD] catalytic subunit 6,
FT mitochondrial"
FT /id="PRO_0000271292"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P50213"
FT SITE 165
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="M -> I (in Ref. 5; AAM60999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 40576 MW; 3587127E0EAB87A4 CRC64;
MTMTAFLARR LIGNGSSQIL GTSSSSSGPF ISVSRAFFSS STPIKATLFP GDGIGPEIAE
SVKQVFTAAD VVIDWDEQFV GTEVDPRTNS FLTWDNLQSV LKNKVGLKGP MATPIGKGHR
SLNLTLRKEL NLYANVRPCY SLPGYKTRYD DVDLITIREN TEGEYSGLEH QVVKGVVESL
KIITRKASMR VAEYAFLYAK THGRKKVSAI HKANIMQKTD GLFLQCCDEV AAKYPEIYYE
KVVIDNCCMM LVKNPALFDV LVMPNLYGDI ISDLCAGLVG GLGLTPSMNI GEDGIALAEA
VHGSAPDIAG MNLANPTALL LSGVMMLRHL KLNKQAEQIH SAIINTIAEG KYRTADLGGS
STTTDFTKAI CDHL
