IDH1_ARATH
ID IDH1_ARATH Reviewed; 367 AA.
AC Q8LFC0; O65501; P94015; Q7DM90;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial;
DE AltName: Full=IDH-I;
DE AltName: Full=Isocitric dehydrogenase 1;
DE AltName: Full=NAD(+)-specific ICDH 1;
DE Flags: Precursor;
GN Name=IDH1; OrderedLocusNames=At4g35260; ORFNames=F23E12.180;
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], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 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 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:0000250|UniProtKB:P93032}.
CC -!- SUBUNIT: Heterooligomer of catalytic and regulatory subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in roots, stems
CC and leaves. {ECO:0000269|PubMed:16527867}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; U81993; AAC49964.1; -; mRNA.
DR EMBL; U82203; AAC49966.1; -; Genomic_DNA.
DR EMBL; AL022604; CAA18743.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80243.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86486.1; -; Genomic_DNA.
DR EMBL; AF428360; AAL16290.1; -; mRNA.
DR EMBL; AY049260; AAK83602.1; -; mRNA.
DR EMBL; AY129494; AAM91080.1; -; mRNA.
DR EMBL; AY084937; AAM61498.1; -; mRNA.
DR PIR; T06131; T06131.
DR RefSeq; NP_195252.1; NM_119692.3.
DR AlphaFoldDB; Q8LFC0; -.
DR SMR; Q8LFC0; -.
DR BioGRID; 14961; 22.
DR IntAct; Q8LFC0; 4.
DR STRING; 3702.AT4G35260.1; -.
DR PaxDb; Q8LFC0; -.
DR PRIDE; Q8LFC0; -.
DR ProteomicsDB; 228793; -.
DR EnsemblPlants; AT4G35260.1; AT4G35260.1; AT4G35260.
DR GeneID; 829679; -.
DR Gramene; AT4G35260.1; AT4G35260.1; AT4G35260.
DR KEGG; ath:AT4G35260; -.
DR Araport; AT4G35260; -.
DR TAIR; locus:2122098; AT4G35260.
DR eggNOG; KOG0784; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; Q8LFC0; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 868374at2759; -.
DR PhylomeDB; Q8LFC0; -.
DR BRENDA; 1.1.1.41; 399.
DR PRO; PR:Q8LFC0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LFC0; baseline and differential.
DR Genevisible; Q8LFC0; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006102; P:isocitrate metabolic process; IMP:TAIR.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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.
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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..367
FT /note="Isocitrate dehydrogenase [NAD] regulatory subunit 1,
FT mitochondrial"
FT /id="PRO_0000271287"
FT CONFLICT 174
FT /note="K -> N (in Ref. 5; AAM61498)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="L -> P (in Ref. 1; AAC49964)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="I -> T (in Ref. 1; AAC49964)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="C -> F (in Ref. 5; AAM61498)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="V -> G (in Ref. 1; AAC49964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39627 MW; 62DF327529961082 CRC64;
MSRRSLTLLK NLARNANGSG IQTRSVTYMP RPGDGAPRAV TLIPGDGIGP LVTNAVEQVM
EAMHAPIFFE KYDVHGEMSR VPPEVMESIR KNKVCLKGGL KTPVGGGVSS LNVQLRKELD
LFASLVNCFN LPGLPTRHEN VDIVVIRENT EGEYAGLEHE VVPGVVESLK VITKFCSERI
AKYAFEYAYL NNRKKVTAVH KANIMKLADG LFLESCREVA KKYPSITYNE IIVDNCCMQL
VAKPEQFDVM VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG ADHAVFEQGA SAGNVGKDKI
VLENKANPVA LLLSSAMMLR HLQFPSFADR LETAVKKVIA EGKCRTKDLG GTSTTQEVVD
AVIAKLD
