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-NOV-2008, entry version 37.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase 1;
DE   AltName: Full=NAD(+)-specific ICDH 1;
DE   AltName: Full=IDH-I;
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP   1-171.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98187249; 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   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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].
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
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
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [6]
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   [7]
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
CC       the citric acid cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heteroligomer of catalytic and regulatory subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Predominantly expressed in roots,
CC       stems and leaves.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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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; 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; -.
DR   UniGene; At.22461; -.
DR   HSSP; P39126; 1HQS.
DR   GeneID; 829679; -.
DR   GenomeReviews; CT486007_GR; AT4G35260.
DR   KEGG; ath:AT4G35260; -.
DR   NMPDR; fig|3702.1.peg.21603; -.
DR   GeneFarm; 4364; 439.
DR   TAIR; At4g35260; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR004434; IsoCit_DHase_NAD_mit.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     25       Mitochondrion (Potential).
FT   CHAIN        26    367       Isocitrate dehydrogenase [NAD] regulatory
FT                                subunit 1, mitochondrial.
FT                                /FTId=PRO_0000271287.
FT   METAL       234    234       Magnesium or manganese (By similarity).
FT   BINDING     116    116       Substrate (By similarity).
FT   BINDING     147    147       Substrate (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
FT   SITE        154    154       Critical for catalysis (By similarity).
FT   SITE        201    201       Critical for catalysis (By similarity).
FT   CONFLICT    174    174       K -> N (in Ref. 4; AAM61498).
FT   CONFLICT    331    331       L -> P (in Ref. 1; AAC49964).
FT   CONFLICT    339    339       I -> T (in Ref. 1; AAC49964).
FT   CONFLICT    344    344       C -> F (in Ref. 4; AAM61498).
FT   CONFLICT    362    362       V -> G (in Ref. 1; AAC49964).
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
//