ID   IDH3_ARATH              Reviewed;         368 AA.
AC   O81796;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] regulatory subunit 3, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase 3;
DE   AltName: Full=NAD(+)-specific ICDH 3;
DE   AltName: Full=IDH-III;
DE   Flags: Precursor;
GN   Name=IDH3; OrderedLocusNames=At4g35650; ORFNames=F8D20.160;
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 [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   [2]
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   [3]
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   [4]
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   [5]
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: Mainly expressed at a low level in pollen.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL031135; CAA20035.1; -; Genomic_DNA.
DR   EMBL; AL161587; CAB80281.1; -; Genomic_DNA.
DR   EMBL; BT003922; AAO41969.1; -; mRNA.
DR   EMBL; BT006081; AAP04066.1; -; mRNA.
DR   IPI; IPI00526671; -.
DR   PIR; T04670; T04670.
DR   RefSeq; NP_195290.1; -.
DR   UniGene; At.31403; -.
DR   HSSP; P39126; 1HQS.
DR   GeneID; 829717; -.
DR   GenomeReviews; CT486007_GR; AT4G35650.
DR   KEGG; ath:AT4G35650; -.
DR   NMPDR; fig|3702.1.peg.21650; -.
DR   GeneFarm; 4368; 439.
DR   TAIR; At4g35650; -.
DR   OMA; O81796; SEVMESI.
DR   BRENDA; 1.1.1.41; 302.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:EC.
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:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD_mit.
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     26       Mitochondrion (Potential).
FT   CHAIN        27    368       Isocitrate dehydrogenase [NAD] regulatory
FT                                subunit 3, mitochondrial.
FT                                /FTId=PRO_0000271289.
FT   METAL       235    235       Magnesium or manganese (By similarity).
FT   BINDING     117    117       Substrate (By similarity).
FT   BINDING     148    148       Substrate (By similarity).
FT   BINDING     235    235       Substrate (By similarity).
FT   SITE        155    155       Critical for catalysis (By similarity).
FT   SITE        202    202       Critical for catalysis (By similarity).
SQ   SEQUENCE   368 AA;  39957 MW;  28EDD697B921650D CRC64;
     MARRSVSIFN RLLANPPSPF TSLSRSITYM PRPGDGAPRT VTLIPGDGIG PLVTGAVEQV
     MEAMHAPVHF ERYEVLGNMR KVPEEVIESV KRNKVCLKGG LATPVGGGVS SLNMQLRKEL
     DIFASLVNCI NVPGLVTRHE NVDIVVIREN TEGEYSGLEH EVVPGVVESL KVITKFCSER
     IARYAFEYAY LNNRKKVTAV HKANIMKLAD GLFLESCREV AKHYSGITYN EIIVDNCCMQ
     LVAKPEQFDV MVTPNLYGNL IANTAAGIAG GTGVMPGGNV GAEHAIFEQG ASAGNVGNDK
     MVEQKKANPV ALLLSSAMML RHLRFPTFAD RLETAVKQVI KEGKYRTKDL GGDCTTQEVV
     DAVIAALE
//