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   25-NOV-2008, entry version 36.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] catalytic subunit 6, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase 6;
DE   AltName: Full=NAD(+)-specific ICDH 6;
DE   AltName: Full=IDH-VI;
DE   Flags: Precursor;
GN   Name=IDH6; OrderedLocusNames=At3g09810/At3g09805; ORFNames=F8A24.14;
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=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
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   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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 leaves.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AC015985; AAF23254.1; -; 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; -.
DR   UniGene; At.22515; -.
DR   HSSP; Q56268; 1A05.
DR   GeneID; 820139; -.
DR   GenomeReviews; BA000014_GR; AT3G09810.
DR   KEGG; ath:AT3G09810; -.
DR   NMPDR; fig|3702.1.peg.12999; -.
DR   TAIR; At3g09810; -.
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; 1.
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     44       Mitochondrion (Potential).
FT   CHAIN        45    374       Isocitrate dehydrogenase [NAD] catalytic
FT                                subunit 6, mitochondrial.
FT                                /FTId=PRO_0000271292.
FT   METAL       245    245       Magnesium or manganese (By similarity).
FT   METAL       269    269       Magnesium or manganese (By similarity).
FT   METAL       273    273       Magnesium or manganese (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     245    245       Substrate (By similarity).
FT   SITE        165    165       Critical for catalysis (By similarity).
FT   SITE        212    212       Critical for catalysis (By similarity).
FT   CONFLICT      3      3       M -> I (in Ref. 4; AAM60999).
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
//