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UniProtKB/Swiss-Prot entry Q8LG77


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDH6_ARATH
Primary accession number Q8LG77
Secondary accession number Q9SF84
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on January 9, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 35)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] catalytic subunit 6, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase 6
NAD(+)-specific ICDH 6
IDH-VI
Gene name
Name: IDH6
OrderedLocusNames: At3g09810/At3g09805
ORFNames: F8A24.14
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[6]
GENE FAMILY.
DOI=10.1016/j.plantsci.2003.12.012; AGRICOLA=IND43633651
Lin M., Behal R.H., Oliver D.J.;
"Characterization of a mutation in the IDH-II subunit of the NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana.";
Plant Sci. 166:983-988(2004).
[7]
TISSUE SPECIFICITY.
DOI=10.1093/pcp/pcj030; PubMed=16527867 [NCBI, ExPASy, EBI, Israel, Japan]
Lemaitre T., Hodges M.;
"Expression analysis of Arabidopsis thaliana NAD-dependent isocitrate dehydrogenase genes shows the presence of a functional subunit that is mainly expressed in the pollen and absent from vegetative organs.";
Plant Cell Physiol. 47:634-643(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC015985; AAF23254.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF324664; AAG40015.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF327427; AAG42017.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF339723; AAK00405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK176269; BAD44032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK228113; BAF00071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084425; AAM60999.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_850549.1; -.
UniGene At.22515
3D structure databases
HSSP Q56268; 1A05. [HSSP ENTRY / PDB]
ModBase Q8LG77.
Organism-specific databases
TAIR At3g09810; -.
Ontologies
GO
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; 1.
BLOCKS Q8LG77.
ProtoNet Q8LG77.
Genome annotation databases
GeneID 820139; -.
GenomeReviews BA000014_GR; AT3G09810.
KEGG ath:AT3G09810; -.
NMPDR fig|3702.1.peg.12999; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    44  44     Mitochondrion (Potential). 
CHAIN   45   374  330     Isocitrate dehydrogenase [NAD] catalytic subunit 6, mitochondrial. PRO_0000271292
METAL   245   245        Magnesium or manganese (By similarity). 
METAL   269   269        Magnesium or manganese (By similarity). 
METAL   273   273        Magnesium or manganese (By similarity). 
BINDING   127   127        Substrate (By similarity). 
BINDING   137   137        Substrate (By similarity). 
BINDING   158   158        Substrate (By similarity). 
BINDING   245   245        Substrate (By similarity). 
SITE   165   165  1     Critical for catalysis (By similarity). 
SITE   212   212  1     Critical for catalysis (By similarity). 
CONFLICT   3     3        M -> I (in Ref. 4; AAM60999). 
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 40576 Da [This is the MW of the unprocessed precursor] CRC64: 3587127E0EAB87A4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTMTAFLARR LIGNGSSQIL GTSSSSSGPF ISVSRAFFSS STPIKATLFP GDGIGPEIAE 

        70         80         90        100        110        120 
SVKQVFTAAD VVIDWDEQFV GTEVDPRTNS FLTWDNLQSV LKNKVGLKGP MATPIGKGHR 

       130        140        150        160        170        180 
SLNLTLRKEL NLYANVRPCY SLPGYKTRYD DVDLITIREN TEGEYSGLEH QVVKGVVESL 

       190        200        210        220        230        240 
KIITRKASMR VAEYAFLYAK THGRKKVSAI HKANIMQKTD GLFLQCCDEV AAKYPEIYYE 

       250        260        270        280        290        300 
KVVIDNCCMM LVKNPALFDV LVMPNLYGDI ISDLCAGLVG GLGLTPSMNI GEDGIALAEA 

       310        320        330        340        350        360 
VHGSAPDIAG MNLANPTALL LSGVMMLRHL KLNKQAEQIH SAIINTIAEG KYRTADLGGS 

       370 
STTTDFTKAI CDHL 

Q8LG77 in FASTA format

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