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UniProtKB/Swiss-Prot entry P93032


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

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Entry information
Entry name IDH2_ARATH
Primary accession number P93032
Secondary accession number Q7XJT6
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 49)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase 2
NAD(+)-specific ICDH 2
IDH-II
Gene name
Name: IDH2
OrderedLocusNames: At2g17130
ORFNames: F6P23.14
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 [MRNA].
STRAIN=cv. Columbia;
DOI=10.1023/A:1005923410940; PubMed=9526501 [NCBI, ExPASy, EBI, Israel, Japan]
Behal R.H., Oliver D.J.;
"NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Characterization of two closely related subunits.";
Plant Mol. Biol. 36:691-698(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[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]
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).
[5]
GENE FAMILY, FUNCTION, AND TISSUE SPECIFICITY.
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).
[6]
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
U81994; AAC49965.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002354; AAB81675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK228337; BAF00277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D84548; D84548.
RefSeq NP_179304.1; -.
NP_849963.1; -.
UniGene At.48484
3D structure databases
HSSP P39126; 1HQS. [HSSP ENTRY / PDB]
ModBase P93032.
Organism-specific databases
GeneFarm 4366; 439.
TAIR At2g17130; -.
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; FALSE_NEG.
BLOCKS P93032.
ProtoNet P93032.
Genome annotation databases
GeneID 816218; -.
GenomeReviews CT485783_GR; AT2G17130.
KEGG ath:AT2G17130; -.
NMPDR fig|3702.1.peg.8702; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; 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    25  25     Mitochondrion (Potential). 
CHAIN   26   367  342     Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial. PRO_0000271288
METAL   234   234        Magnesium or manganese (By similarity). 
BINDING   116   116        Substrate (By similarity). 
BINDING   147   147        Substrate (By similarity). 
BINDING   234   234        Substrate (By similarity). 
SITE   154   154  1     Critical for catalysis (By similarity). 
SITE   201   201  1     Critical for catalysis (By similarity). 
VAR_SEQ   171   174        Missing (in isoform 2). VSP_027467
CONFLICT   6     6        F -> S (in Ref. 1; AAC49965). 
CONFLICT   18    18        G -> R (in Ref. 1; AAC49965). 
CONFLICT   271   271        T -> S (in Ref. 1; AAC49965). 
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 39590 Da [This is the MW of the unprocessed precursor] CRC64: B5BC1C422AF757F7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRQSFSLLK NLRSIASGSK IQTRSVTYMP RPGDGKPRPV TLIPGDGVGP LVTNAVQQVM 

        70         80         90        100        110        120 
EAMHAPVYFE PFEVHGDMKS LPEGLLESIK KNKVCLKGGL KTPVGGGVSS LNVNLRKELD 

       130        140        150        160        170        180 
LFASLVNCFN LPGLASRHEN VDIVVIRENT EGEYAGLEHE VVPGVVESLK VITKFCSERI 

       190        200        210        220        230        240 
AKYAFEYAYL NNRKKVTAVH KANIMKLADG LFLESCQEVA KKYPSIAYNE IIVDNCCMQL 

       250        260        270        280        290        300 
VARPEQFDVM VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG AEYAVFEQGA SAGNVGKDTT 

       310        320        330        340        350        360 
EEQKNANPVA LLLSSAMMLR HLQFPSFADR LETAVKRVIA EGNCRTEDLG GNSTTQEVVD 


AVIANLD 

P93032 in FASTA format

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