Reviewed, UniProtKB/Swiss-Prot P93032 (IDH2_ARATH)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase 2
    NAD(+)-specific ICDH 2
    IDH-II

Gene names

Name:	IDH2
Ordered Locus Names:	At2g17130
ORF Names:	F6P23.14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Performs an essential role in the oxidative function of the citric acid cycle. Ref.5
Catalytic activity	Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Heteroligomer of catalytic and regulatory subunits.
Subcellular location	Mitochondrion Ref.4.
Tissue specificity	Ubiquitous. Predominantly expressed in roots, stems and leaves. Ref.5 Ref.6
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Ref.4 Inferred from direct assay. Source: TAIR
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P93032-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P93032-2)

The sequence of this isoform differs from the canonical sequence as follows:
     171-174: Missing.

Note: Derived from EST data. May be due to a competing acceptor splice site. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion Potential
	Chain	26 – 367	342	Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial		PRO_0000271288
Sites
	Metal binding	234	1	Magnesium or manganese By similarity
	Binding site	116	1	Substrate By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	234	1	Substrate By similarity
	Site	154	1	Critical for catalysis By similarity
	Site	201	1	Critical for catalysis By similarity
Natural variations
	Alternative sequence	171 – 174	4	Missing in isoform 2.		VSP_027467
Experimental info
	Sequence conflict	6	1	F → S in AAC49965. Ref.1
	Sequence conflict	18	1	G → R in AAC49965. Ref.1
	Sequence conflict	271	1	T → S in AAC49965. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: B5BC1C422AF757F7	FASTA	367	39,590
	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
	Isoform 2. Checksum: 1F691FD0BE2E7146	FASTA	363	39,149
	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 FCSERIAKYA 190 200 210 220 230 240 FEYAYLNNRK KVTAVHKANI MKLADGLFLE SCQEVAKKYP SIAYNEIIVD NCCMQLVARP 250 260 270 280 290 300 EQFDVMVTPN LYGNLVANTA AGIAGGTGVM PGGNVGAEYA VFEQGASAGN VGKDTTEEQK 310 320 330 340 350 360 NANPVALLLS SAMMLRHLQF PSFADRLETA VKRVIAEGNC RTEDLGGNST TQEVVDAVIA NLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Characterization of two closely related subunits." Behal R.H., Oliver D.J. Plant Mol. Biol. 36:691-698(1998) [PubMed: 9526501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." 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. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." 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. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Characterization of a mutation in the IDH-II subunit of the NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana." Lin M., Behal R.H., Oliver D.J. Plant Sci. 166:983-988(2004) [Agricola: IND43633651] Cited for: GENE FAMILY, FUNCTION, TISSUE SPECIFICITY.
[6]	"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." Lemaitre T., Hodges M. Plant Cell Physiol. 47:634-643(2006) [PubMed: 16527867] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U81994 mRNA. Translation: AAC49965.1. AK228337 mRNA. Translation: BAF00277.1.
IPI	IPI00536659. IPI00548170.
PIR	D84548.
RefSeq	NP_179304.1. NP_849963.1.
UniGene	At.12294 At.48484 Rra.11327 Rsa.17113 Rsa.6769
3D structure databases
HSSP	HSSP built from PDB template 1X0L based on UniProtKB Q8RQU4.
SMR	P93032. Positions 35-367.
ModBase	Search...
Protein-protein interaction databases
STRING	P93032.
Proteomic databases
PRIDE	P93032.
Genome annotation databases
GeneID	816218.
GenomeReviews	Gene locus AT2G17130 in contig CT485783_GR.
KEGG	ath:AT2G17130.
NMPDR	fig|3702.1.peg.8702.
Organism-specific databases
GeneFarm	4366. 439.
TAIR	At2g17130.
Phylogenomic databases
HOGENOM	HBG518924.
InParanoid	P93032.
OMA	MENMATE.
PhylomeDB	P93032.
Enzyme and pathway databases
BRENDA	1.1.1.41. 302.
Gene expression databases
Genevestigator	P93032.
Family and domain databases
InterPro	IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD_mit. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00175. mito_nad_idh. 1 hit.
PROSITE	PS00470. IDH_IMDH. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH2_ARATH

Accession

Primary (citable) accession number: P93032
Secondary accession number(s): Q7XJT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	February 9, 2010
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)