Reviewed, UniProtKB/Swiss-Prot Q8LFC0 (IDH1_ARATH)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase 1
    NAD(+)-specific ICDH 1
    IDH-I

Gene names

Name:	IDH1
Ordered Locus Names:	At4g35260
ORF Names:	F23E12.180

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 By similarity.
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.5.
Tissue specificity	Ubiquitous. Predominantly expressed in roots, stems and leaves. Ref.7
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
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.5 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...

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 1, mitochondrial		PRO_0000271287
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
Experimental info
	Sequence conflict	174	1	K → N in AAM61498. Ref.4
	Sequence conflict	331	1	L → P in AAC49964. Ref.1
	Sequence conflict	339	1	I → T in AAC49964. Ref.1
	Sequence conflict	344	1	C → F in AAM61498. Ref.4
	Sequence conflict	362	1	V → G in AAC49964. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8LFC0-1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 62DF327529961082	FASTA	367	39,627
	10 20 30 40 50 60 MSRRSLTLLK NLARNANGSG IQTRSVTYMP RPGDGAPRAV TLIPGDGIGP LVTNAVEQVM 70 80 90 100 110 120 EAMHAPIFFE KYDVHGEMSR VPPEVMESIR KNKVCLKGGL KTPVGGGVSS LNVQLRKELD 130 140 150 160 170 180 LFASLVNCFN LPGLPTRHEN VDIVVIRENT EGEYAGLEHE VVPGVVESLK VITKFCSERI 190 200 210 220 230 240 AKYAFEYAYL NNRKKVTAVH KANIMKLADG LFLESCREVA KKYPSITYNE IIVDNCCMQL 250 260 270 280 290 300 VAKPEQFDVM VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG ADHAVFEQGA SAGNVGKDKI 310 320 330 340 350 360 VLENKANPVA LLLSSAMMLR HLQFPSFADR LETAVKKVIA EGKCRTKDLG GTSTTQEVVD AVIAKLD

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], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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].
[6]	"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.
[7]	"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	U81993 mRNA. Translation: AAC49964.1. U82203 Genomic DNA. Translation: AAC49966.1. AL022604 Genomic DNA. Translation: CAA18743.1. AL161587 Genomic DNA. Translation: CAB80243.1. AF428360 mRNA. Translation: AAL16290.1. AY049260 mRNA. Translation: AAK83602.1. AY129494 mRNA. Translation: AAM91080.1. AY084937 mRNA. Translation: AAM61498.1.
IPI	IPI00541759.
PIR	T06131.
RefSeq	NP_195252.1.
UniGene	At.22461 Rra.11327 Rra.15795 Rsa.6769
3D structure databases
HSSP	HSSP built from PDB template 1X0L based on UniProtKB Q8RQU4.
SMR	Q8LFC0. Positions 38-367.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8LFC0.
Proteomic databases
PRIDE	Q8LFC0.
Genome annotation databases
GeneID	829679.
GenomeReviews	Gene locus AT4G35260 in contig CT486007_GR.
KEGG	ath:AT4G35260.
NMPDR	fig|3702.1.peg.21603.
Organism-specific databases
GeneFarm	4364. 439.
TAIR	At4g35260.
Phylogenomic databases
eggNOG	KOG0784.
HOGENOM	HBG518924.
InParanoid	Q8LFC0.
OMA	MILCAAN.
PhylomeDB	Q8LFC0.
Enzyme and pathway databases
BRENDA	1.1.1.41. 302.
Gene expression databases
Genevestigator	Q8LFC0.
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

IDH1_ARATH

Accession

Primary (citable) accession number: Q8LFC0
Secondary accession number(s): O65501, P94015, Q7DM90

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	February 9, 2010
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)