Reviewed, UniProtKB/Swiss-Prot Q945K7 (IDH5_ARATH)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] catalytic subunit 5, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase 5
    NAD(+)-specific ICDH 5
    IDH-V

Gene names

Name:	IDH5
Ordered Locus Names:	At5g03290
ORF Names:	MOK16.20, F12E4_20

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	374 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.4.
Tissue specificity	Ubiquitous. Ref.6
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	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Ref.4 Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from direct assay. Source: TAIR 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 – 44	44	Mitochondrion Potential
	Chain	45 – 374	330	Isocitrate dehydrogenase [NAD] catalytic subunit 5, mitochondrial		PRO_0000271291
Sites
	Metal binding	245	1	Magnesium or manganese By similarity
	Metal binding	269	1	Magnesium or manganese By similarity
	Metal binding	273	1	Magnesium or manganese By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	245	1	Substrate By similarity
	Site	165	1	Critical for catalysis By similarity
	Site	212	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q945K7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 723D0150C360F7A1	FASTA	374	40,625
	10 20 30 40 50 60 MTMAANLARR LIGNRSTQIL GAVNSSSGAA SSVARAFCSS TTPITATLFP GDGIGPEIAE 70 80 90 100 110 120 SVKKVFTTAG VPIEWEEHYV GTEIDPRTQS FLTWESLESV RRNKVGLKGP MATPIGKGHR 130 140 150 160 170 180 SLNLTLRKEL NLYANVRPCY SLPGYKTRYD DVDLITIREN TEGEYSGLEH QVVRGVVESL 190 200 210 220 230 240 KIITRQASLR VAEYAFLYAK THGRERVSAI HKANIMQKTD GLFLKCCREV AEKYPEITYE 250 260 270 280 290 300 EVVIDNCCMM LVKNPALFDV LVMPNLYGDI ISDLCAGLVG GLGLTPSCNI GEDGVALAEA 310 320 330 340 350 360 VHGSAPDIAG KNLANPTALL LSGVMMLRHL KFNEQAEQIH SAIINTIAEG KYRTADLGGS 370 STTTEFTKAI CDHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed: 9330910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [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]	"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.
[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	AB005240 Genomic DNA. Translation: BAB08389.1. Different initiation. AL162751 Genomic DNA. Translation: CAB83285.1. Different initiation. AF412100 mRNA. Translation: AAL06553.1. AY099823 mRNA. Translation: AAM20674.1. BT008460 mRNA. Translation: AAP37819.1.
IPI	IPI00530201.
PIR	T48350.
RefSeq	NP_568113.1.
UniGene	At.25268 Rra.8263 Rsa.4566
3D structure databases
HSSP	HSSP built from PDB template 1X0L based on UniProtKB Q8RQU4.
SMR	Q945K7. Positions 41-374.
ModBase	Search...
Protein-protein interaction databases
STRING	Q945K7.
Proteomic databases
PRIDE	Q945K7.
Genome annotation databases
GeneID	831884.
GenomeReviews	Gene locus AT5G03290 in contig BA000015_GR.
KEGG	ath:AT5G03290.
NMPDR	fig|3702.1.peg.22410.
Organism-specific databases
TAIR	At5g03290.
Phylogenomic databases
eggNOG	KOG0785.
HOGENOM	HBG518924.
InParanoid	Q945K7.
OMA	RRNKVGL.
PhylomeDB	Q945K7.
Enzyme and pathway databases
BRENDA	1.1.1.41. 302.
Gene expression databases
ArrayExpress	Q945K7.
Genevestigator	Q945K7.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IDH5_ARATH

Accession

Primary (citable) accession number: Q945K7
Secondary accession number(s): Q9LZG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)