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Q945K7 (IDH5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NAD] catalytic subunit 5, mitochondrial

EC=1.1.1.41
Alternative name(s):
IDH-V
Isocitric dehydrogenase 5
NAD(+)-specific ICDH 5
Gene names
Name:IDH5
Ordered Locus Names:At5g03290
ORF Names:F12E4_20, MOK16.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Heterooligomer of catalytic and regulatory subunits.

Subcellular location

Mitochondrion Ref.5.

Tissue specificity

Ubiquitous. Ref.7

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence caution

The sequence BAB08389.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB83285.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 374330Isocitrate dehydrogenase [NAD] catalytic subunit 5, mitochondrial
PRO_0000271291

Sites

Metal binding2451Magnesium or manganese By similarity
Metal binding2691Magnesium or manganese By similarity
Metal binding2731Magnesium or manganese By similarity
Binding site1271Substrate By similarity
Binding site1371Substrate By similarity
Binding site1581Substrate By similarity
Binding site2451Substrate By similarity
Site1651Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q945K7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 723D0150C360F7A1

FASTA37440,625
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
[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] [Europe PMC]
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] [Europe PMC] [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.
CP002688 Genomic DNA. Translation: AED90581.1.
AF412100 mRNA. Translation: AAL06553.1.
AY099823 mRNA. Translation: AAM20674.1.
BT008460 mRNA. Translation: AAP37819.1.
PIRT48350.
RefSeqNP_568113.1. NM_120407.5.
UniGeneAt.25268.

3D structure databases

ProteinModelPortalQ945K7.
SMRQ945K7. Positions 40-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17160. 2 interactions.
IntActQ945K7. 1 interaction.
STRING3702.AT5G03290.1-P.

Proteomic databases

PaxDbQ945K7.
PRIDEQ945K7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G03290.1; AT5G03290.1; AT5G03290.
GeneID831884.
KEGGath:AT5G03290.

Organism-specific databases

TAIRAT5G03290.

Phylogenomic databases

eggNOGCOG0473.
HOGENOMHOG000021113.
InParanoidQ945K7.
KOK00030.
OMAEGMYSGL.
PhylomeDBQ945K7.
ProtClustDBPLN00118.

Enzyme and pathway databases

BioCycMetaCyc:AT5G03290-MONOMER.

Gene expression databases

GenevestigatorQ945K7.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDH5_ARATH
AccessionPrimary (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: March 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names