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Q8LFC0

- IDH1_ARATH

UniProt

Q8LFC0 - IDH1_ARATH

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Protein

Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial

Gene

IDH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Performs an essential role in the oxidative function of the citric acid cycle.By similarity

Catalytic activityi

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactori

Binds 1 magnesium or manganese ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161SubstrateBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Sitei154 – 1541Critical for catalysisBy similarity
Sitei201 – 2011Critical for catalysisBy similarity
Metal bindingi234 – 2341Magnesium or manganeseBy similarity
Binding sitei234 – 2341SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate dehydrogenase (NAD+) activity Source: UniProtKB-EC
  2. magnesium ion binding Source: InterPro
  3. NAD binding Source: InterPro
  4. zinc ion binding Source: TAIR

GO - Biological processi

  1. isocitrate metabolic process Source: TAIR
  2. tricarboxylic acid cycle Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial (EC:1.1.1.41)
Alternative name(s):
IDH-I
Isocitric dehydrogenase 1
NAD(+)-specific ICDH 1
Gene namesi
Name:IDH1
Ordered Locus Names:At4g35260
ORF Names:F23E12.180
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G35260.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionSequence AnalysisAdd
BLAST
Chaini26 – 367342Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrialPRO_0000271287Add
BLAST

Proteomic databases

PaxDbiQ8LFC0.
PRIDEiQ8LFC0.

Expressioni

Tissue specificityi

Ubiquitous. Predominantly expressed in roots, stems and leaves.1 Publication

Gene expression databases

GenevestigatoriQ8LFC0.

Interactioni

Subunit structurei

Heterooligomer of catalytic and regulatory subunits.

Protein-protein interaction databases

BioGridi14961. 4 interactions.
IntActiQ8LFC0. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8LFC0.
SMRiQ8LFC0. Positions 40-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiQ8LFC0.
KOiK00030.
OMAiAMHAPIF.
PhylomeDBiQ8LFC0.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8LFC0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRRSLTLLK NLARNANGSG IQTRSVTYMP RPGDGAPRAV TLIPGDGIGP
60 70 80 90 100
LVTNAVEQVM EAMHAPIFFE KYDVHGEMSR VPPEVMESIR KNKVCLKGGL
110 120 130 140 150
KTPVGGGVSS LNVQLRKELD LFASLVNCFN LPGLPTRHEN VDIVVIRENT
160 170 180 190 200
EGEYAGLEHE VVPGVVESLK VITKFCSERI AKYAFEYAYL NNRKKVTAVH
210 220 230 240 250
KANIMKLADG LFLESCREVA KKYPSITYNE IIVDNCCMQL VAKPEQFDVM
260 270 280 290 300
VTPNLYGNLV ANTAAGIAGG TGVMPGGNVG ADHAVFEQGA SAGNVGKDKI
310 320 330 340 350
VLENKANPVA LLLSSAMMLR HLQFPSFADR LETAVKKVIA EGKCRTKDLG
360
GTSTTQEVVD AVIAKLD
Length:367
Mass (Da):39,627
Last modified:January 9, 2007 - v2
Checksum:i62DF327529961082
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741K → N in AAM61498. 1 PublicationCurated
Sequence conflicti331 – 3311L → P in AAC49964. (PubMed:9526501)Curated
Sequence conflicti339 – 3391I → T in AAC49964. (PubMed:9526501)Curated
Sequence conflicti344 – 3441C → F in AAM61498. 1 PublicationCurated
Sequence conflicti362 – 3621V → G in AAC49964. (PubMed:9526501)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81993 mRNA. Translation: AAC49964.1.
U82203 Genomic DNA. Translation: AAC49966.1.
AL022604 Genomic DNA. Translation: CAA18743.1.
AL161587 Genomic DNA. Translation: CAB80243.1.
CP002687 Genomic DNA. Translation: AEE86486.1.
AF428360 mRNA. Translation: AAL16290.1.
AY049260 mRNA. Translation: AAK83602.1.
AY129494 mRNA. Translation: AAM91080.1.
AY084937 mRNA. Translation: AAM61498.1.
PIRiT06131.
RefSeqiNP_195252.1. NM_119692.2.
UniGeneiAt.22461.
At.74835.

Genome annotation databases

EnsemblPlantsiAT4G35260.1; AT4G35260.1; AT4G35260.
GeneIDi829679.
KEGGiath:AT4G35260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81993 mRNA. Translation: AAC49964.1 .
U82203 Genomic DNA. Translation: AAC49966.1 .
AL022604 Genomic DNA. Translation: CAA18743.1 .
AL161587 Genomic DNA. Translation: CAB80243.1 .
CP002687 Genomic DNA. Translation: AEE86486.1 .
AF428360 mRNA. Translation: AAL16290.1 .
AY049260 mRNA. Translation: AAK83602.1 .
AY129494 mRNA. Translation: AAM91080.1 .
AY084937 mRNA. Translation: AAM61498.1 .
PIRi T06131.
RefSeqi NP_195252.1. NM_119692.2.
UniGenei At.22461.
At.74835.

3D structure databases

ProteinModelPortali Q8LFC0.
SMRi Q8LFC0. Positions 40-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 14961. 4 interactions.
IntActi Q8LFC0. 4 interactions.

Proteomic databases

PaxDbi Q8LFC0.
PRIDEi Q8LFC0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G35260.1 ; AT4G35260.1 ; AT4G35260 .
GeneIDi 829679.
KEGGi ath:AT4G35260.

Organism-specific databases

GeneFarmi 4364. 439.
TAIRi AT4G35260.

Phylogenomic databases

eggNOGi COG0473.
HOGENOMi HOG000021113.
InParanoidi Q8LFC0.
KOi K00030.
OMAi AMHAPIF.
PhylomeDBi Q8LFC0.

Gene expression databases

Genevestigatori Q8LFC0.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11835. PTHR11835. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00175. mito_nad_idh. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [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.
    , 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. "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].
  6. "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.
  7. "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.
  8. "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.

Entry informationi

Entry nameiIDH1_ARATH
AccessioniPrimary (citable) accession number: Q8LFC0
Secondary accession number(s): O65501, P94015, Q7DM90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: October 1, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3