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UniProtKB/Swiss-Prot entry Q8LFC0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IDH1_ARATH
Primary accession number Q8LFC0
Secondary accession numbers O65501 P94015 Q7DM90
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on January 9, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 35)
Name and origin of the protein
Protein name Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial [Precursor]
Synonyms EC 1.1.1.41
Isocitric dehydrogenase 1
NAD(+)-specific ICDH 1
IDH-I
Gene name
Name: IDH1
OrderedLocusNames: At4g35260
ORFNames: F23E12.180
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
STRAIN=cv. Columbia;
DOI=10.1023/A:1005923410940; PubMed=9526501 [NCBI, ExPASy, EBI, Israel, Japan]
Behal R.H., Oliver D.J.;
"NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana. Characterization of two closely related subunits.";
Plant Mol. Biol. 36:691-698(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[6]
GENE FAMILY.
DOI=10.1016/j.plantsci.2003.12.012; AGRICOLA=IND43633651
Lin M., Behal R.H., Oliver D.J.;
"Characterization of a mutation in the IDH-II subunit of the NAD(+)-dependent isocitrate dehydrogenase from Arabidopsis thaliana.";
Plant Sci. 166:983-988(2004).
[7]
TISSUE SPECIFICITY.
DOI=10.1093/pcp/pcj030; PubMed=16527867 [NCBI, ExPASy, EBI, Israel, Japan]
Lemaitre T., Hodges M.;
"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.";
Plant Cell Physiol. 47:634-643(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U81993; AAC49964.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U82203; AAC49966.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022604; CAA18743.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161587; CAB80243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428360; AAL16290.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY049260; AAK83602.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY129494; AAM91080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084937; AAM61498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T06131; T06131.
RefSeq NP_195252.1; -.
UniGene At.22461
3D structure databases
HSSP P39126; 1HQS. [HSSP ENTRY / PDB]
ModBase Q8LFC0.
Organism-specific databases
GeneFarm 4364; 439.
TAIR At4g35260; -.
Family and domain databases
InterPro IPR004434; IsoCit_DHase_NAD_mit.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00175; mito_nad_idh; 1.
PROSITE PS00470; IDH_IMDH; FALSE_NEG.
BLOCKS Q8LFC0.
Genome annotation databases
GeneID 829679; -.
GenomeReviews CT486007_GR; AT4G35260.
KEGG ath:AT4G35260; -.
NMPDR fig|3702.1.peg.21603; -.
Other
ProtoNet Q8LFC0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Manganese; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    25  25     Mitochondrion (Potential). 
CHAIN   26   367  342     Isocitrate dehydrogenase [NAD] regulatory subunit 1, mitochondrial. PRO_0000271287
METAL   234   234        Magnesium or manganese (By similarity). 
BINDING   116   116        Substrate (By similarity). 
BINDING   147   147        Substrate (By similarity). 
BINDING   234   234        Substrate (By similarity). 
SITE   154   154  1     Critical for catalysis (By similarity). 
SITE   201   201  1     Critical for catalysis (By similarity). 
CONFLICT   174   174        K -> N (in Ref. 4; AAM61498). 
CONFLICT   331   331        L -> P (in Ref. 1; AAC49964). 
CONFLICT   339   339        I -> T (in Ref. 1; AAC49964). 
CONFLICT   344   344        C -> F (in Ref. 4; AAM61498). 
CONFLICT   362   362        V -> G (in Ref. 1; AAC49964). 
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 39627 Da [This is the MW of the unprocessed precursor] CRC64: 62DF327529961082 [This is a checksum on the sequence]
        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 

Q8LFC0 in FASTA format

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