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Q9SRZ6 (ICDHC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 110. 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:
Cytosolic isocitrate dehydrogenase [NADP]

EC=1.1.1.42
Gene names
Name:CICDH
Ordered Locus Names:At1g65930
ORF Names:F12P19.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May supply 2-oxoglutarate for amino acid biosynthesis and ammonia assimilation via the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway. May be involved in the production of NADPH to promote redox signaling or homeostasis in response to oxidative stress. Ref.6

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subcellular location

Cytoplasmcytosol.

Disruption phenotype

Slight reduction in plant growth. Constitutive expression of pathogenesis-related genes and enhanced resistance to the bacterial pathogen P.syringae pv. tomato. Ref.6

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
   Biological processPlant defense
Stress response
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNADP metabolic process

Inferred from mutant phenotype Ref.6. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype Ref.6. Source: TAIR

isocitrate metabolic process

Inferred from mutant phenotype Ref.6. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

response to zinc ion

Inferred from expression pattern PubMed 19880396. Source: TAIR

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 20061580. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

copper ion binding

Inferred from direct assay PubMed 16526091. Source: TAIR

isocitrate dehydrogenase (NADP+) activity

Inferred from mutant phenotype Ref.6. Source: TAIR

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Cytosolic isocitrate dehydrogenase [NADP]
PRO_0000421963

Regions

Nucleotide binding77 – 793NADP By similarity
Nucleotide binding310 – 3156NADP By similarity
Region96 – 1027Substrate binding By similarity

Sites

Metal binding2521Magnesium or manganese By similarity
Metal binding2751Magnesium or manganese By similarity
Binding site791Substrate By similarity
Binding site841NADP By similarity
Binding site1111Substrate By similarity
Binding site1341Substrate By similarity
Binding site2601NADP By similarity
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1411Critical for catalysis By similarity
Site2121Critical for catalysis By similarity

Experimental info

Sequence conflict1811A → V in CAD24782. Ref.1
Sequence conflict2621E → K in AAM65674. Ref.5
Sequence conflict2801F → L in CAD24782. Ref.1
Sequence conflict3021T → S in CAD24782. Ref.1
Sequence conflict3221G → A in AAM65674. Ref.5
Sequence conflict3951E → D in AAM13090. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9SRZ6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6CC3CA11AB631D28

FASTA41045,746
        10         20         30         40         50         60 
MAFEKIKVAN PIVEMDGDEM TRVIWKSIKD KLITPFVELD IKYFDLGLPH RDATDDKVTI 

        70         80         90        100        110        120 
ESAEATKKYN VAIKCATITP DEGRVTEFGL KQMWRSPNGT IRNILNGTVF REPIICKNVP 

       130        140        150        160        170        180 
KLVPGWTKPI CIGRHAFGDQ YRATDAVIKG PGKLTMTFEG KDGKTETEVF TFTGEGGVAM 

       190        200        210        220        230        240 
AMYNTDESIR AFADASMNTA YEKKWPLYLS TKNTILKKYD GRFKDIFQEV YEASWKSKYD 

       250        260        270        280        290        300 
AAGIWYEHRL IDDMVAYALK SEGGYVWACK NYDGDVQSDF LAQGFGSLGL MTSVLVCPDG 

       310        320        330        340        350        360 
KTIEAEAAHG TVTRHFRVHQ KGGETSTNSI ASIFAWTRGL AHRAKLDDNA KLLDFTEKLE 

       370        380        390        400        410 
AACVGTVESG KMTKDLALII HGSKLSRDTY LNTEEFIDAV AAELKERLNA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a full lenght cDNA encoding for NADP+-isocitrate dehydrogenase from Arabidopsis thaliana."
Pistelli L., De Bellis L., Alpi A., Gonzali S.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(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]"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]"Cytosolic NADP-dependent isocitrate dehydrogenase contributes to redox homeostasis and the regulation of pathogen responses in Arabidopsis leaves."
Mhamdi A., Mauve C., Gouia H., Saindrenan P., Hodges M., Noctor G.
Plant Cell Environ. 33:1112-1123(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ437268 mRNA. Translation: CAD24782.1.
AC009513 Genomic DNA. Translation: AAF06054.1.
CP002684 Genomic DNA. Translation: AEE34442.1.
AF419575 mRNA. Translation: AAL31907.1.
AY045631 mRNA. Translation: AAK73989.1.
AY093091 mRNA. Translation: AAM13090.1.
AY097340 mRNA. Translation: AAM19856.1.
BT002400 mRNA. Translation: AAO00760.1.
AY088129 mRNA. Translation: AAM65674.1.
PIRF96683.
RefSeqNP_176768.1. NM_105265.4.
UniGeneAt.24713.

3D structure databases

ProteinModelPortalQ9SRZ6.
SMRQ9SRZ6. Positions 5-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9SRZ6. 1 interaction.
STRING3702.AT1G65930.1-P.

Proteomic databases

PRIDEQ9SRZ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65930.1; AT1G65930.1; AT1G65930.
GeneID842905.
KEGGath:AT1G65930.

Organism-specific databases

TAIRAT1G65930.

Phylogenomic databases

InParanoidQ9SRZ6.
KOK00031.
OMANEHYVIT.
PhylomeDBQ9SRZ6.

Enzyme and pathway databases

BioCycMetaCyc:AT1G65930-MONOMER.

Gene expression databases

ArrayExpressQ9SRZ6.
GenevestigatorQ9SRZ6.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERPTHR11822. PTHR11822. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsTIGR00127. nadp_idh_euk. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameICDHC_ARATH
AccessionPrimary (citable) accession number: Q9SRZ6
Secondary accession number(s): Q8L9Z4, Q8RWH2, Q8RYD5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 110 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