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Q9SLK0 (ICDHX_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. 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:
Peroxisomal isocitrate dehydrogenase [NADP]

EC=1.1.1.42
Gene names
Name:ICDH
Ordered Locus Names:At1g54340
ORF Names:F20D21.16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in response to oxidative stresses By similarity.

Catalytic activity

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

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Subcellular location

Peroxisome Ref.5 Ref.6.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Peroxisomal isocitrate dehydrogenase [NADP]
PRO_0000421962

Regions

Nucleotide binding77 – 793NADP By similarity
Nucleotide binding311 – 3166NADP By similarity
Region96 – 1027Substrate binding By similarity
Motif414 – 4163Peroxisomal targeting signal Probable

Sites

Metal binding2531Magnesium or manganese By similarity
Metal binding2761Magnesium or manganese By similarity
Binding site791Substrate By similarity
Binding site841NADP By similarity
Binding site1111Substrate By similarity
Binding site1341Substrate By similarity
Binding site2611NADP By similarity
Binding site3291NADP; via amide nitrogen and carbonyl oxygen By similarity
Site1411Critical for catalysis By similarity
Site2131Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9SLK0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EEAAAC9E5C6B2FA5

FASTA41647,234
        10         20         30         40         50         60 
MEFEKIKVIN PVVEMDGDEM TRVIWKFIKD KLIFPFLELD IKYFDLGLPN RDFTDDKVTI 

        70         80         90        100        110        120 
ETAEATLKYN VAIKCATITP DEARVREFGL KKMWRSPNGT IRNILNGTVF REPIICRNIP 

       130        140        150        160        170        180 
RLVPGWTKPI CIGRHAFGDQ YRATDLIVNE PGKLKLVFEP SGSSQKTEFE VFNFTGGGVA 

       190        200        210        220        230        240 
LAMYNTDESI RAFAESSMYT AYQKKWPLYL STKNTILKIY DGRFKDIFQE VYEANWRSKY 

       250        260        270        280        290        300 
EAAGIWYEHR LIDDMVAYAM KSEGGYVWAC KNYDGDVQSD FLAQGYGSLG MMTSVLVCPD 

       310        320        330        340        350        360 
GKTIEAEAAH GTVTRHYRVH QKGGETSTNS IASIFAWSRG LAHRAKLDSN AALLSYTEKL 

       370        380        390        400        410 
EAACMGTVES GKMTKDLALL IHGAKVRRDQ YVNTEEFIDA VAWELKRRLL GNNSRL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of cDNA encoding NADP-specific isocitrate dehydrogenase from Arabidopsis thaliana."
Kihara T., Ito N., Koyama H., Hara T.
Submitted (OCT-2000) 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]"Arabidopsis ORF clones."
Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms."
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.
Plant Cell 19:3170-3193(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-51, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with in vivo subcellular targeting verification indicates novel metabolic and regulatory functions of peroxisomes."
Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D., Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.
Plant Physiol. 150:125-143(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF316501 mRNA. Translation: AAK06592.1.
AC005287 Genomic DNA. Translation: AAD25614.1.
CP002684 Genomic DNA. Translation: AEE33082.1.
BT025983 mRNA. Translation: ABG25072.1.
PIRA96585.
RefSeqNP_175836.1. NM_104312.2.
UniGeneAt.11811.
At.37230.

3D structure databases

ProteinModelPortalQ9SLK0.
SMRQ9SLK0. Positions 4-409.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9SLK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G54340.1; AT1G54340.1; AT1G54340.
GeneID841875.
KEGGath:AT1G54340.

Organism-specific databases

TAIRAT1G54340.

Phylogenomic databases

HOGENOMHOG000019858.
InParanoidQ9SLK0.
KOK00031.
OMAEANWRSK.
PhylomeDBQ9SLK0.
ProtClustDBPLN00103.

Enzyme and pathway databases

BioCycARA:AT1G54340-MONOMER.

Gene expression databases

ArrayExpressQ9SLK0.
GenevestigatorQ9SLK0.

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 nameICDHX_ARATH
AccessionPrimary (citable) accession number: Q9SLK0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 102 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