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Q9SRZ6 (Q9SRZ6_ARATH) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 90. Feed History...

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

Names and origin

Protein namesRecommended name:
Isocitrate dehydrogenase [NADP] PIRNR PIRNR000108
EC=1.1.1.42 PIRNR PIRNR000108
Gene names
Name:F12P19.10 EMBL AAF06054.1
Synonyms:cICDH EMBL AEE34442.1
Ordered Locus Names:At1g65930 TAIR At1g65930 EMBL AAO00760.1
ORF Names:AT1G65930 EMBL AEE34442.1
OrganismArabidopsis thaliana (Mouse-ear cress) EMBL AAF06054.1
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

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

General annotation (Comments)

Catalytic activity

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. PIRNR PIRNR000108

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity. PIRNR PIRNR000108 PIRSR PIRSR000108-3

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. RuleBase RU004443 PIRNR PIRNR000108

Ontologies

Keywords
   Biological processTricarboxylic acid cycle PIRNR PIRNR000108
   LigandMagnesium PIRNR PIRNR000108 PIRSR PIRSR000108-3
Manganese PIRNR PIRNR000108 PIRSR PIRSR000108-3
Metal-binding PIRNR PIRNR000108 PIRSR PIRSR000108-3
NADP PIRNR PIRNR000108 PIRSR PIRSR000108-4
   Molecular functionOxidoreductase RuleBase RU004444 PIRNR PIRNR000108
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processNADP metabolic process

Inferred from mutant phenotype. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype. Source: TAIR

isocitrate metabolic process

Inferred from mutant phenotype. Source: TAIR

response to cadmium ion

Inferred from expression pattern. Source: TAIR

response to salt stress

Inferred from expression pattern. Source: TAIR

response to zinc ion

Inferred from expression pattern. Source: TAIR

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentapoplast

Inferred from direct assay. Source: TAIR

chloroplast stroma

Inferred from direct assay. Source: TAIR

cytosol

Inferred from direct assay. Source: TAIR

plasma membrane

Inferred from direct assay. Source: TAIR

plasmodesma

Inferred from direct assay. Source: TAIR

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

copper ion binding

Inferred from direct assay. Source: TAIR

isocitrate dehydrogenase (NADP+) activity

Inferred from mutant phenotype. Source: TAIR

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding77 – 793NADP By similarity PIRSR PIRSR000108-4
Nucleotide binding310 – 3156NADP By similarity PIRSR PIRSR000108-4
Region96 – 1027Substrate binding By similarity PIRSR PIRSR000108-2

Sites

Metal binding2521Magnesium or manganese By similarity PIRSR PIRSR000108-3
Metal binding2751Magnesium or manganese By similarity PIRSR PIRSR000108-3
Binding site791Substrate By similarity PIRSR PIRSR000108-2
Binding site841NADP By similarity PIRSR PIRSR000108-4
Binding site1111Substrate By similarity PIRSR PIRSR000108-2
Binding site1341Substrate By similarity PIRSR PIRSR000108-2
Binding site2601NADP By similarity PIRSR PIRSR000108-4
Binding site3281NADP; via amide nitrogen and carbonyl oxygen By similarity PIRSR PIRSR000108-4
Site1411Critical for catalysis By similarity PIRSR PIRSR000108-1
Site2121Critical for catalysis By similarity PIRSR PIRSR000108-1

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]"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: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Arabidopsis cDNA clones."
Kim C.J., Chen H., Cheuk R., Koesema E., Meyers M.C., Banh J., Bowser L., Carninci P., Dale J.M., Gibson H.A., Goldsmith A.D., Hayashizaki Y., Ishida J., Jiang P.X., Jones T., Kamiya A., Karlin-Neumann G., Kawai J. expand/collapse author list , Lam B., Lee J.M., Lin J., Liu S.X., Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., Pham P.K., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Yamada K., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Arabidopsis ORF clones."
Kim C.J., Chen H., Cheuk R., Meyers M.C., Shinn P., Banh J., Bowser L., Carninci P., Chang E., Dale J.M., Goldsmith A.D., Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B. expand/collapse author list , Lee J.M., Lin J., Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Wu H.C., Yamada K., Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[4]"Arabidopsis cDNA clones."
Cheuk R., Chen H., Kim C.J., Koesema E., Meyers M.C., Banh J., Bowser L., Carninci P., Dale J.M., Goldsmith A.D., Hayashizaki Y., Ishida J., Jiang P.X., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B. expand/collapse author list , Lee J.M., Lin J., Liu S.X., Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., Pham P.K., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Yamada K., Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[6]Southwick A., Nguyen M., Tripp M., Palm C.J., Jones T., Wu T., Carninci P., Chen H., Cheuk R., Chan M.M., Chang C.H., Dale J.M., Deng J.M., Hayashizaki Y., Hsuan V.W., Lee J.M., Ishida J., Kamiya A. expand/collapse author list , Kawai J., Kim C.J., Narusaka M., Onodera C.S., Quach H.L., Sakurai T., Satou M., Seki M., Shinn P., Tang C.C., Toroumi M., Wong C., Wu H.C., Yamada K., Yu G., Yuan S., Shinozaki K., Ecker J., Theologis A., Davis R.W.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[7]"Arabidopsis thaliana chromosome 1 BAC F12P19 sequence."
Schwartz J.R., Yu G., Toriumi M., Lenz C., Liu S., Lee J.M., Li J., Gonzalez A., Liu A., Liu K., Sakano H., Vaysberg M., Chin C., Choi E., Chiou J., Altafi H., Araujo R., Brooks S. expand/collapse author list , Buehler E., Chao Q., Conn L., Conway A., Dunn P., Hansen N., Howng B., Huizar L., Johnson-Hopson C., Khan S., Kim C., Lam B., Nguyen M., Palm C., Rowley D., Shinn P., Southwick A., Tambunga G., Walker M., Davis R.W., Ecker J.R., Federspiel N.A., Theologis A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC009513 Genomic DNA. Translation: AAF06054.1.
AY045631 mRNA. Translation: AAK73989.1.
AF419575 mRNA. Translation: AAL31907.1.
AY097340 mRNA. Translation: AAM19856.1.
BT002400 mRNA. Translation: AAO00760.1.
CP002684 Genomic DNA. Translation: AEE34442.1.
IPIIPI00539206.
PIRF96683.
RefSeqNP_176768.1. NM_105265.4.
UniGeneAt.24713.

3D structure databases

HSSPHSSP built from PDB template 1LWD based on UniProtKB P33198.
ProteinModelPortalQ9SRZ6.
SMRQ9SRZ6. Positions 2-408.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9SRZ6. 1 interaction.
STRINGQ9SRZ6.

Proteomic databases

PRIDEQ9SRZ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65930.1; AT1G65930.1; AT1G65930.
GeneID842905.
KEGGath:AT1G65930.
NMPDRfig|3702.1.peg.6015.

Organism-specific databases

TAIRAt1g65930.

Phylogenomic databases

GeneTreeEPGT00050000007928.
InParanoidQ9SRZ6.
OMATPDEARM.
PhylomeDBQ9SRZ6.
ProtClustDBPLN00103.

Gene expression databases

GenevestigatorQ9SRZ6.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP_euk-typ.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK00031.
PANTHERPTHR11822. IDH_NADP_euk. 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 nameQ9SRZ6_ARATH
AccessionPrimary (citable) accession number: Q9SRZ6
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info