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P29976 (AROF_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic

EC=2.5.1.54
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 1
DAHP synthase 1
Phospho-2-keto-3-deoxyheptonate aldolase 1
Gene names
Name:DHS1
Ordered Locus Names:At4g39980
ORF Names:T5J17.150
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.

Subcellular location

Plastidchloroplast.

Induction

By pathogen infection and wounding.

Sequence similarities

Belongs to the class-II DAHP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Chloroplast Potential
Chain53 – 525473Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic
PRO_0000002298

Experimental info

Sequence conflict429 – 4302AP → ST in AAA32784. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29976 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 13CA141A3C71D9E6

FASTA52557,979
        10         20         30         40         50         60 
MALSNASSLS TRSIYGGDLS HRPSNRQSSF TFHPAVNTKP KSVNLVTAVH AAEPARNAVS 

        70         80         90        100        110        120 
VKESVASSSS GALKWTPESW KLKKALQLPD YPNANELESV LKTIEAFPPI VFAGEARNLE 

       130        140        150        160        170        180 
ERLADAAVGK AFLLQGGDCA ESFKEFNATN IRDTFRVLLQ MSIVLTFGGQ VPVIKVGRMA 

       190        200        210        220        230        240 
GQFAKPRSDA FEEKDGVKLP SYKGDNINGD TFDEKSRIPD PNRMIRAYTQ SAATLNLLRA 

       250        260        270        280        290        300 
FATGGYAAIQ RVTQWNLDFV EQSEQADRYQ ELANRVDEAL GFMSACGLGT DHPLMTTTDF 

       310        320        330        340        350        360 
YTSHECLLLP YEQSLTRLDS TSGLYYDCSA HMVWCGERTR QLDGAHVEFL RGIANPLGIK 

       370        380        390        400        410        420 
VSNKMDPFEL VKLVEILNPN NKPGRITVIV RMGAENMRVK LPHLIRAVRR SGQIVTWVCD 

       430        440        450        460        470        480 
PMHGNTIKAP CGLKTRAFDS ILAEVRAFLD VHEQEGSHAG GIHLEMTGQN VTECIGGSRT 

       490        500        510        520 
VTYDDLSSRY HTHCDPRLNA SQSLELAFIV AERLRKRRTG SQRVS 

« Hide

References

« Hide 'large scale' references
[1]"Differential induction of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase genes in Arabidopsis thaliana by wounding and pathogenic attack."
Keith B., Dong X.N., Ausubel F.M., Fink G.R.
Proc. Natl. Acad. Sci. U.S.A. 88:8821-8825(1991) [PubMed: 1681544] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. expand/collapse author list , 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: 10617198] [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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74819 mRNA. Translation: AAA32784.1.
AL035708 Genomic DNA. Translation: CAB38911.1.
AL161596 Genomic DNA. Translation: CAB80661.1.
CP002687 Genomic DNA. Translation: AEE87148.1.
AY090349 mRNA. Translation: AAL91255.1.
AY140052 mRNA. Translation: AAM98193.1.
BT000821 mRNA. Translation: AAN33196.1.
IPIIPI00521831.
PIRA41370.
T06104.
RefSeqNP_195708.1. NM_120162.4.
UniGeneAt.23161.

3D structure databases

ProteinModelPortalP29976.
SMRP29976. Positions 73-516.
ModBaseSearch...

Protein-protein interaction databases

IntActP29976. 1 interaction.
STRINGP29976.

Proteomic databases

PRIDEP29976.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G39980.1; AT4G39980.1; AT4G39980.
GeneID830159.
GenomeReviewsGene locus AT4G39980 in contig CT486007_GR.
KEGGath:AT4G39980.
NMPDRfig|3702.1.peg.22145.

Organism-specific databases

TAIRAt4g39980.

Phylogenomic databases

eggNOGeuNOG04328.
GeneTreeEPGT00050000007510.
HOGENOMHBG292577.
InParanoidP29976.
OMAHAWNQDF.
PhylomeDBP29976.
ProtClustDBPLN02291.

Gene expression databases

ArrayExpressP29976.
GenevestigatorP29976.
GermOnlineAT4G39980. Arabidopsis thaliana.

Family and domain databases

InterProIPR002480. DAHP_synth_2.
[Graphical view]
KOK01626.
PANTHERPTHR21337. DAHP_synth_2. 1 hit.
PfamPF01474. DAHP_synth_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01358. DAHP_synth_II. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAROF_ARATH
AccessionPrimary (citable) accession number: P29976
Secondary accession number(s): Q9SMQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2002
Last modified: December 14, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families