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Reviewed, UniProtKB/Swiss-Prot Q9SGD6 (AROD6_ARATH)

Last modified February 9, 2010. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arogenate dehydratase/prephenate dehydratase 6, chloroplastic
      Short name=AtADT6
      Short name=AtPDT6
    EC=4.2.1.91
    EC=4.2.1.51
Gene names
Name: ADT6
Synonyms: PDT6
Ordered Locus Names: At1g08250
ORF Names: T23G18.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Ref.4

Catalytic activity

L-arogenate = L-phenylalanine + H2O + CO2.

Prephenate = phenylpyruvate + H2O + CO2.

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.

Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.

Subcellular location

Plastidchloroplast stroma Ref.5.

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques. Ref.4

Sequence similarities

Contains 1 prephenate dehydratase domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.58 mM for arogenate

KM=2.44 mM for prephenate

Vmax=42.61 pmol/sec/µg enzyme with arogenate as substrate

Vmax=0.4 pmol/sec/µg enzyme with prephenate as substrate

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Phenylalanine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-phenylalanine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarogenate dehydratase activity Ref.4

Inferred from direct assay. Source: TAIR

prephenate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Chloroplast Potential
Chain45 – 413369Arogenate dehydratase/prephenate dehydratase 6, chloroplastic
PRO_0000373795

Regions

Domain117 – 294178Prephenate dehydratase

Sequences

Sequence LengthMass (Da)Tools
Q9SGD6-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 70099DC47A932022

FASTA41344,802
        10         20         30         40         50         60 
MKALSSSSPI LGASQPATAT ALIARSGRSE WQSSCAILTS KVISQEESES LPVPPVSGGV 

        70         80         90        100        110        120 
DHLNGHNSAA ARVPGMNLVP IEKSDSNPLV PQHRHNPLKP LSMTDLSPAP MHGSNLRVAY 

       130        140        150        160        170        180 
QGVPGAYSEA AAGKAYPNCQ AIPCDQFEVA FQAVELWIAD RAVLPVENSL GGSIHRNYDL 

       190        200        210        220        230        240 
LLRHRLHIVG EVQLPVHHCL LALPGVRKEF LTRVISHPQG LAQCEHTLTK LGLNVAREAV 

       250        260        270        280        290        300 
DDTAGAAEFI ASNNLRDTAA IASARAAEIY GLEILEDGIQ DDVSNVTRFV MLAREPIIPR 

       310        320        330        340        350        360 
TDRPFKTSIV FAHEKGTSVL FKVLSAFAFR DISLTKIESR PNHNRPIRVV DDANVGTAKH 

       370        380        390        400        410 
FEYMFYVDFE ASMAEARAQN ALAEVQEFTS FLRVLGSYPM DMTPWSPTSS TSS 

« Hide

References

« Hide 'large scale' references
[1]Matringe M., Grisollet D., Rippert P.
Submitted (FEB-2006) 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: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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.
[4]"Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and characterization of arogenate dehydratases."
Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D., Anterola A.M., Moog-Anterola F.A., Hood R.L., Kohalmi S.E., Bernards M.A., Kang C., Davin L.B., Lewis N.G.
J. Biol. Chem. 282:30827-30835(2007) [PubMed: 17726025] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis."
Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M.
Plant Physiol. 149:1251-1260(2009) [PubMed: 19136569] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ411468 mRNA. Translation: ABD67754.1.
AC011438 Genomic DNA. Translation: AAF18250.1.
AY056290 mRNA. Translation: AAL07139.1.
AY091181 mRNA. Translation: AAM14120.1.
IPIIPI00523853.
PIRE86216.
RefSeqNP_563809.1.
UniGeneAt.16611

3D structure databases

SMRQ9SGD6. Positions 115-401.
ModBaseSearch...

Proteomic databases

PRIDEQ9SGD6.

Genome annotation databases

GeneID837345.
GenomeReviewsGene locus AT1G08250 in contig CT485782_GR.
KEGGath:AT1G08250.
NMPDRfig|3702.1.peg.1031.

Organism-specific databases

TAIRAt1g08250.

Phylogenomic databases

eggNOGKOG2797.
HOGENOMHBG693866.
InParanoidQ9SGD6.
OMANANIERI.
PhylomeDBQ9SGD6.

Gene expression databases

ArrayExpressQ9SGD6.
GenevestigatorQ9SGD6.

Family and domain databases

InterProIPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamPF00800. PDT. 1 hit.
[Graphical view]
PROSITEPS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROD6_ARATH
AccessionPrimary (citable) accession number: Q9SGD6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents