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Q9SA96 (AROD1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arogenate dehydratase/prephenate dehydratase 1, chloroplastic
Short name=AtADT1
Short name=AtPDT1
EC=4.2.1.51
EC=4.2.1.91
Gene names
Name:ADT1
Synonyms:PDT1
Ordered Locus Names:At1g11790
ORF Names:F25C20.4
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length392 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.5

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

Plastid › chloroplast stroma Ref.6.

Tissue specificity

Expressed in roots, leaves, stems, flowers and siliques. Ref.5

Sequence similarities

Contains 1 ACT domain.

Contains 1 prephenate dehydratase domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.05 mM for arogenate Ref.5

KM=0.80 mM for prephenate

Vmax=31 pmol/sec/µg enzyme with arogenate as substrate

Vmax=0.28 pmol/sec/µg enzyme with prephenate as substrate

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Phenylalanine biosynthesis
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionLyase
   Technical termComplete proteome
Reference 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 functionamino acid binding

Inferred from electronic annotation. Source: InterPro

arogenate dehydratase activity

Inferred from direct assay Ref.5. Source: TAIR

prephenate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9SA96-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9SA96-2)

The sequence of this isoform differs from the canonical sequence as follows:
     325-341: IESRPQRRRPLRVVDGS → VSSKEKLDPIISNSFQK
     342-392: Missing.
Note: Derived from EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Chloroplast Potential
Chain49 – 392344Arogenate dehydratase/prephenate dehydratase 1, chloroplastic
PRO_0000373790

Regions

Domain107 – 282176Prephenate dehydratase
Domain295 – 37884ACT

Natural variations

Alternative sequence325 – 34117IESRP…VVDGS → VSSKEKLDPIISNSFQK in isoform 2.
VSP_037227
Alternative sequence342 – 39251Missing in isoform 2.
VSP_037228

Experimental info

Sequence conflict1461L → H in AAM10090. Ref.4
Sequence conflict1461L → H in AAK68844. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 1B1468660C420BCE

FASTA39243,605
        10         20         30         40         50         60 
MALRCFPIWV CPQTTHHRSP LMGLAEFDAD KRRRFCLWEC SSSASQRAVT AIEGEIPFSR 

        70         80         90        100        110        120 
ELKKSSDELG LTQETQSLSF HRDLSMLPKP LTANSLYSSD GDDSKVRISF QGIPGAYSET 

       130        140        150        160        170        180 
AALKAFPNCE TVPCEQFEAA FQAVELWLVD KAVLPIENSV GGSIHRNYDL LLRHRLHIVQ 

       190        200        210        220        230        240 
EVHLPVNHCL LGVPGVKKED IKCVLSHPQA LDQCVNSLNN LGIQRISAKD TATAAQTVSS 

       250        260        270        280        290        300 
SGKIDVGAIA SVRAANIYGL DILAENIQDD VNNVTRFLIL AREPMIPRTD RPYKTSIVFS 

       310        320        330        340        350        360 
LEEGPGVLFK ALAVFALRSI NLSKIESRPQ RRRPLRVVDG SNNGSAKYFD YLFYIDFEAS 

       370        380        390 
MADTRAQHAL GHLQEFASFI RILGCYPMDL VR

« Hide

Isoform 2 [UniParc].

Checksum: F5505FB14FE6BB7B
Show »

FASTA34137,614

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] (ISOFORM 1).
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]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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"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.
[6]"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		DQ411466 mRNA. Translation: ABD67752.1.
AC007296 Genomic DNA. Translation: AAD30242.1.
CP002684 Genomic DNA. Translation: AEE28786.1.
CP002684 Genomic DNA. Translation: AEE28787.1.
AY042904 mRNA. Translation: AAK68844.1.
AY081528 mRNA. Translation: AAM10090.1.
IPIIPI00516602.
IPI00656740.
PIRA86252.
RefSeqNP_001031024.1. NM_001035947.1.
NP_172644.1. NM_101051.2.
UniGeneAt.11172.

3D structure databases

ProteinModelPortalQ9SA96.
SMRQ9SA96. Positions 106-389.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9SA96.

Proteomic databases

PRIDEQ9SA96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G11790.1; AT1G11790.1; AT1G11790.
GeneID837725.
GenomeReviewsGene locus AT1G11790 in contig CT485782_GR.
KEGGath:AT1G11790.
NMPDRfig|3702.1.peg.1436.

Organism-specific databases

TAIRAt1g11790.

Phylogenomic databases

eggNOGKOG2797.
GeneTreeEPGT00050000005675.
InParanoidQ9SA96.
OMAIPIENSV.
PhylomeDBQ9SA96.
ProtClustDBPLN02317.

Enzyme and pathway databases

BRENDA4.2.1.91. 399.

Gene expression databases

GenevestigatorQ9SA96.

Family and domain databases

InterProIPR002912. ACT-bd.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF00800. 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 nameAROD1_ARATH
AccessionPrimary (citable) accession number: Q9SA96
Secondary accession number(s): Q2V4P0, Q94B20
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: September 21, 2011
This is version 71 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents