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Protein

Arogenate dehydratase/prephenate dehydratase 1, chloroplastic

Gene

ADT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=3.05 mM for arogenate1 Publication
  2. KM=0.80 mM for prephenate1 Publication
  1. Vmax=31 pmol/sec/µg enzyme with arogenate as substrate1 Publication
  2. Vmax=0.28 pmol/sec/µg enzyme with prephenate as substrate1 Publication

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-phenylalanine from L-arogenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Arogenate dehydratase/prephenate dehydratase 1, chloroplastic (ADT1), Arogenate dehydratase 5, chloroplastic (ADT5), Arogenate dehydratase 4, chloroplastic (ADT4), Arogenate dehydratase 3, chloroplastic (ADT3), Arogenate dehydratase/prephenate dehydratase 2, chloroplastic (ADT2), Arogenate dehydratase/prephenate dehydratase 6, chloroplastic (ADT6)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-phenylalanine from L-arogenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Arogenate dehydratase/prephenate dehydratase 1, chloroplastic (ADT1), Arogenate dehydratase/prephenate dehydratase 2, chloroplastic (ADT2), Arogenate dehydratase/prephenate dehydratase 6, chloroplastic (ADT6)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylpyruvate from prephenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciARA:AT1G11790-MONOMER.
ARA:GQT-181-MONOMER.
BRENDAi4.2.1.91. 399.
SABIO-RKQ9SA96.
UniPathwayiUPA00121; UER00344.
UPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Arogenate dehydratase/prephenate dehydratase 1, chloroplastic (EC:4.2.1.51, EC:4.2.1.91)
Short name:
AtADT1
Short name:
AtPDT1
Gene namesi
Name:ADT1
Synonyms:PDT1
Ordered Locus Names:At1g11790
ORF Names:F25C20.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G11790.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848ChloroplastSequence analysisAdd
BLAST
Chaini49 – 392344Arogenate dehydratase/prephenate dehydratase 1, chloroplasticPRO_0000373790Add
BLAST

Proteomic databases

PaxDbiQ9SA96.
PRIDEiQ9SA96.

Expressioni

Tissue specificityi

Expressed in roots, leaves, stems, flowers and siliques.1 Publication

Gene expression databases

GenevisibleiQ9SA96. AT.

Interactioni

Protein-protein interaction databases

BioGridi22965. 1 interaction.
STRINGi3702.AT1G11790.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SA96.
SMRiQ9SA96. Positions 108-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 282176Prephenate dehydratasePROSITE-ProRule annotationAdd
BLAST
Domaini296 – 38792ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2797. Eukaryota.
COG0077. LUCA.
HOGENOMiHOG000018970.
InParanoidiQ9SA96.
KOiK05359.
OMAiREPMIPR.
PhylomeDBiQ9SA96.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9SA96-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALRCFPIWV CPQTTHHRSP LMGLAEFDAD KRRRFCLWEC SSSASQRAVT
60 70 80 90 100
AIEGEIPFSR ELKKSSDELG LTQETQSLSF HRDLSMLPKP LTANSLYSSD
110 120 130 140 150
GDDSKVRISF QGIPGAYSET AALKAFPNCE TVPCEQFEAA FQAVELWLVD
160 170 180 190 200
KAVLPIENSV GGSIHRNYDL LLRHRLHIVQ EVHLPVNHCL LGVPGVKKED
210 220 230 240 250
IKCVLSHPQA LDQCVNSLNN LGIQRISAKD TATAAQTVSS SGKIDVGAIA
260 270 280 290 300
SVRAANIYGL DILAENIQDD VNNVTRFLIL AREPMIPRTD RPYKTSIVFS
310 320 330 340 350
LEEGPGVLFK ALAVFALRSI NLSKIESRPQ RRRPLRVVDG SNNGSAKYFD
360 370 380 390
YLFYIDFEAS MADTRAQHAL GHLQEFASFI RILGCYPMDL VR
Length:392
Mass (Da):43,605
Last modified:May 1, 2000 - v1
Checksum:i1B1468660C420BCE
GO
Isoform 2 (identifier: Q9SA96-2) [UniParc]FASTAAdd to basket

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

Note: Derived from EST data.
Show »
Length:341
Mass (Da):37,614
Checksum:iF5505FB14FE6BB7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461L → H in AAM10090 (PubMed:14593172).Curated
Sequence conflicti146 – 1461L → H in AAK68844 (PubMed:14593172).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei325 – 34117IESRP…VVDGS → VSSKEKLDPIISNSFQK in isoform 2. CuratedVSP_037227Add
BLAST
Alternative sequencei342 – 39251Missing in isoform 2. CuratedVSP_037228Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA86252.
RefSeqiNP_001031024.1. NM_001035947.1. [Q9SA96-2]
NP_172644.1. NM_101051.2. [Q9SA96-1]
UniGeneiAt.11172.

Genome annotation databases

EnsemblPlantsiAT1G11790.1; AT1G11790.1; AT1G11790. [Q9SA96-1]
GeneIDi837725.
KEGGiath:AT1G11790.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA86252.
RefSeqiNP_001031024.1. NM_001035947.1. [Q9SA96-2]
NP_172644.1. NM_101051.2. [Q9SA96-1]
UniGeneiAt.11172.

3D structure databases

ProteinModelPortaliQ9SA96.
SMRiQ9SA96. Positions 108-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22965. 1 interaction.
STRINGi3702.AT1G11790.1.

Proteomic databases

PaxDbiQ9SA96.
PRIDEiQ9SA96.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G11790.1; AT1G11790.1; AT1G11790. [Q9SA96-1]
GeneIDi837725.
KEGGiath:AT1G11790.

Organism-specific databases

TAIRiAT1G11790.

Phylogenomic databases

eggNOGiKOG2797. Eukaryota.
COG0077. LUCA.
HOGENOMiHOG000018970.
InParanoidiQ9SA96.
KOiK05359.
OMAiREPMIPR.
PhylomeDBiQ9SA96.

Enzyme and pathway databases

UniPathwayiUPA00121; UER00344.
UPA00121; UER00345.
BioCyciARA:AT1G11790-MONOMER.
ARA:GQT-181-MONOMER.
BRENDAi4.2.1.91. 399.
SABIO-RKQ9SA96.

Miscellaneous databases

PROiQ9SA96.

Gene expression databases

GenevisibleiQ9SA96. AT.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF00800. PDT. 1 hit.
[Graphical view]
PROSITEiPS51671. ACT. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiAROD1_ARATH
AccessioniPrimary (citable) accession number: Q9SA96
Secondary accession number(s): Q2V4P0, Q94B20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.