Arogenate dehydratase 3, chloroplastic precursor - Arabidopsis thaliana (Mouse-ear cress)

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Q9ZUY3 (AROD3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Arogenate dehydratase 3, chloroplastic
Short name=AtADT3
EC=4.2.1.91

Alternative name(s):
Prephenate dehydratase 1
Short name=AtPDT1

Gene names

Name:	ADT3
Synonyms:	PD1, PDT1
Ordered Locus Names:	At2g27820
ORF Names:	F15K20.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine. Together with GCR1 and GPA1, required for blue light-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Ref.7 Ref.8
Catalytic activity	L-arogenate = L-phenylalanine + H₂O + CO₂.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.
Subunit structure	May interact with GPA1.
Subcellular location	Plastid › chloroplast stroma Ref.7 Ref.9.
Tissue specificity	Expressed in roots, leaves, stems, flowers and siliques. Ref.8
Disruption phenotype	Lack of Phe and Tyr accumulation after blue light irradiation of etiolated seedlings. Ref.7
Miscellaneous	Has no detectable prehenate dehydratase activity.
Sequence similarities	Contains 1 prephenate dehydratase domain.
Caution	Was reported (Ref.7) to be a cytosolic prephenate dehydratase interacting with a G-protein alpha-subunit.
Biophysicochemical properties	Kinetic parameters: K_M=0.43 mM for arogenate Ref.8 V_max=5.17 pmol/sec/µg enzyme with arogenate as substrate

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine biosynthetic process Inferred from mutant phenotype Ref.7. Source: TAIR response to karrikin Inferred from expression pattern PubMed 20351290. Source: TAIR response to low fluence blue light stimulus by blue low-fluence system Inferred from mutant phenotype Ref.7. Source: TAIR tyrosine biosynthetic process Inferred from mutant phenotype Ref.7. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay Ref.9. Source: TAIR chloroplast stroma Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from mutant phenotype Ref.7. Source: TAIR
Molecular_function	arogenate dehydratase activity Inferred from direct assay Ref.8. Source: TAIR prephenate dehydratase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 24

Chloroplast Potential

Chain

25 – 424

400

Arogenate dehydratase 3, chloroplastic

PRO_0000373792

Regions

Domain

122 – 299

178

Prephenate dehydratase

Compositional bias

30 – 75

Ser-rich

Compositional bias

241 – 272

Ala-rich

Compositional bias

409 – 420

Poly-Ser

Experimental info

Sequence conflict

206

I → M in AAM65232. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZUY3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 52471CE9914FDA89
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FASTA

424

46,102

        10         20         30         40         50         60 
MRTLLPSHTP ATVTTAARRR HVIHCAGKRS DSFSINSSSS DWQSSCAILS SKVNSQEQSE 

        70         80         90        100        110        120 
SLSSNSNGSS SYHVSAVNGH NNGAGVSDLN LVPFNNNQSI QSKKPLSISD LSPAPMHGSN 

       130        140        150        160        170        180 
LRVAYQGVPG AYSEAAAGKA YPNCQAIPCD QFEVAFQAVE LWIADRAVLP VENSLGGSIH 

       190        200        210        220        230        240 
RNYDLLLRHR LHIVGEVQLP VHHCLIALPG VRKEFLTRVI SHPQGLAQCE HTLTKLGLNV 

       250        260        270        280        290        300 
AREAVDDTAG AAEFIAANNI RDTAAIASAR AAEIYGLEIL EDGIQDDASN VTRFVMLARE 

       310        320        330        340        350        360 
PIIPRTDRPF KTSIVFAHEK GTCVLFKVLS AFAFRNISLT KIESRPNHNV PIRLVDEANV 

       370        380        390        400        410        420 
GTAKHFEYMF YIDFEASMAE SRAQNALSEV QEFTSFLRVL GSYPMDMTSW SPSSSSSSSS 


TFSL

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References

	« Hide 'large scale' referencesShow '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 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C. Nature 402:761-768(1999) [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]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Arabidopsis ORF clones." Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-424. Strain: cv. Columbia.
[7]	"G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate dehydratase 1 are required for blue light-induced production of phenylalanine in etiolated Arabidopsis." Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S., Kaufman L.S. Plant Physiol. 140:844-855(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH GPA1.
[8]	"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.
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ411464 mRNA. Translation: ABD67750.1. AC005824 Genomic DNA. Translation: AAC73018.1. CP002685 Genomic DNA. Translation: AEC08050.1. AY087695 mRNA. Translation: AAM65232.1. BT025989 mRNA. Translation: ABG25078.1. AK229426 mRNA. Translation: BAF01286.1.
IPI	IPI00538715.
PIR	D84677.
RefSeq	NP_180350.1. NM_128342.2.
UniGene	At.38711.
3D structure databases
ProteinModelPortal	Q9ZUY3.
SMR	Q9ZUY3. Positions 120-403.
ModBase	Search...
Proteomic databases
PaxDb	Q9ZUY3.
PRIDE	Q9ZUY3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G27820.1; AT2G27820.1; AT2G27820.
GeneID	817329.
KEGG	ath:AT2G27820.
Organism-specific databases
TAIR	At2g27820.
Phylogenomic databases
eggNOG	COG0077.
HOGENOM	HOG000018970.
InParanoid	Q9ZUY3.
KO	K05359.
OMA	MFYIDFE.
PhylomeDB	Q9ZUY3.
ProtClustDB	PLN02317.
Enzyme and pathway databases
BRENDA	4.2.1.51. 399.
SABIO-RK	Q9ZUY3.
UniPathway	UPA00121; UER00344.
Gene expression databases
Genevestigator	Q9ZUY3.
Family and domain databases
InterPro	IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Pfam	PF00800. PDT. 1 hit. [Graphical view]
PROSITE	PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. 1 hit. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AROD3_ARATH

Accession

Primary (citable) accession number: Q9ZUY3
Secondary accession number(s): Q0WNL3, Q8LAP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents