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Database: UniProt
Entry: Q9ZUY3
LinkDB: Q9ZUY3
Original site: Q9ZUY3 
ID   AROD3_ARATH             Reviewed;         424 AA.
AC   Q9ZUY3; Q0WNL3; Q8LAP1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-OCT-2019, entry version 108.
DE   RecName: Full=Arogenate dehydratase 3, chloroplastic;
DE            Short=AtADT3;
DE            EC=4.2.1.91;
DE   AltName: Full=Prephenate dehydratase 1;
DE            Short=AtPDT1;
DE   Flags: Precursor;
GN   Name=ADT3; Synonyms=PD1, PDT1; OrderedLocusNames=At2g27820;
GN   ORFNames=F15K20.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Matringe M., Grisollet D., Rippert P.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-424.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION
RP   WITH GPA1.
RX   PubMed=16415218; DOI=10.1104/pp.105.071282;
RA   Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S.,
RA   Kaufman L.S.;
RT   "G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and
RT   prephenate dehydratase 1 are required for blue light-induced
RT   production of phenylalanine in etiolated Arabidopsis.";
RL   Plant Physiol. 140:844-855(2006).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17726025; DOI=10.1074/jbc.m702662200;
RA   Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D.,
RA   Anterola A.M., Moog-Anterola F.A., Hood R.L., Kohalmi S.E.,
RA   Bernards M.A., Kang C., Davin L.B., Lewis N.G.;
RT   "Phenylalanine biosynthesis in Arabidopsis thaliana. Identification
RT   and characterization of arogenate dehydratases.";
RL   J. Biol. Chem. 282:30827-30835(2007).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19136569; DOI=10.1104/pp.108.130070;
RA   Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M.;
RT   "Tyrosine and phenylalanine are synthesized within the plastids in
RT   Arabidopsis.";
RL   Plant Physiol. 149:1251-1260(2009).
CC   -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC       chorismate pathway into phenylalanine. Together with GCR1 and
CC       GPA1, required for blue light-mediated synthesis of phenylpyruvate
CC       and subsequently of phenylalanine (Phe), in etiolated seedlings.
CC       {ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:17726025}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arogenate = CO2 + H2O + L-phenylalanine;
CC         Xref=Rhea:RHEA:12536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58095, ChEBI:CHEBI:58180;
CC         EC=4.2.1.91;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.43 mM for arogenate {ECO:0000269|PubMed:17726025};
CC         Vmax=5.17 pmol/sec/ug enzyme with arogenate as substrate
CC         {ECO:0000269|PubMed:17726025};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from L-arogenate: step 1/1.
CC   -!- SUBUNIT: May interact with GPA1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:19136569}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:17726025}.
CC   -!- DISRUPTION PHENOTYPE: Lack of Phe and Tyr accumulation after blue
CC       light irradiation of etiolated seedlings.
CC       {ECO:0000269|PubMed:16415218}.
CC   -!- MISCELLANEOUS: Has no detectable prehenate dehydratase activity.
CC   -!- CAUTION: Was reported to be a cytosolic prephenate dehydratase
CC       interacting with a G-protein alpha-subunit.
CC       {ECO:0000305|PubMed:16415218}.
DR   EMBL; DQ411464; ABD67750.1; -; mRNA.
DR   EMBL; AC005824; AAC73018.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08050.1; -; Genomic_DNA.
DR   EMBL; AY087695; AAM65232.1; -; mRNA.
DR   EMBL; BT025989; ABG25078.1; -; mRNA.
DR   EMBL; AK229426; BAF01286.1; -; mRNA.
DR   PIR; D84677; D84677.
DR   RefSeq; NP_180350.1; NM_128342.3.
DR   SMR; Q9ZUY3; -.
DR   BioGrid; 2679; 1.
DR   STRING; 3702.AT2G27820.1; -.
DR   PaxDb; Q9ZUY3; -.
DR   PRIDE; Q9ZUY3; -.
DR   EnsemblPlants; AT2G27820.1; AT2G27820.1; AT2G27820.
DR   GeneID; 817329; -.
DR   Gramene; AT2G27820.1; AT2G27820.1; AT2G27820.
DR   KEGG; ath:AT2G27820; -.
DR   Araport; AT2G27820; -.
DR   TAIR; locus:2042021; AT2G27820.
DR   eggNOG; KOG2797; Eukaryota.
DR   eggNOG; COG0077; LUCA.
DR   HOGENOM; HOG000018970; -.
DR   InParanoid; Q9ZUY3; -.
DR   KO; K05359; -.
DR   OMA; YRFDSAN; -.
DR   OrthoDB; 1090069at2759; -.
DR   PhylomeDB; Q9ZUY3; -.
DR   BioCyc; ARA:AT2G27820-MONOMER; -.
DR   BRENDA; 4.2.1.51; 399.
DR   BRENDA; 4.2.1.91; 399.
DR   SABIO-RK; Q9ZUY3; -.
DR   UniPathway; UPA00121; UER00344.
DR   PRO; PR:Q9ZUY3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZUY3; baseline and differential.
DR   Genevisible; Q9ZUY3; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IMP:TAIR.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:TAIR.
DR   GO; GO:0080167; P:response to karrikin; IEP:TAIR.
DR   GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:TAIR.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IMP:TAIR.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Chloroplast; Complete proteome; Lyase; Phenylalanine biosynthesis;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT       1     24       Chloroplast. {ECO:0000255}.
FT   CHAIN        25    424       Arogenate dehydratase 3, chloroplastic.
FT                                /FTId=PRO_0000373792.
FT   DOMAIN      122    299       Prephenate dehydratase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00517}.
FT   DOMAIN      313    404       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   COMPBIAS     30     75       Ser-rich.
FT   COMPBIAS    241    272       Ala-rich.
FT   COMPBIAS    409    420       Poly-Ser.
FT   CONFLICT    206    206       I -> M (in Ref. 4; AAM65232).
FT                                {ECO:0000305}.
SQ   SEQUENCE   424 AA;  46102 MW;  52471CE9914FDA89 CRC64;
     MRTLLPSHTP ATVTTAARRR HVIHCAGKRS DSFSINSSSS DWQSSCAILS SKVNSQEQSE
     SLSSNSNGSS SYHVSAVNGH NNGAGVSDLN LVPFNNNQSI QSKKPLSISD LSPAPMHGSN
     LRVAYQGVPG AYSEAAAGKA YPNCQAIPCD QFEVAFQAVE LWIADRAVLP VENSLGGSIH
     RNYDLLLRHR LHIVGEVQLP VHHCLIALPG VRKEFLTRVI SHPQGLAQCE HTLTKLGLNV
     AREAVDDTAG AAEFIAANNI RDTAAIASAR AAEIYGLEIL EDGIQDDASN VTRFVMLARE
     PIIPRTDRPF KTSIVFAHEK GTCVLFKVLS AFAFRNISLT KIESRPNHNV PIRLVDEANV
     GTAKHFEYMF YIDFEASMAE SRAQNALSEV QEFTSFLRVL GSYPMDMTSW SPSSSSSSSS
     TFSL
//
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