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Database: UniProt
Entry: D3U715
LinkDB: D3U715
Original site: D3U715 
ID   AROD1_PETHY             Reviewed;         424 AA.
AC   D3U715;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Arogenate dehydratase 1 {ECO:0000303|PubMed:20215586};
DE            Short=PhADT1 {ECO:0000303|PubMed:20215586};
DE            EC=4.2.1.91 {ECO:0000269|PubMed:20215586};
DE   Flags: Precursor;
GN   Name=ADT1 {ECO:0000303|PubMed:20215586};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP   ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=20215586; DOI=10.1105/tpc.109.073247;
RA   Maeda H., Shasany A.K., Schnepp J., Orlova I., Taguchi G., Cooper B.R.,
RA   Rhodes D., Pichersky E., Dudareva N.;
RT   "RNAi suppression of Arogenate Dehydratase1 reveals that phenylalanine is
RT   synthesized predominantly via the arogenate pathway in petunia petals.";
RL   Plant Cell 22:832-849(2010).
RN   [2]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Violet 26;
RX   PubMed=20543029; DOI=10.1105/tpc.109.067280;
RA   Spitzer-Rimon B., Marhevka E., Barkai O., Marton I., Edelbaum O., Masci T.,
RA   Prathapani N.K., Shklarman E., Ovadis M., Vainstein A.;
RT   "EOBII, a gene encoding a flower-specific regulator of phenylpropanoid
RT   volatiles' biosynthesis in petunia.";
RL   Plant Cell 22:1961-1976(2010).
RN   [3]
RP   INDUCTION BY EOBI.
RC   STRAIN=cv. W115;
RX   PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA   Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA   Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT   "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT   regulates scent production by activating ODO1 and structural scent-related
RT   genes in petunia.";
RL   Plant Cell 24:5089-5105(2012).
RN   [4]
RP   INDUCTION.
RX   PubMed=26124104; DOI=10.1073/pnas.1422875112;
RA   Fenske M.P., Hewett Hazelton K.D., Hempton A.K., Shim J.S., Yamamoto B.M.,
RA   Riffell J.A., Imaizumi T.;
RT   "Circadian clock gene LATE ELONGATED HYPOCOTYL directly regulates the
RT   timing of floral scent emission in Petunia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:9775-9780(2015).
CC   -!- FUNCTION: Converts L-arogenate produced from the shikimate-chorismate
CC       pathway into phenylalanine (Phe) (PubMed:20215586). Involved in floral
CC       volatile benzenoids and phenylpropanoids (FVBP) production
CC       (PubMed:20215586). {ECO:0000269|PubMed:20215586}.
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; EC=4.2.1.91;
CC         Evidence={ECO:0000269|PubMed:20215586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12537;
CC         Evidence={ECO:0000269|PubMed:20215586};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=179 uM for L-arogenate {ECO:0000269|PubMed:20215586};
CC         Vmax=6.234 pmol/sec/mg enzyme with L-arogenate as substrate
CC         {ECO:0000269|PubMed:20215586};
CC         Note=kcat is 0.267 sec(-1) with L-arogenate as substrate.
CC         {ECO:0000269|PubMed:20215586};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from L-arogenate: step 1/1.
CC       {ECO:0000269|PubMed:20215586}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:20215586}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers, especially in petals
CC       (corollas and tubes), and, at low levels, in roots, stems, leaves,
CC       pistils, stamens, ovaries and sepals. {ECO:0000269|PubMed:20215586,
CC       ECO:0000269|PubMed:20543029}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout flower development
CC       (PubMed:20215586). In corollas, accumulates progressively during flower
CC       development, from buds to anthesis (PubMed:20543029, PubMed:20215586).
CC       {ECO:0000269|PubMed:20215586, ECO:0000269|PubMed:20543029}.
CC   -!- INDUCTION: Circadian-regulation with peak levels occurring at the end
CC       of the light period in flowers (PubMed:26124104). Triggered by EOBI in
CC       flowers (PubMed:23275577). {ECO:0000269|PubMed:23275577,
CC       ECO:0000269|PubMed:26124104}.
CC   -!- DISRUPTION PHENOTYPE: Reduced arogenate dehydratase activity leading to
CC       lower levels of phenylalanine (Phe) and downstream
CC       phenylpropanoid/benzenoid volatiles (PubMed:20215586). Petals
CC       accumulate unaltered arogenate levels but decreased shikimate and
CC       tryptophan (Trp) levels associated with the down-regulation of carbon
CC       flux toward shikimic acid (PubMed:20215586).
CC       {ECO:0000269|PubMed:20215586}.
CC   -!- MISCELLANEOUS: Has no detectable prehenate dehydratase activity.
CC       {ECO:0000269|PubMed:20215586}.
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DR   EMBL; FJ790412; ACY79502.1; -; mRNA.
DR   AlphaFoldDB; D3U715; -.
DR   SMR; D3U715; -.
DR   BRENDA; 4.2.1.91; 4700.
DR   UniPathway; UPA00121; UER00344.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; SSF55021; 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; Chloroplast;
KW   Lyase; Phenylalanine biosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..424
FT                   /note="Arogenate dehydratase 1"
FT                   /id="PRO_0000451502"
FT   DOMAIN          131..308
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          321..412
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   424 AA;  45902 MW;  0D43A86BF86F2F0A CRC64;
     MQSLTPSSGV NLKSIIRKTS LPPGQTRFIT GRVIKCGYQV DSANTVNTAG APASYNSGHV
     GASRADWQSS CAILASKVVS QQPDTEKTGG AGNITAVNGH KTLDLVSIDN LPKALTITDL
     SPAPMHGSTL RVAYQGVPGA YSEAAAGKAY PNCEAIPCDQ FEVAFQAVEL WIADRAVLPV
     ENSLGGSIHR NYDLLLRHRL HIVGEVQLPV HHCLLALPGV RKEYLTRVIS HPQALAQCEL
     TITKLGLNVA REAVDDTAGA AEYIAANNLR DTAAVASARA AELYGLQILA EGIQDDSSNV
     TRFVMLAREP IIPRMDRPFK TSIVFAHEGT GVLFKVLSAF AFRNISLTKI ESRPHRNRPI
     RLVDDANVGT AKHFEYMFYV DFDASMADVR AQNALAEVQE FTSFLRVLGS YPMDMTPCCP
     SRDE
//
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