AROD1_PETHY
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
