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Database: UniProt
Entry: D3U716
LinkDB: D3U716
Original site: D3U716 
ID   AROD2_PETHY             Reviewed;         394 AA.
AC   D3U716;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Arogenate dehydratase 2 {ECO:0000303|PubMed:20215586};
DE            Short=PhADT2 {ECO:0000303|PubMed:20215586};
DE            EC=4.2.1.91 {ECO:0000269|PubMed:20215586};
DE   AltName: Full=Prephenate dehydratase ADT3 {ECO:0000305};
DE            EC=4.2.1.51 {ECO:0000255|PROSITE-ProRule:PRU00517, ECO:0000269|PubMed:20215586};
DE   Flags: Precursor;
GN   Name=ADT2 {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, CATALYTIC ACTIVITY, PATHWAY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   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).
CC   -!- FUNCTION: Converts the prephenate and L-arogenate produced from the
CC       shikimate-chorismate pathway into 3-phenylpyruvate and phenylalanine
CC       (Phe), respectively (PubMed:20215586). Involved in floral volatile
CC       benzenoids and phenylpropanoids (FVBP) production (By similarity).
CC       {ECO:0000250|UniProtKB:D3U715, ECO:0000269|PubMed:20215586}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC         Evidence={ECO:0000269|PubMed:20215586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21649;
CC         Evidence={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=66.7 uM for L-arogenate {ECO:0000269|PubMed:20215586};
CC         KM=752 uM for prephenate {ECO:0000269|PubMed:20215586};
CC         Vmax=30.277 pmol/sec/mg enzyme with L-arogenate as substrate
CC         {ECO:0000269|PubMed:20215586};
CC         Vmax=1.473 pmol/sec/mg enzyme with prephenate as substrate
CC         {ECO:0000269|PubMed:20215586};
CC         Note=kcat is 1.231 sec(-1) with L-arogenate as substrate
CC         (PubMed:20215586). kcat is 0.060 sec(-1) with prephenate as substrate
CC         (PubMed:20215586). {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: Expressed at low levels in petals (corollas and
CC       tubes), stems, leaves, pistils, stamens, ovaries and sepals.
CC       {ECO:0000269|PubMed:20215586}.
CC   -!- DEVELOPMENTAL STAGE: Barely expressed throughout flower development.
CC       {ECO:0000269|PubMed:20215586}.
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DR   EMBL; FJ790413; ACY79503.1; -; mRNA.
DR   AlphaFoldDB; D3U716; -.
DR   SMR; D3U716; -.
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:0004664; F:prephenate dehydratase activity; IDA: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..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..394
FT                   /note="Arogenate dehydratase 2"
FT                   /id="PRO_0000451503"
FT   DOMAIN          108..283
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          297..388
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  43424 MW;  6E25D48147921418 CRC64;
     MAATTTLRSP KIPHPPPEST PSNLSYLSQI SLTPVPKRRR FISIYACSNA ESNSQFGSEI
     KKSQAIELNK VSDEHPYEFN SKDSPNPLPR PLTSADLSNM ATEGSRLRVA YQGVRGAYSE
     SAAEKAYPNC EAVPCEQFDT AFEAVERWLV DRAVLPIENS LGGSIHRNYD LLLRHRLHIV
     GEVKLAIRHC LLANNGVKIE DLKRVLSHPQ ALAQCENNLT KLGLVREAVD DTAGAAKYIA
     FQQLKDAGAV ASLAAARIYG LNVLAQDIQD DSDNVTRFLM LAREPIIPGT DKPFKTSVVF
     SLDEGPGVLF KALAVFAMRN INLTKIESRP LQKQALRVLD DSADGFPKYF PYLFYVDFEA
     SMADQRAQNA LGHLKEFATF LRVLGSYPSD SGIA
//
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