AROD2_PETHY
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
