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Database: UniProt
Entry: D3U717
LinkDB: D3U717
Original site: D3U717 
ID   AROD3_PETHY             Reviewed;         434 AA.
AC   D3U717;
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 3 {ECO:0000303|PubMed:20215586};
DE            Short=PhADT3 {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=ADT3 {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:0000255|PROSITE-ProRule:PRU00517,
CC         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=48.8 uM for L-arogenate {ECO:0000269|PubMed:20215586};
CC         KM=465.8 uM for prephenate {ECO:0000269|PubMed:20215586};
CC         Vmax=4.464 pmol/sec/mg enzyme with L-arogenate as substrate
CC         {ECO:0000269|PubMed:20215586};
CC         Vmax=280 pmol/sec/mg enzyme with prephenate as substrate
CC         {ECO:0000269|PubMed:20215586};
CC         Note=kcat is 0.194 sec(-1) with L-arogenate as substrate
CC         (PubMed:20215586). kcat is 0.012 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: Expressed, at low levels, throughout flower
CC       development (PubMed:20215586). In corollas, accumulates progressively
CC       during flower development, from buds to anthesis (PubMed:20215586).
CC       {ECO:0000269|PubMed:20215586}.
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DR   EMBL; FJ790414; ACY79504.1; -; mRNA.
DR   AlphaFoldDB; D3U717; -.
DR   SMR; D3U717; -.
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..43
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..434
FT                   /note="Arogenate dehydratase 3"
FT                   /id="PRO_0000451504"
FT   DOMAIN          140..317
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          331..422
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   434 AA;  47332 MW;  371356C8C9E5F2E3 CRC64;
     MQSLTPSSSG INIKLLNRKK IQTHRVTPSR VVIKCVYRFD SVNAGAAAVN TGVVNTPASN
     NTAGHVGASR TDWQSSCAIL ASKVVSQQQD TEKSGGAGNI TAVNGHKILN LDLLPVESNR
     AKPLTITDLS PAPMHGAQLR VAYQGVPGAY SEAAAGKAYP KCEAIPCDQF EVAFQAVELW
     IADRAVLPIE NSLGGSIHRN YDLLLRHRLH IVGEVQLPVH HCLLALPGVR KEYLTRVISH
     PQALAQCELT LTKLGLNVAR EAVDDTAGAA EYIAANNLRD TAAIASSRAA ELYGLDILEQ
     GIQDDLSNVT RFVMLAREPI IPRTDRPFKT SIVFAHDKGT SVLFKVLSAF AFRNISLTKI
     ESRPHRNRPI RLVDDANVGT AKHFEYMFYV DFEASMADVR AQNALAEVQE FTSFLRVLGS
     YPMDMTPWSP SRDA
//
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