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Database: UniProt
Entry: U5CVN8_AMBTC
LinkDB: U5CVN8_AMBTC
Original site: U5CVN8_AMBTC 
ID   U5CVN8_AMBTC            Unreviewed;       463 AA.
AC   U5CVN8;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Arogenate dehydratase {ECO:0000256|ARBA:ARBA00013259, ECO:0000256|RuleBase:RU363004};
DE            EC=4.2.1.91 {ECO:0000256|ARBA:ARBA00013259, ECO:0000256|RuleBase:RU363004};
GN   ORFNames=AMTR_s00037p00204590 {ECO:0000313|EMBL:ERN17391.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN17391.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
CC   -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC       chorismate pathway into phenylalanine. {ECO:0000256|RuleBase:RU363004}.
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:0000256|RuleBase:RU363004};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from L-arogenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004929, ECO:0000256|RuleBase:RU363004}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU363004}.
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DR   EMBL; KI392350; ERN17391.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5CVN8; -.
DR   STRING; 13333.U5CVN8; -.
DR   EnsemblPlants; ERN17391; ERN17391; AMTR_s00037p00204590.
DR   Gramene; ERN17391; ERN17391; AMTR_s00037p00204590.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_591022_0_0_1; -.
DR   OMA; CYPMDTV; -.
DR   UniPathway; UPA00121; UER00344.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13631; PBP2_Ct-PDT_like; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   PANTHER; PTHR21022:SF20; AROGENATE DEHYDRATASE_PREPHENATE DEHYDRATASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU363004};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU363004};
KW   Chloroplast {ECO:0000256|RuleBase:RU363004};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU363004};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW   ECO:0000256|RuleBase:RU363004}; Plastid {ECO:0000256|RuleBase:RU363004};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT   DOMAIN          97..272
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          286..391
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          34..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  51273 MW;  EA823FE935FBDB19 CRC64;
     MALNAFYNSW QLPPLLLNDQ KLDLEAKALT LSFKPKENNG SSTSPNVNDP QTPLPPVELK
     PLLPNPPIEL RKEFISLPRP LSVTDLAACP SHGAPVRVAY QGVPGAYSEE AALKAYPQCE
     AVPCDQFEAA FKAVELWLVD KAVLPIENSL GGSIHRNYDL LLRHRLHIVG EVQILVNHCL
     LGLPGVRREE LTRVLSHPQA LAQCEIALSQ LGVVRESVDN IAGAAQLVAT QRLRDTGAIA
     SARAAELYGL IILAERIQDD FENVTRFLIL AREPIIPRGD QPFKTSIVFT LEEGPGVLFK
     ALAVFALREI NLTKIESRPQ RKRPLRVVDD SNNGSAKYFD YLFYIDFEAS MADPRAQNAL
     GHLQVHVRKI LFTHMHGALP AIIVTLLICW QSECKSGSCI IVSHKTWLMS LSHGLKSFAE
     NPCVLGSICH CWVDTLTGSP NFSRKDADRC ALRRRLGRFQ IGN
//
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