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Database: UniProt
Entry: A0A0D9XGW8_9ORYZ
LinkDB: A0A0D9XGW8_9ORYZ
Original site: A0A0D9XGW8_9ORYZ 
ID   A0A0D9XGW8_9ORYZ        Unreviewed;       411 AA.
AC   A0A0D9XGW8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR09G15870.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR09G15870.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR09G15870.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR09G15870.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D9XGW8; -.
DR   STRING; 77586.A0A0D9XGW8; -.
DR   EnsemblPlants; LPERR09G15870.1; LPERR09G15870.1; LPERR09G15870.
DR   Gramene; LPERR09G15870.1; LPERR09G15870.1; LPERR09G15870.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_035008_4_1_1; -.
DR   UniPathway; UPA00121; UER00344.
DR   Proteomes; UP000032180; Chromosome 9.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF40; OS08G0411000 PROTEIN; 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:UP000032180};
KW   Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT   DOMAIN          102..279
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          294..385
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  44375 MW;  26B8162364A24CE6 CRC64;
     METASSPAPR RPAQIRRSTA RPPPPSATPF SRADWQTTCA AILSNSNSPA PRVNGDTNSN
     PALAAAAPPP PAELDLLPVS NLPRPLSITD LSPAPMHGSQ LRVAYQGVPG AYSEAAAAKA
     YPSCDAIPCD QFEVAFQAVE LWIADRAVLP VENSLGGSIH RNYDLLLRHR LHIVGEVQLP
     VHHCLLALPG VRRELLTRVI SHPQALAQCE LTLNAMGLNV AREAFDDTAA AAEHVAAAGL
     RDTAAIASAR AADLYGLHVL ADGIQDDAGN VTRFVMLARE PIIPRTDRPF KTSIVFAHDG
     EGTSVLFKVL SAFAFRGISL TKIESRPHRH RPIRLVDDAN VGTAKHFEYM FYIDFQASMA
     EVRAQNALAE IQEFTSFLRV LGSYPMDMTP WDSNSTSSTS AARRNNNTTS S
//
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