ID A0A453IBR0_AEGTS Unreviewed; 399 AA.
AC A0A453IBR0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20511400.15, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET4Gv20511400.15}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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; A0A453IBR0; -.
DR SMR; A0A453IBR0; -.
DR EnsemblPlants; AET4Gv20511400.15; AET4Gv20511400.15; AET4Gv20511400.
DR Gramene; AET4Gv20511400.15; AET4Gv20511400.15; AET4Gv20511400.
DR OMA; QFSRFPS; -.
DR OrthoDB; 2783975at2759; -.
DR UniPathway; UPA00121; UER00344.
DR Proteomes; UP000015105; Chromosome 4D.
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:SF36; AROGENATE DEHYDRATASE; 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:UP000015105};
KW Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT DOMAIN 112..288
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 302..393
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 43507 MW; B275304A085EF7E8 CRC64;
MASMTTPRLP FLPARTRSAV AATSSSSPSS PLPRRSIKCS SSTNANSAPL PSTSRQPRAP
VADGVGSADL NGLRAPPIPV ADSPLPAYRD PHGLPRPLTS ADLMESSGEG LKVAYQGFPG
AYSEAAAKKA YPNCQTVPCE HFDTAFQAVQ NWIVDRAVLP LENTLGGSIH RNYDLLLRHE
LHIVGEVRLA VRHCLLANRG VKIGNLRNVI SHPQALAQCE HTLTELGIEH RQAVDDTAGA
AKLVAEQMLQ DTGAVASSLA AELYGLDILA ENIQDEKVNV TRFMMLAREP IIPRVDKPFK
TSIVFSLEEG PGQLFKALAV FALREINLTK IESRPHKKRP FRVADDAFST RVKYFDYLFY
VDLEASMADP KTQNALRNLE EFATFLRVLG SYPTDVSEA
//
