ID A0A0D3DP72_BRAOL Unreviewed; 324 AA.
AC A0A0D3DP72;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Arogenate dehydratase {ECO:0000256|RuleBase:RU363004};
DE EC=4.2.1.91 {ECO:0000256|RuleBase:RU363004};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo8g061390.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo8g061390.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo8g061390.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU363004}.
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DR AlphaFoldDB; A0A0D3DP72; -.
DR STRING; 109376.A0A0D3DP72; -.
DR EnsemblPlants; Bo8g061390.1; Bo8g061390.1; Bo8g061390.
DR Gramene; Bo8g061390.1; Bo8g061390.1; Bo8g061390.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_0_1; -.
DR OMA; CYPMDTV; -.
DR UniPathway; UPA00121; UER00344.
DR Proteomes; UP000032141; Chromosome C8.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0047769; F:arogenate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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; IPR008242; Chor_mutase/pphenate_deHydtase.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR PANTHER; PTHR21022:SF29; AROGENATE DEHYDRATASE; 1.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 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:UP000032141};
KW Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT DOMAIN 39..214
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 228..319
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 324 AA; 35751 MW; 4098AED3AEE9920D CRC64;
MGLVQEAKPV AFHRDLSMLP KPLSANSLYS SAGDDSKVRI SFQGIPGAYS ETAALEAYPN
CETVPCEHFE TAFQAAELWL VDKAVLPIEN SVGGSIHRNY DLLLRHRLHI VQEVHLPVNH
CLLGVPGVNK EEIKRVLSHP QALDQCVNSL NDLGIQRLSA KDTATAAQTV ASSGKKDVGA
IASVRAANIY GLDILAENIQ DDANNVTRFL ILSREPMIPR TDRPYKTSIV FSLEEGPGVL
FKALAVFALR SINLSKIESR PQRRRPLRVV DGSNNGSAKS FDYLFYIDFE ASMAEIRAQH
ALGHLQEFTS FIRVLGCYPM DLVR
//
