ID A0A0D3AKI8_BRAOL Unreviewed; 432 AA.
AC A0A0D3AKI8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 30.
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 Name=106327879 {ECO:0000313|EnsemblPlants:Bo2g024140.1};
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:Bo2g024140.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo2g024140.1, 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:Bo2g024140.1}
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU363004}.
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DR RefSeq; XP_013621630.1; XM_013766176.1.
DR AlphaFoldDB; A0A0D3AKI8; -.
DR STRING; 109376.A0A0D3AKI8; -.
DR EnsemblPlants; Bo2g024140.1; Bo2g024140.1; Bo2g024140.
DR GeneID; 106327879; -.
DR Gramene; Bo2g024140.1; Bo2g024140.1; Bo2g024140.
DR KEGG; boe:106327879; -.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_1_1; -.
DR OMA; PMDMAPW; -.
DR OrthoDB; 2783975at2759; -.
DR UniPathway; UPA00121; UER00344.
DR Proteomes; UP000032141; Chromosome C2.
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:SF30; 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:UP000032141};
KW Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT DOMAIN 134..311
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 327..418
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 432 AA; 46504 MW; E4A96F848C212E3D CRC64;
MQAVSPTFSC DLKPMIQTNL TAKIARYSHV NRNRVSVRCS YKSESFSFPN GVGSSRADWQ
SSCAILASKV ASAENSSSIT GSLAGQVAAV NGHSNDSVNL SLVPSNTQNG KPGLIQPLTN
TDLSPAPSHG STLRVAYQGV PGAYSEAAAG KAYPKSEAIP CDQFDVAFQA VELWIADRAV
LPVENSLGGS IHRNYDLLLR HRLHIVGEVQ IPVHHCLLAL PGVRPDCVRR VISHPQALAQ
TEGSLNKLTP KAAIEAFHDT AAAAEYIAAN NLRDTAAVAS ARAAELYGLQ ILADGIQDDA
GNVTRFLMLA RDPIIPRTDR PFKTSIVFAA QEREGTSVLF KVLSAFAFRN ISLTKIESRP
HQNCPVRVVG DGGVGTAKQF EYTFYVDFEA SMAEARAQNA LSEVQEYTSF LRVLGSYPMD
MSPWSTLPSE DA
//
