ID A0A0K9NLA9_ZOSMR Unreviewed; 341 AA.
AC A0A0K9NLA9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:KMZ56867.1};
GN ORFNames=ZOSMA_8G00050 {ECO:0000313|EMBL:KMZ56867.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ56867.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ56867.1}.
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DR EMBL; LFYR01002110; KMZ56867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NLA9; -.
DR STRING; 29655.A0A0K9NLA9; -.
DR OMA; LACDENK; -.
DR OrthoDB; 2783975at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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; 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; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR PANTHER; PTHR21022:SF43; AROGENATE DEHYDRATASE_PREPHENATE DEHYDRATASE 2, 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; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 114..289
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
SQ SEQUENCE 341 AA; 37515 MW; B43DD218286779B6 CRC64;
MSSLSLTPDP STFFSRCTKE PSPRCALSTS VAVAGSRRRS FVALSISTMV SLHMDYDNTR
SSSRSQAMEL SRVLDQSLSS SKIESGDISV SRSLPKPLTA SDLVEVTSTG PRFRVAYQGL
PGAYSESAAA KAYPKCEAVP CEQFETTFEA VERWQVDRAV LPIENSLGGS IHRNYDLLIR
HKLHIVGEVR FAVRHCLLAN RGVKKENLRR VLSHPQALAQ CEHTLTKLAV VKEAVDDTAG
AAQFVSINQF RDTAAVASSL ASKIYGLDIL VHDIQDDSDN ITRFLMLARE PIIPKVDRPF
KTSVVFSLEE GPGVLFKALA VFAMRNINLT KVLPLYFLRG L
//