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Database: UniProt
Entry: A5BWG3_VITVI
LinkDB: A5BWG3_VITVI
Original site: A5BWG3_VITVI 
ID   A5BWG3_VITVI            Unreviewed;       411 AA.
AC   A5BWG3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Arogenate dehydratase {ECO:0000256|RuleBase:RU363004};
DE            EC=4.2.1.91 {ECO:0000256|RuleBase:RU363004};
GN   OrderedLocusNames=VIT_06s0061g01300 {ECO:0000313|EMBL:CCB44187.1};
GN   ORFNames=VITISV_041082 {ECO:0000313|EMBL:CAN68383.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN68383.1};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
RN   [2] {ECO:0000313|EMBL:CAN68383.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT   vinifera L.): coping with a highly heterozygous genome.";
RL   PLoS ONE 2:e1326-e1326(2007).
RN   [3] {ECO:0000313|EMBL:CCB44187.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Vitulo N., Olivier J., Forcato C., Albiero A., D'Angelo M., Zimbello R.,
RA   Schiavon R., Rigobello C., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Vezzi A., Hugueney P., Horner D., Mica E., Cattonaro F.,
RA   Del Fabbro C., Alaux M., Di Gaspero G., Scalabrin S., Pesole G.,
RA   Delledonne M., Pezzotti M., Pe E.M., Caboche M., Adam-Blondon A.-F.,
RA   Weissenbach J., Quetier F., Wincker P., Morgante M., Valle G.;
RT   "High quality assembly and annotation of grapevine genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363004}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|RuleBase:RU363004}.
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DR   EMBL; AM473632; CAN68383.1; -; Genomic_DNA.
DR   EMBL; FN594957; CCB44187.1; -; Genomic_DNA.
DR   RefSeq; XP_002268701.1; XM_002268665.4.
DR   STRING; 29760.VIT_06s0061g01300.t01; -.
DR   EnsemblPlants; VIT_06s0061g01300.t01; VIT_06s0061g01300.t01; VIT_06s0061g01300.
DR   GeneID; 100267022; -.
DR   Gramene; VIT_06s0061g01300.t01; VIT_06s0061g01300.t01; VIT_06s0061g01300.
DR   KEGG; vvi:100267022; -.
DR   eggNOG; KOG2797; Eukaryota.
DR   eggNOG; COG0077; LUCA.
DR   KO; K05359; -.
DR   OrthoDB; 1090069at2759; -.
DR   UniPathway; UPA00121; UER00344.
DR   Proteomes; UP000009183; Chromosome 6.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 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|RuleBase:RU363004};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU363004};
KW   Chloroplast {ECO:0000256|RuleBase:RU363004};
KW   Lyase {ECO:0000256|RuleBase:RU363004};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU363004};
KW   Plastid {ECO:0000256|RuleBase:RU363004};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT   DOMAIN          117..294
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          308..399
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   411 AA;  45109 MW;  AE5EF28DAB4686D9 CRC64;
     MQALSPSPNL KSLIRTRPLV PTHRVAPHRL VVQCVYKSDY SNFSGGVGFS RADWQSSCAI
     LASKVVSQQQ DTEKSGNADL TAVNGHKTLD LVPIENLPKP LTITDLSPAP MHGSELRVAY
     QGVPGAYSEA AAGKAYPNCE AIPCDQFEVA FQAVELWIAD RAVLPVENSL GGSIHRNYDL
     LLRHRLHIVG EVQLPVHHCL LALPGVRKEY LTRVISHPQA LAQCEHTLTK LGLNVAREAV
     DDTAGAAEYV ALNNLRDTAA IASARAADLY GLQILADGIQ DDSSNVTRFV MLAREPIIPR
     TDRPFKTSIV FAHDKGTSVL FKVLSAFAFR NISLTKIESR PHRNRPIRLV DDANVGTAKH
     FEYMFYVDFE ASMAEVRAQN ALAEVQEFTS FLRVLGSYPM DMTPWCPSGG D
//
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