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Database: UniProt
Entry: A0A1S3CFY0_CUCME
LinkDB: A0A1S3CFY0_CUCME
Original site: A0A1S3CFY0_CUCME 
ID   A0A1S3CFY0_CUCME        Unreviewed;       433 AA.
AC   A0A1S3CFY0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-2019, entry version 10.
DE   RecName: Full=Arogenate dehydratase {ECO:0000256|RuleBase:RU363004};
DE            EC=4.2.1.91 {ECO:0000256|RuleBase:RU363004};
GN   Name=LOC103500446 {ECO:0000313|RefSeq:XP_008461970.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Cucurbitales; Cucurbitaceae;
OC   Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008461970.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B.,
RA   Gabaldon T., Roma G., Guigo R., Casacuberta J.M., Arus P.,
RA   Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_008461970.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
CC   -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC       chorismate pathway into phenylalanine.
CC       {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;
CC         EC=4.2.1.91; 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   RefSeq; XP_008461970.1; XM_008463748.1.
DR   STRING; 3656.XP_008461970.1; -.
DR   GeneID; 103500446; -.
DR   KEGG; cmo:103500446; -.
DR   KO; K05359; -.
DR   OrthoDB; 1090069at2759; -.
DR   UniPathway; UPA00121; UER00344.
DR   Proteomes; UP000089565; Genome assembly.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000089565};
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:UP000089565};
KW   Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT   DOMAIN      138    315       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      329    420       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   433 AA;  47326 MW;  127D2594BE44C277 CRC64;
     MHLQSLTLSS SHSLLKSIPH FPTTTTSTST TAAVRFPIQS VYRYDPVTYP NAIGSSRADW
     QSSCAILSSQ SQQLLSQDDP SSSSTDHISS VNGHNSTIEN LNLVPISNLS DSTSLKPQPK
     PLTITDLAPA PMHGSNLRVA YQGVPGAYSE AAAGKAYPNC DAIPCDQFEV AFQSVELWIA
     DRAVLPVENS LGGSIHRNYD LLLRHKLHIV GEVQLPVHHC LLALPGVRKE YLTRVISHPQ
     ALAQCEHTLT KLGLNVTREA VDDTAGAAEF VAINNLRDTA AIASARAAEL YGLDILANGI
     QDDSGNVTRF VMLAREPIIP RTDRPFKTSI VFAHEKGTSV LFKVLSAFAF RNISLTKIES
     RPHRSHPIRV VDGADAGTAK HFEYLFYVDF EASMAEPRAQ NALAEVQEFT SFLRVLGSYP
     MDMTPWSPSR IEE
//
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