ID A0A0D2RTW0_GOSRA Unreviewed; 426 AA.
AC A0A0D2RTW0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=B456_006G109800 {ECO:0000313|EMBL:KJB35339.1}, Gorai_000716
GN {ECO:0000313|EMBL:MBA0587590.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB35339.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB35339.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
RN [2] {ECO:0000313|EMBL:MBA0587590.1, ECO:0000313|Proteomes:UP000593578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:MBA0587590.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0587590.1};
RX PubMed=30476109;
RA Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA Wendel J.F.;
RT "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT Subgenus Houzingenia) Based on Genome Sequencing.";
RL Genome Biol. Evol. 11:53-71(2019).
RN [3] {ECO:0000313|EMBL:MBA0587590.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8 {ECO:0000313|EMBL:MBA0587590.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0587590.1};
RA Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL Submitted (APR-2020) 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|ARBA:ARBA00004929, ECO:0000256|RuleBase:RU363004}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470, ECO:0000256|RuleBase:RU363004}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001745; KJB35339.1; -; Genomic_DNA.
DR EMBL; JABEZZ010000006; MBA0587590.1; -; Genomic_DNA.
DR RefSeq; XP_012485071.1; XM_012629617.1.
DR AlphaFoldDB; A0A0D2RTW0; -.
DR STRING; 29730.A0A0D2RTW0; -.
DR EnsemblPlants; KJB35339; KJB35339; B456_006G109800.
DR GeneID; 105799193; -.
DR Gramene; KJB35339; KJB35339; B456_006G109800.
DR KEGG; gra:105799193; -.
DR eggNOG; KOG2797; Eukaryota.
DR OrthoDB; 2783975at2759; -.
DR UniPathway; UPA00121; UER00344.
DR Proteomes; UP000032304; Chromosome 6.
DR Proteomes; UP000593578; Unassembled WGS sequence.
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; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 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:UP000032304};
KW Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT DOMAIN 132..309
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 323..414
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 426 AA; 46865 MW; 991D5951E40B5D1E CRC64;
MQAVSPTQNL NSSVIRPSKP RRFHQLTRSF IRCVYHNDSV QFPNGVGLNR ADWQSSCAIL
SSKVFSQDQG SGDKSTAPSN SDHLAAAVNG HKTSIDLNLV PIEKNNKPQP PTQKPLTITD
LSPAPMHGSQ LRVAYQGVPG AYSEAAAGKA YPNCEAIPCD QFEVAFQAVE LWIADRAVLP
VENSLGGSIH RNYDLLLRHR LHIVGEVQLP VHHCLLALPG VRKEYLARVI SHPQALSQCE
HTLTKLGLNV TREAVDDTAG AAEYIAANNL RDTAAIASAR AAELYGLQIL ADGIQDDSSN
VTRFVMLARE PIIPRTDRPF KTSIVFAHDK GTSVLFKVLS AFAFRNISLT KIESRPHRNR
PIRLVDDANV GTAKHFEYMF YVDFEASMAE VRAQNALAEV QEFTSFLRVL GSYPMDMTPW
CPSSGD
//
