ID A0A0P0VWW4_ORYSJ Unreviewed; 227 AA.
AC A0A0P0VWW4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JUN-2023, entry version 27.
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 OrderedLocusNames=Os03g0286200 {ECO:0000313|EMBL:BAS83628.1};
GN ORFNames=OSNPB_030286200 {ECO:0000313|EMBL:BAS83628.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS83628.1, ECO:0000313|Proteomes:UP000059680};
RN [1] {ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2] {ECO:0000313|EMBL:BAS83628.1, ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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 EMBL; AP014959; BAS83628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0VWW4; -.
DR EnsemblPlants; Os03t0286200-02; Os03t0286200-02; Os03g0286200.
DR Gramene; Os03t0286200-02; Os03t0286200-02; Os03g0286200.
DR UniPathway; UPA00121; UER00344.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; A0A0P0VWW4; baseline and differential.
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:SF36; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|ProteomicsDB:A0A0P0VWW4};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW Transit peptide {ECO:0000256|RuleBase:RU363004}.
FT DOMAIN 1..116
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 130..221
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAS83628.1"
SQ SEQUENCE 227 AA; 25322 MW; 50DA62D7EC303B5E CRC64;
FDLLLRHRLH IVGEVRLAVR HCLLANPGVK IENLKSAMSH PQALAQCEHT LTEFGIEHRE
AVDDTAGAAK TVAEQNLQDT GAIASSLAAE LYGLNVLAEN IQDDKDNVTR FMMLAREPII
PRTDKPFKTS IVFSLEEGPG QLFKALGVFA LREINLTKIE SRPHKKRPLR ITDDSFSTPS
KQFDYLFYMD LEASMADPKT QNALGNLKEF ATFLRVLGSY PTDVNEA
//
