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Database: UniProt
Entry: Q9FNJ8
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Original site: Q9FNJ8 
ID   AROD5_ARATH             Reviewed;         425 AA.
AC   Q9FNJ8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Arogenate dehydratase 5, chloroplastic {ECO:0000303|PubMed:17726025};
DE            Short=AtADT5 {ECO:0000303|PubMed:17726025};
DE            EC=4.2.1.91 {ECO:0000269|PubMed:17726025};
DE   Flags: Precursor;
GN   Name=ADT5 {ECO:0000303|PubMed:17726025};
GN   OrderedLocusNames=At5g22630 {ECO:0000312|Araport:AT5G22630};
GN   ORFNames=MDJ22.5 {ECO:0000312|EMBL:BAB11669.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Matringe M., Grisollet D., Rippert P.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   INDUCTION.
RX   PubMed=15918878; DOI=10.1111/j.1365-313x.2005.02403.x;
RA   Ehlting J., Mattheus N., Aeschliman D.S., Li E., Hamberger B., Cullis I.F.,
RA   Zhuang J., Kaneda M., Mansfield S.D., Samuels L., Ritland K., Ellis B.E.,
RA   Bohlmann J., Douglas C.J.;
RT   "Global transcript profiling of primary stems from Arabidopsis thaliana
RT   identifies candidate genes for missing links in lignin biosynthesis and
RT   transcriptional regulators of fiber differentiation.";
RL   Plant J. 42:618-640(2005).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17726025; DOI=10.1074/jbc.m702662200;
RA   Cho M.-H., Corea O.R.A., Yang H., Bedgar D.L., Laskar D.D., Anterola A.M.,
RA   Moog-Anterola F.A., Hood R.L., Kohalmi S.E., Bernards M.A., Kang C.,
RA   Davin L.B., Lewis N.G.;
RT   "Phenylalanine biosynthesis in Arabidopsis thaliana. Identification and
RT   characterization of arogenate dehydratases.";
RL   J. Biol. Chem. 282:30827-30835(2007).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19136569; DOI=10.1104/pp.108.130070;
RA   Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M.;
RT   "Tyrosine and phenylalanine are synthesized within the plastids in
RT   Arabidopsis.";
RL   Plant Physiol. 149:1251-1260(2009).
CC   -!- FUNCTION: Converts the prephenate produced from the shikimate-
CC       chorismate pathway into phenylalanine. {ECO:0000269|PubMed:17726025}.
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:0000269|PubMed:17726025};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.72 mM for arogenate {ECO:0000269|PubMed:17726025};
CC         Vmax=11.26 pmol/sec/ug enzyme with arogenate as substrate
CC         {ECO:0000269|PubMed:17726025};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC       phenylalanine from L-arogenate: step 1/1.
CC       {ECO:0000269|PubMed:17726025}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:19136569}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. More abundant in stems and roots.
CC       {ECO:0000269|PubMed:17726025}.
CC   -!- INDUCTION: Strongly up-regulated during stem elongation.
CC       {ECO:0000269|PubMed:15918878}.
CC   -!- MISCELLANEOUS: Has no detectable prehenate dehydratase activity.
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DR   EMBL; DQ411469; ABD67755.1; -; mRNA.
DR   EMBL; AB006699; BAB11669.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93055.1; -; Genomic_DNA.
DR   EMBL; AY058097; AAL24205.1; -; mRNA.
DR   EMBL; AY090235; AAL90899.1; -; mRNA.
DR   EMBL; AY149958; AAN31112.1; -; mRNA.
DR   RefSeq; NP_197655.1; NM_122169.3.
DR   AlphaFoldDB; Q9FNJ8; -.
DR   SMR; Q9FNJ8; -.
DR   BioGRID; 17601; 5.
DR   IntAct; Q9FNJ8; 5.
DR   STRING; 3702.AT5G22630.1; -.
DR   PaxDb; Q9FNJ8; -.
DR   PRIDE; Q9FNJ8; -.
DR   ProteomicsDB; 246781; -.
DR   EnsemblPlants; AT5G22630.1; AT5G22630.1; AT5G22630.
DR   GeneID; 832326; -.
DR   Gramene; AT5G22630.1; AT5G22630.1; AT5G22630.
DR   KEGG; ath:AT5G22630; -.
DR   Araport; AT5G22630; -.
DR   TAIR; locus:2162459; AT5G22630.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_035008_4_1_1; -.
DR   InParanoid; Q9FNJ8; -.
DR   OMA; PMDMAPW; -.
DR   OrthoDB; 1090069at2759; -.
DR   PhylomeDB; Q9FNJ8; -.
DR   BioCyc; ARA:AT5G22630-MON; -.
DR   BRENDA; 4.2.1.91; 399.
DR   SABIO-RK; Q9FNJ8; -.
DR   UniPathway; UPA00121; UER00344.
DR   PRO; PR:Q9FNJ8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FNJ8; baseline and differential.
DR   Genevisible; Q9FNJ8; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEP:TAIR.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; SSF55021; 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; Aromatic amino acid biosynthesis; Chloroplast;
KW   Lyase; Phenylalanine biosynthesis; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..425
FT                   /note="Arogenate dehydratase 5, chloroplastic"
FT                   /id="PRO_0000373794"
FT   DOMAIN          127..304
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          320..411
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   425 AA;  45928 MW;  7B6AD16F3DE48B3F CRC64;
     MQTISPAFSC DLKSVIQPNL TAKKARYSHV NGKRVSVRCS YRSESFSFPN GVGSSRADWQ
     SSCAILASKV VSAENSSSVA VVNGHSNGSV DLSLVPSKSQ HNGKPGLIQP LTITDLSPAP
     SHGSTLRVAY QGVPGAYSEA AAGKAYPNSE AIPCDQFDVA FQAVELWIAD RAVLPVENSL
     GGSIHRNYDL LLRHRLHIVG EVQIPVHHCL LALPGVRTDC ITRVISHPQA LAQTEGSLNK
     LTPKAAIEAF HDTAAAAEYI AANNLHDTAA VASARAAELY GLQILADGIQ DDAGNVTRFL
     MLARDPIIPR TDRPFKTSIV FAAQEHKGTS VLFKVLSAFA FRNISLTKIE SRPHQNCPVR
     VVGDENVGTS KHFEYTFYVD FEASMAEARA QNALAEVQEY TSFLRVLGSY PMDMTPWSTL
     PSEDV
//
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