AROD5_ARATH
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
