AROD3_ARATH
ID AROD3_ARATH Reviewed; 424 AA.
AC Q9ZUY3; Q0WNL3; Q8LAP1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Arogenate dehydratase 3, chloroplastic {ECO:0000303|PubMed:17726025};
DE Short=AtADT3 {ECO:0000303|PubMed:17726025};
DE EC=4.2.1.91 {ECO:0000269|PubMed:17726025};
DE AltName: Full=Prephenate dehydratase 1 {ECO:0000305};
DE Short=AtPDT1 {ECO:0000305};
DE Flags: Precursor;
GN Name=ADT3 {ECO:0000303|PubMed:17726025};
GN Synonyms=PD1 {ECO:0000303|PubMed:16415218}, PDT1 {ECO:0000305};
GN OrderedLocusNames=At2g27820 {ECO:0000312|Araport:AT2G27820};
GN ORFNames=F15K20.8 {ECO:0000312|EMBL:AAC73018.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-424.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP GPA1.
RX PubMed=16415218; DOI=10.1104/pp.105.071282;
RA Warpeha K.M., Lateef S.S., Lapik Y., Anderson M., Lee B.-S., Kaufman L.S.;
RT "G-protein-coupled receptor 1, G-protein Galpha-subunit 1, and prephenate
RT dehydratase 1 are required for blue light-induced production of
RT phenylalanine in etiolated Arabidopsis.";
RL Plant Physiol. 140:844-855(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP 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 [9]
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 (PubMed:17726025). Together with
CC GCR1 and GPA1, required for blue light-mediated synthesis of
CC phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated
CC seedlings (PubMed:16415218). {ECO:0000269|PubMed:16415218,
CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12537;
CC Evidence={ECO:0000269|PubMed:17726025};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.43 mM for arogenate {ECO:0000269|PubMed:17726025};
CC Vmax=5.17 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. {ECO:0000305}.
CC -!- SUBUNIT: May interact with GPA1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16415218, ECO:0000269|PubMed:19136569}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:17726025}.
CC -!- DISRUPTION PHENOTYPE: Lack of Phe and Tyr accumulation after blue light
CC irradiation of etiolated seedlings. {ECO:0000269|PubMed:16415218}.
CC -!- MISCELLANEOUS: Has no detectable prehenate dehydratase activity.
CC {ECO:0000269|PubMed:17726025}.
CC -!- CAUTION: Was reported to be a cytosolic prephenate dehydratase
CC interacting with a G-protein alpha-subunit.
CC {ECO:0000305|PubMed:16415218}.
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DR EMBL; DQ411464; ABD67750.1; -; mRNA.
DR EMBL; AC005824; AAC73018.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08050.1; -; Genomic_DNA.
DR EMBL; AY087695; AAM65232.1; -; mRNA.
DR EMBL; BT025989; ABG25078.1; -; mRNA.
DR EMBL; AK229426; BAF01286.1; -; mRNA.
DR PIR; D84677; D84677.
DR RefSeq; NP_180350.1; NM_128342.3.
DR AlphaFoldDB; Q9ZUY3; -.
DR SMR; Q9ZUY3; -.
DR BioGRID; 2679; 1.
DR STRING; 3702.AT2G27820.1; -.
DR PaxDb; Q9ZUY3; -.
DR PRIDE; Q9ZUY3; -.
DR ProteomicsDB; 246999; -.
DR EnsemblPlants; AT2G27820.1; AT2G27820.1; AT2G27820.
DR GeneID; 817329; -.
DR Gramene; AT2G27820.1; AT2G27820.1; AT2G27820.
DR KEGG; ath:AT2G27820; -.
DR Araport; AT2G27820; -.
DR TAIR; locus:2042021; AT2G27820.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_1_1; -.
DR InParanoid; Q9ZUY3; -.
DR OMA; IHCAGKR; -.
DR OrthoDB; 1090069at2759; -.
DR PhylomeDB; Q9ZUY3; -.
DR BioCyc; ARA:AT2G27820-MON; -.
DR BRENDA; 4.2.1.51; 399.
DR BRENDA; 4.2.1.91; 399.
DR SABIO-RK; Q9ZUY3; -.
DR UniPathway; UPA00121; UER00344.
DR PRO; PR:Q9ZUY3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUY3; baseline and differential.
DR Genevisible; Q9ZUY3; 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:0005829; C:cytosol; IMP:TAIR.
DR GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:TAIR.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:TAIR.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP:TAIR.
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..24
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 25..424
FT /note="Arogenate dehydratase 3, chloroplastic"
FT /id="PRO_0000373792"
FT DOMAIN 122..299
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 313..404
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 57..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 206
FT /note="I -> M (in Ref. 4; AAM65232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46102 MW; 52471CE9914FDA89 CRC64;
MRTLLPSHTP ATVTTAARRR HVIHCAGKRS DSFSINSSSS DWQSSCAILS SKVNSQEQSE
SLSSNSNGSS SYHVSAVNGH NNGAGVSDLN LVPFNNNQSI QSKKPLSISD LSPAPMHGSN
LRVAYQGVPG AYSEAAAGKA YPNCQAIPCD QFEVAFQAVE LWIADRAVLP VENSLGGSIH
RNYDLLLRHR LHIVGEVQLP VHHCLIALPG VRKEFLTRVI SHPQGLAQCE HTLTKLGLNV
AREAVDDTAG AAEFIAANNI RDTAAIASAR AAEIYGLEIL EDGIQDDASN VTRFVMLARE
PIIPRTDRPF KTSIVFAHEK GTCVLFKVLS AFAFRNISLT KIESRPNHNV PIRLVDEANV
GTAKHFEYMF YIDFEASMAE SRAQNALSEV QEFTSFLRVL GSYPMDMTSW SPSSSSSSSS
TFSL
