AROD1_ARATH
ID AROD1_ARATH Reviewed; 392 AA.
AC Q9SA96; Q2V4P0; Q94B20;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Arogenate dehydratase/prephenate dehydratase 1, chloroplastic {ECO:0000305};
DE Short=AtADT1 {ECO:0000303|PubMed:17726025};
DE Short=AtPDT1 {ECO:0000303|PubMed:17726025};
DE EC=4.2.1.51 {ECO:0000269|PubMed:17726025};
DE EC=4.2.1.91 {ECO:0000269|PubMed:17726025};
DE Flags: Precursor;
GN Name=ADT1 {ECO:0000303|PubMed:17726025};
GN Synonyms=PDT1 {ECO:0000303|PubMed:17726025};
GN OrderedLocusNames=At1g11790 {ECO:0000312|Araport:AT1G11790};
GN ORFNames=F25C20.4 {ECO:0000312|EMBL:AAD30242.1};
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] (ISOFORM 1).
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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 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 [6]
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). Dehydratase
CC that uses arogenate and prephenate as substrates (PubMed:17726025).
CC Utilzes more efficiently arogenate than prephenate (PubMed:17726025).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000269|PubMed:17726025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21649;
CC Evidence={ECO:0000269|PubMed:17726025};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.05 mM for arogenate {ECO:0000269|PubMed:17726025};
CC KM=0.80 mM for prephenate {ECO:0000269|PubMed:17726025};
CC Vmax=31 pmol/sec/ug enzyme with arogenate as substrate
CC {ECO:0000269|PubMed:17726025};
CC Vmax=0.28 pmol/sec/ug enzyme with prephenate 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:0000305|PubMed:17726025}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000305|PubMed:17726025}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19136569}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SA96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SA96-2; Sequence=VSP_037227, VSP_037228;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:17726025}.
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DR EMBL; DQ411466; ABD67752.1; -; mRNA.
DR EMBL; AC007296; AAD30242.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28786.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28787.1; -; Genomic_DNA.
DR EMBL; AY042904; AAK68844.1; -; mRNA.
DR EMBL; AY081528; AAM10090.1; -; mRNA.
DR PIR; A86252; A86252.
DR RefSeq; NP_001031024.1; NM_001035947.1. [Q9SA96-2]
DR RefSeq; NP_172644.1; NM_101051.3. [Q9SA96-1]
DR AlphaFoldDB; Q9SA96; -.
DR SMR; Q9SA96; -.
DR BioGRID; 22965; 1.
DR STRING; 3702.AT1G11790.1; -.
DR PaxDb; Q9SA96; -.
DR PRIDE; Q9SA96; -.
DR ProteomicsDB; 246989; -. [Q9SA96-1]
DR EnsemblPlants; AT1G11790.1; AT1G11790.1; AT1G11790. [Q9SA96-1]
DR EnsemblPlants; AT1G11790.2; AT1G11790.2; AT1G11790. [Q9SA96-2]
DR GeneID; 837725; -.
DR Gramene; AT1G11790.1; AT1G11790.1; AT1G11790. [Q9SA96-1]
DR Gramene; AT1G11790.2; AT1G11790.2; AT1G11790. [Q9SA96-2]
DR KEGG; ath:AT1G11790; -.
DR Araport; AT1G11790; -.
DR TAIR; locus:2027332; AT1G11790.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_0_1; -.
DR InParanoid; Q9SA96; -.
DR OMA; HTRFVIL; -.
DR PhylomeDB; Q9SA96; -.
DR BioCyc; ARA:AT1G11790-MON; -.
DR BRENDA; 4.2.1.91; 399.
DR SABIO-RK; Q9SA96; -.
DR UniPathway; UPA00121; UER00344.
DR UniPathway; UPA00121; UER00345.
DR PRO; PR:Q9SA96; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA96; baseline and differential.
DR Genevisible; Q9SA96; 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; IBA:GO_Central.
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 Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Lyase;
KW Phenylalanine biosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..392
FT /note="Arogenate dehydratase/prephenate dehydratase 1,
FT chloroplastic"
FT /id="PRO_0000373790"
FT DOMAIN 107..282
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 296..387
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT VAR_SEQ 325..341
FT /note="IESRPQRRRPLRVVDGS -> VSSKEKLDPIISNSFQK (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037227"
FT VAR_SEQ 342..392
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037228"
FT CONFLICT 146
FT /note="L -> H (in Ref. 4; AAM10090/AAK68844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 43605 MW; 1B1468660C420BCE CRC64;
MALRCFPIWV CPQTTHHRSP LMGLAEFDAD KRRRFCLWEC SSSASQRAVT AIEGEIPFSR
ELKKSSDELG LTQETQSLSF HRDLSMLPKP LTANSLYSSD GDDSKVRISF QGIPGAYSET
AALKAFPNCE TVPCEQFEAA FQAVELWLVD KAVLPIENSV GGSIHRNYDL LLRHRLHIVQ
EVHLPVNHCL LGVPGVKKED IKCVLSHPQA LDQCVNSLNN LGIQRISAKD TATAAQTVSS
SGKIDVGAIA SVRAANIYGL DILAENIQDD VNNVTRFLIL AREPMIPRTD RPYKTSIVFS
LEEGPGVLFK ALAVFALRSI NLSKIESRPQ RRRPLRVVDG SNNGSAKYFD YLFYIDFEAS
MADTRAQHAL GHLQEFASFI RILGCYPMDL VR
