ID AROD6_ARATH Reviewed; 413 AA.
AC Q9SGD6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Arogenate dehydratase/prephenate dehydratase 6, chloroplastic {ECO:0000305};
DE Short=AtADT6 {ECO:0000303|PubMed:17726025};
DE Short=AtPDT6 {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=ADT6 {ECO:0000303|PubMed:17726025};
GN Synonyms=PDT6 {ECO:0000303|PubMed:17726025};
GN OrderedLocusNames=At1g08250 {ECO:0000312|Araport:AT1G08250};
GN ORFNames=T23G18.10 {ECO:0000312|EMBL:AAF18250.1};
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=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].
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=2.58 mM for arogenate {ECO:0000269|PubMed:17726025};
CC KM=2.44 mM for prephenate {ECO:0000269|PubMed:17726025};
CC Vmax=42.61 pmol/sec/ug enzyme with arogenate as substrate
CC {ECO:0000269|PubMed:17726025};
CC Vmax=0.4 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. {ECO:0000305}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19136569}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:17726025}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ411468; ABD67754.1; -; mRNA.
DR EMBL; AC011438; AAF18250.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28265.1; -; Genomic_DNA.
DR EMBL; AY056290; AAL07139.1; -; mRNA.
DR EMBL; AY091181; AAM14120.1; -; mRNA.
DR PIR; E86216; E86216.
DR RefSeq; NP_563809.1; NM_100698.4.
DR AlphaFoldDB; Q9SGD6; -.
DR SMR; Q9SGD6; -.
DR STRING; 3702.Q9SGD6; -.
DR PaxDb; 3702-AT1G08250-1; -.
DR ProteomicsDB; 247000; -.
DR EnsemblPlants; AT1G08250.1; AT1G08250.1; AT1G08250.
DR GeneID; 837345; -.
DR Gramene; AT1G08250.1; AT1G08250.1; AT1G08250.
DR KEGG; ath:AT1G08250; -.
DR Araport; AT1G08250; -.
DR TAIR; AT1G08250; ADT6.
DR eggNOG; KOG2797; Eukaryota.
DR HOGENOM; CLU_035008_4_1_1; -.
DR InParanoid; Q9SGD6; -.
DR OMA; SEWQSSC; -.
DR PhylomeDB; Q9SGD6; -.
DR BioCyc; ARA:AT1G08250-MONOMER; -.
DR BRENDA; 4.2.1.91; 399.
DR SABIO-RK; Q9SGD6; -.
DR UniPathway; UPA00121; UER00344.
DR UniPathway; UPA00121; UER00345.
DR PRO; PR:Q9SGD6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGD6; differential.
DR Genevisible; Q9SGD6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0047769; F:arogenate dehydratase activity; IDA:TAIR.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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:SF41; AROGENATE DEHYDRATASE_PREPHENATE DEHYDRATASE 6, CHLOROPLASTIC; 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; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Phenylalanine biosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..413
FT /note="Arogenate dehydratase/prephenate dehydratase 6,
FT chloroplastic"
FT /id="PRO_0000373795"
FT DOMAIN 117..294
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 308..399
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ SEQUENCE 413 AA; 44802 MW; 70099DC47A932022 CRC64;
MKALSSSSPI LGASQPATAT ALIARSGRSE WQSSCAILTS KVISQEESES LPVPPVSGGV
DHLNGHNSAA ARVPGMNLVP IEKSDSNPLV PQHRHNPLKP LSMTDLSPAP MHGSNLRVAY
QGVPGAYSEA AAGKAYPNCQ AIPCDQFEVA FQAVELWIAD RAVLPVENSL GGSIHRNYDL
LLRHRLHIVG EVQLPVHHCL LALPGVRKEF LTRVISHPQG LAQCEHTLTK LGLNVAREAV
DDTAGAAEFI ASNNLRDTAA IASARAAEIY GLEILEDGIQ DDVSNVTRFV MLAREPIIPR
TDRPFKTSIV FAHEKGTSVL FKVLSAFAFR DISLTKIESR PNHNRPIRVV DDANVGTAKH
FEYMFYVDFE ASMAEARAQN ALAEVQEFTS FLRVLGSYPM DMTPWSPTSS TSS
//
