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Database: UniProt
Entry: Q9SGD6
LinkDB: Q9SGD6
Original site: Q9SGD6 
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   03-AUG-2022, entry version 116.
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}.
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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.AT1G08250.1; -.
DR   PaxDb; Q9SGD6; -.
DR   PRIDE; Q9SGD6; -.
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; locus:2199963; AT1G08250.
DR   eggNOG; KOG2797; Eukaryota.
DR   HOGENOM; CLU_035008_4_1_1; -.
DR   InParanoid; Q9SGD6; -.
DR   OMA; YPNITIC; -.
DR   PhylomeDB; Q9SGD6; -.
DR   BioCyc; ARA:AT1G08250-MON; -.
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: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:UniProtKB-EC.
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..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
//
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