TYRA2_ARATH
ID TYRA2_ARATH Reviewed; 358 AA.
AC Q9LMR3; Q8L7Z4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Arogenate dehydrogenase 2, chloroplastic;
DE EC=1.3.1.78;
DE AltName: Full=TyrAAT2;
DE Flags: Precursor;
GN Name=TYRAAT2; OrderedLocusNames=At1g15710; ORFNames=F7H2.5;
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;
RX PubMed=11905963; DOI=10.1023/a:1014018926676;
RA Rippert P., Matringe M.;
RT "Molecular and biochemical characterization of an Arabidopsis thaliana
RT arogenate dehydrogenase with two highly similar and active protein
RT domains.";
RL Plant Mol. Biol. 48:361-368(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12354106; DOI=10.1046/j.1432-1033.2002.03172.x;
RA Rippert P., Matringe M.;
RT "Purification and kinetic analysis of the two recombinant arogenate
RT dehydrogenase isoforms of Arabidopsis thaliana.";
RL Eur. J. Biochem. 269:4753-4761(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [8]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in the biosynthesis of tyrosine. Has a weak
CC prephenate dehydrogenase activity. {ECO:0000269|PubMed:12354106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + NADP(+) = CO2 + L-tyrosine + NADPH;
CC Xref=Rhea:RHEA:15417, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58180, ChEBI:CHEBI:58315, ChEBI:CHEBI:58349; EC=1.3.1.78;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.3 uM for NADP {ECO:0000269|PubMed:12354106};
CC KM=84.2 uM for arogenate {ECO:0000269|PubMed:12354106};
CC KM=17000 uM for prephenate {ECO:0000269|PubMed:12354106};
CC Vmax=73 umol/min/mg enzyme {ECO:0000269|PubMed:12354106};
CC Note=NADP increases the apparent affinity for arogenate.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine
CC from L-arogenate (NADP(+) route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19136569}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers,
CC siliques and seeds. More abundant in seeds.
CC {ECO:0000269|PubMed:19136569}.
CC -!- INDUCTION: Strongly inhibited by tyrosine.
CC -!- MISCELLANEOUS: Unlike TYRAAT1, TYRAAT2 is composed of a single
CC catalytically active domain.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF434682; AAL30406.1; -; mRNA.
DR EMBL; AC034256; AAF82141.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29352.1; -; Genomic_DNA.
DR EMBL; AK221665; BAD95346.1; -; mRNA.
DR EMBL; AY123984; AAM74497.1; -; mRNA.
DR EMBL; BT000566; AAN18135.1; -; mRNA.
DR PIR; C86291; C86291.
DR RefSeq; NP_173023.1; NM_101439.5.
DR AlphaFoldDB; Q9LMR3; -.
DR SMR; Q9LMR3; -.
DR BioGRID; 23380; 4.
DR IntAct; Q9LMR3; 4.
DR STRING; 3702.AT1G15710.1; -.
DR PaxDb; Q9LMR3; -.
DR PRIDE; Q9LMR3; -.
DR ProteomicsDB; 242602; -.
DR EnsemblPlants; AT1G15710.1; AT1G15710.1; AT1G15710.
DR GeneID; 838140; -.
DR Gramene; AT1G15710.1; AT1G15710.1; AT1G15710.
DR KEGG; ath:AT1G15710; -.
DR Araport; AT1G15710; -.
DR TAIR; locus:2036164; AT1G15710.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_036672_0_1_1; -.
DR InParanoid; Q9LMR3; -.
DR OMA; KTHYQKS; -.
DR OrthoDB; 655176at2759; -.
DR PhylomeDB; Q9LMR3; -.
DR BioCyc; ARA:AT1G15710-MON; -.
DR BioCyc; MetaCyc:AT1G15710-MON; -.
DR BRENDA; 1.3.1.78; 399.
DR SABIO-RK; Q9LMR3; -.
DR UniPathway; UPA00122; UER00960.
DR PRO; PR:Q9LMR3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMR3; baseline and differential.
DR Genevisible; Q9LMR3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0033730; F:arogenate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR012070; Arogenate_DH_2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR045011; TYRAAT1/2.
DR PANTHER; PTHR43207; PTHR43207; 1.
DR Pfam; PF02153; PDH; 1.
DR PIRSF; PIRSF036577; PDH_ADH_plant; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Transit peptide;
KW Tyrosine biosynthesis.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 37..358
FT /note="Arogenate dehydrogenase 2, chloroplastic"
FT /id="PRO_0000269678"
FT DOMAIN 59..338
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 222
FT /note="V -> F (in Ref. 4; AAM74497/BAD95346 and 5;
FT AAN18135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40633 MW; DCEFA72C62D1AF78 CRC64;
MLLHFSPAKP LISPPNLRRN SPTFLISPPR SLRIRAIDAA QIFDYETQLK SEYRKSSALK
IAVLGFGNFG QFLSKTLIRH GHDLITHSRS DYSDAANSIG ARFFDNPHDL CEQHPDVVLL
CTSILSTESV LRSFPFQRLR RSTLFVDVLS VKEFPKALFI KYLPKEFDIL CTHPMFGPES
GKHSWSGLPF VYDKVRIGDA ASRQERCEKF LRIFENEGCK MVEMSCEKHD YYAAGSQFVT
HTMGRVLEKY GVESSPINTK GYETLLDLVE NTSSDSFELF YGLFMYNPNA LEQLERLDMA
FESVKKELFG RLHQQYRKQM FGGEVQSPKK TEQKLLNDGG VVPMNDISSS SSSSSSSS
