TYRA1_ARATH
ID TYRA1_ARATH Reviewed; 640 AA.
AC Q944B6; O82603;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Arogenate dehydrogenase 1, chloroplastic;
DE EC=1.3.1.78;
DE AltName: Full=TYRATC;
DE AltName: Full=TyrAAT1;
DE Flags: Precursor;
GN Name=TYRAAT1; OrderedLocusNames=At5g34930; ORFNames=T2L5.1;
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], INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LACK OF PROCESSING.
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: Involved in the biosynthesis of tyrosine. Has no prephenate
CC 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=10.2 uM for NADP {ECO:0000269|PubMed:11905963,
CC ECO:0000269|PubMed:12354106};
CC KM=52.6 uM for arogenate {ECO:0000269|PubMed:11905963,
CC ECO:0000269|PubMed:12354106};
CC Vmax=142 umol/min/mg enzyme {ECO:0000269|PubMed:11905963,
CC ECO:0000269|PubMed:12354106};
CC Note=NADP increases the apparent affinity for arogenate. The two
CC active domains have the same KM values 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 {ECO:0000305}.
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 {ECO:0000269|PubMed:11905963}.
CC -!- MISCELLANEOUS: Unlike TYRAAT2, TYRAAT1 is composed of two highly
CC similar and catalytically active peptide domains. No proteolytic
CC cleavage between the two domains.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62791.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF434681; AAL30405.1; -; mRNA.
DR EMBL; AF096371; AAC62791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB028613; BAB10786.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93921.1; -; Genomic_DNA.
DR PIR; T01952; T01952.
DR RefSeq; NP_001331736.1; NM_001344090.1.
DR RefSeq; NP_198343.1; NM_122884.2.
DR AlphaFoldDB; Q944B6; -.
DR SMR; Q944B6; -.
DR BioGRID; 18693; 1.
DR STRING; 3702.AT5G34930.1; -.
DR iPTMnet; Q944B6; -.
DR PaxDb; Q944B6; -.
DR PRIDE; Q944B6; -.
DR ProteomicsDB; 242803; -.
DR EnsemblPlants; AT5G34930.1; AT5G34930.1; AT5G34930.
DR GeneID; 833436; -.
DR Gramene; AT5G34930.1; AT5G34930.1; AT5G34930.
DR KEGG; ath:AT5G34930; -.
DR Araport; AT5G34930; -.
DR TAIR; locus:2183532; AT5G34930.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_442363_0_0_1; -.
DR InParanoid; Q944B6; -.
DR OMA; YNANAME; -.
DR OrthoDB; 655176at2759; -.
DR PhylomeDB; Q944B6; -.
DR BioCyc; ARA:AT5G34930-MON; -.
DR BioCyc; MetaCyc:AT5G34930-MON; -.
DR BRENDA; 1.3.1.78; 399.
DR SABIO-RK; Q944B6; -.
DR UniPathway; UPA00122; UER00960.
DR PRO; PR:Q944B6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q944B6; baseline and differential.
DR Genevisible; Q944B6; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR InterPro; IPR045011; TYRAAT1/2.
DR PANTHER; PTHR43207; PTHR43207; 2.
DR Pfam; PF02153; PDH; 2.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR PROSITE; PS51176; PDH_ADH; 2.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW NADP; Oxidoreductase; Plastid; Reference proteome; Repeat; Transit peptide;
KW Tyrosine biosynthesis.
FT TRANSIT 1..18
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 19..640
FT /note="Arogenate dehydrogenase 1, chloroplastic"
FT /id="PRO_0000269677"
FT DOMAIN 53..334
FT /note="Prephenate/arogenate dehydrogenase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT DOMAIN 365..640
FT /note="Prephenate/arogenate dehydrogenase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
SQ SEQUENCE 640 AA; 72301 MW; 3D9922F91B8FF810 CRC64;
MAETLITKPP LSLSFTSLSS MLPSLSLSTA NRHLSVTDTI PLPNSNSNAT PPLRIAIIGF
GNYGQFLAET LISQGHILFA HSRSDHSSAA RRLGVSYFTD LHDLCERHPD VVLLCTSILS
IENILKTLPF QRLRRNTLFV DVLSVKEFAK TLLLQYLPED FDILCTHPMF GPQSVSSNHG
WRGLRFVYDK VRIGEERLRV SRCESFLEIF VREGCEMVEM SVTDHDKFAA ESQFITHTLG
RLLGMLKLIS TPINTKGYEA LLDLAENICG DSFDLYYGLF VYNNNSLEVL ERIDLAFEAL
RKELFSRLHG VVRKQSFEGE AKKVHVFPNC GENDASLDMM RSEDVVVKYE YNSQVSGSVN
DGSRLKIGIV GFGNFGQFLG KTMVKQGHTV LAYSRSDYTD EAAKLGVSYF SDLDDLFEEH
PEVIILCTSI LSTEKVLESL PFQRLKRSTL FVDVLSVKEF PRNLFLQTLP QDFDILCTHP
MFGPESGKNG WNNLAFVFDK VRIGMDDRRK SRCNSFLDIF AREGCRMVEM SCAEHDWHAA
GSQFITHTVG RLLEKLSLES TPIDTKGYET LLKLVENTAG DSFDLYYGLF LYNPNAMEQL
ERFHVAFESL KTQLFGRLHS QHSHELAKSS SPKTTKLLTS
