TYDC2_ARATH
ID TYDC2_ARATH Reviewed; 545 AA.
AC Q9M0G4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tyrosine decarboxylase 2 {ECO:0000305};
DE Short=AtTYDC {ECO:0000303|PubMed:21284755};
DE EC=4.1.1.25 {ECO:0000269|PubMed:19450582};
DE AltName: Full=TyrDC-like protein {ECO:0000303|PubMed:19450582};
GN Name=TYRDC {ECO:0000303|PubMed:19450582};
GN Synonyms=TYDC {ECO:0000303|PubMed:21284755};
GN OrderedLocusNames=At4g28680 {ECO:0000312|Araport:AT4G28680};
GN ORFNames=T5F17.130 {ECO:0000312|EMBL:CAB81456.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19450582; DOI=10.1016/j.febslet.2009.05.017;
RA Lehmann T., Pollmann S.;
RT "Gene expression and characterization of a stress-induced tyrosine
RT decarboxylase from Arabidopsis thaliana.";
RL FEBS Lett. 583:1895-1900(2009).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21284755; DOI=10.1111/j.1365-313x.2011.04515.x;
RA Gutensohn M., Klempien A., Kaminaga Y., Nagegowda D.A., Negre-Zakharov F.,
RA Huh J.H., Luo H., Weizbauer R., Mengiste T., Tholl D., Dudareva N.;
RT "Role of aromatic aldehyde synthase in wounding/herbivory response and
RT flower scent production in different Arabidopsis ecotypes.";
RL Plant J. 66:591-602(2011).
CC -!- FUNCTION: Converts tyrosine into tyramine, a precursor of isoquinoline
CC alkaloids and various amides. {ECO:0000269|PubMed:19450582,
CC ECO:0000269|PubMed:21284755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-tyrosine = CO2 + tyramine; Xref=Rhea:RHEA:14345,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58315,
CC ChEBI:CHEBI:327995; EC=4.1.1.25;
CC Evidence={ECO:0000269|PubMed:19450582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14346;
CC Evidence={ECO:0000269|PubMed:19450582};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19450582};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=745 uM for L-tyrosine {ECO:0000269|PubMed:19450582};
CC Vmax=61.35 nmol/sec/mg enzyme with L-tyrosine as substrate
CC {ECO:0000269|PubMed:19450582};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19450582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19450582}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M0G4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed specifically in flowers.
CC {ECO:0000269|PubMed:21284755}.
CC -!- INDUCTION: Induced by drougt stress, wounding and methyl jasmonate.
CC {ECO:0000269|PubMed:19450582}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction of pollen grain size.
CC {ECO:0000269|PubMed:21284755}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AL049917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161573; CAB81456.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85522.1; -; Genomic_DNA.
DR PIR; T10662; T10662.
DR RefSeq; NP_194597.1; NM_119010.3. [Q9M0G4-1]
DR AlphaFoldDB; Q9M0G4; -.
DR SMR; Q9M0G4; -.
DR STRING; 3702.AT4G28680.3; -.
DR PaxDb; Q9M0G4; -.
DR EnsemblPlants; AT4G28680.1; AT4G28680.1; AT4G28680. [Q9M0G4-1]
DR GeneID; 828986; -.
DR Gramene; AT4G28680.1; AT4G28680.1; AT4G28680. [Q9M0G4-1]
DR KEGG; ath:AT4G28680; -.
DR Araport; AT4G28680; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; Q9M0G4; -.
DR OMA; IPCYVVA; -.
DR PhylomeDB; Q9M0G4; -.
DR BioCyc; ARA:AT4G28680-MON; -.
DR PRO; PR:Q9M0G4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0G4; baseline and differential.
DR Genevisible; Q9M0G4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..545
FT /note="Tyrosine decarboxylase 2"
FT /id="PRO_0000146994"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:O82415"
FT BINDING 360
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:O82415"
FT BINDING 390
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:O82415"
FT MOD_RES 361
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O82415"
SQ SEQUENCE 545 AA; 60804 MW; 96D297C718BE9031 CRC64;
MFKPQHMYDR EFGTGNGYSN GNGYTNGNGH TNGNGNYNGN GHVNGNGKAN GAKVVKMKPM
DSELLREQGH IMVDFIADYY KNLQDSPQDF PVLSQVQPGY LRDMLPDSAP ERPESLKELL
DDVSKKIMPG ITHWQSPSYF AYYASSTSVA GFLGEMLNAG LSVVGFTWLT SPAATELEII
VLDWLAKLLQ LPDHFLSTGN GGGVIQGTGC EAVLVVVLAA RDRILKKVGK TLLPQLVVYG
SDQTHSSFRK ACLIGGIHEE NIRLLKTDSS TNYGMPPESL EEAISHDLAK GFIPFFICAT
VGTTSSAAVD PLVPLGNIAK KYGIWLHVDA AYAGNACICP EYRKFIDGIE NADSFNMNAH
KWLFANQTCS PLWVKDRYSL IDALKTNPEY LEFKVSKKDT VVNYKDWQIS LSRRFRSLKL
WMVLRLYGSE NLRNFIRDHV NLAKHFEDYV AQDPSFEVVT TRYFSLVCFR LAPVDGDEDQ
CNERNRELLA AVNSTGKIFI SHTALSGKFV LRFAVGAPLT EEKHVTEAWQ IIQKHASKFT
RNDHY
