ID A0A1P8B7T7_ARATH Unreviewed; 381 AA.
AC A0A1P8B7T7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=L-tyrosine decarboxylase {ECO:0000313|EMBL:ANM67657.1};
GN Name=TYRDC {ECO:0000313|EMBL:ANM67657.1, ECO:0000313|TAIR:AT4G28680};
GN Synonyms=AtTYDC {ECO:0000313|EMBL:ANM67657.1}, L-tyrosine
GN decarboxylase {ECO:0000313|EMBL:ANM67657.1}, L-TYROSINE DECARBOXYLASE
GN 1 {ECO:0000313|EMBL:ANM67657.1}, TYDC {ECO:0000313|EMBL:ANM67657.1},
GN TYRDC1 {ECO:0000313|EMBL:ANM67657.1};
GN OrderedLocusNames=At4g28680 {ECO:0000313|Araport:AT4G28680,
GN ECO:0000313|EMBL:ANM67657.1};
GN ORFNames=T5F17.130 {ECO:0000313|EMBL:ANM67657.1}, T5F17_130
GN {ECO:0000313|EMBL:ANM67657.1};
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 {ECO:0000313|EMBL:ANM67657.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM67657.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617198; DOI=10.1038/47134;
RG EU;
RG CSHL and WU Arabidopsis Sequencing Project;
RA Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Kotter 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., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA Montfort 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., Sehkon 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., Nelson J.,
RA Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA 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., Hoffmann J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
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] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP002687; ANM67657.1; -; Genomic_DNA.
DR RefSeq; NP_001329474.1; NM_001341928.1.
DR AlphaFoldDB; A0A1P8B7T7; -.
DR SMR; A0A1P8B7T7; -.
DR EnsemblPlants; AT4G28680.6; AT4G28680.6; AT4G28680.
DR GeneID; 828986; -.
DR Gramene; AT4G28680.6; AT4G28680.6; AT4G28680.
DR Araport; AT4G28680; -.
DR TAIR; AT4G28680; TYRDC.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A0A1P8B7T7; baseline and differential.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF152; TYROSINE DECARBOXYLASE 2; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 1: Evidence at protein level;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8B7T7,
KW ECO:0007829|ProteomicsDB:A0A1P8B7T7};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT REGION 17..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 354
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 381 AA; 41509 MW; A7572096B0359948 CRC64;
MEFGTGNGYS NGNGYTNGNG HTNGNGNYNG NGHVNGNGKA NGAKVVKMKP MDSELLREQG
HIMVDFIADY YKNLQDSPQD FPVLSQVQPG YLRDMLPDSA PERPESLKEL LDDVSKKIMP
GITHWQSPSY FAYYASSTSV AGFLGEMLNA GLSVVGFTWL TSPAATELEI IVLDWLAKLL
QLPDHFLSTG KGNGGGVIQG TGCEAVLVVV LAARDRILKK VGKTLLPQLV VYGSDQTHSS
FRKACLIGGI HEENIRLLKT DSSTNYGMPP ESLEEAISHD LAKGFIPFFI CATVGTTSSA
AVDPLVPLGN IAKKYGIWLH VDAAYAGNAC ICPEYRKFID GIENADSFNM NAHKWLFANQ
TCSPLWVKVC WFYLILNLLF N
//
