ID TYDC1_PAPSO Reviewed; 518 AA. AC P54768; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Tyrosine/DOPA decarboxylase 1; DE Includes: DE RecName: Full=DOPA decarboxylase; DE Short=DDC; DE EC=4.1.1.28; DE Includes: DE RecName: Full=Tyrosine decarboxylase; DE EC=4.1.1.25; GN Name=TYDC1; OS Papaver somniferum (Opium poppy). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae; OC Papaver. OX NCBI_TaxID=3469; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Marianne; RX PubMed=7929401; DOI=10.1016/s0021-9258(18)47073-1; RA Facchini P.J., de Luca V.; RT "Differential and tissue-specific expression of a gene family for RT tyrosine/dopa decarboxylase in opium poppy."; RL J. Biol. Chem. 269:26684-26690(1994). CC -!- FUNCTION: Marginally higher substrate specificity for L-DOPA over L- CC tyrosine. 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 -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, CC ChEBI:CHEBI:59905; EC=4.1.1.28; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin; CC Xref=Rhea:RHEA:18533, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:58266, ChEBI:CHEBI:350546; EC=4.1.1.28; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Predominantly expressed in the roots. CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U08597; AAA62346.1; -; Genomic_DNA. DR PIR; A55066; A55066. DR AlphaFoldDB; P54768; -. DR SMR; P54768; -. DR BRENDA; 4.1.1.25; 4515. DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA. DR GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:RHEA. 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:amino acid metabolic process; IEA:InterPro. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. 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 InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR InterPro; IPR021115; Pyridoxal-P_BS. DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1. DR PANTHER; PTHR11999:SF96; TYROSINE DECARBOXYLASE; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR PRINTS; PR00800; YHDCRBOXLASE. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. PE 2: Evidence at transcript level; KW Decarboxylase; Lyase; Pyridoxal phosphate. FT CHAIN 1..518 FT /note="Tyrosine/DOPA decarboxylase 1" FT /id="PRO_0000146999" FT MOD_RES 321 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000250" SQ SEQUENCE 518 AA; 57020 MW; E63A53B45ECF2702 CRC64; MGSLPANNFE SMSLCSQNPL DPDEFRRQGH MIIDFLADYY KNVEKYPVRT QVDPGYLKKR LPESAPYNPE SIETILEDVT NDIIPGLTHW QSPNYFAYFP SSGSIAGFLG EMLSTGFNVV GFNWMSSPAA TELESIVMNW LGQMLTLPKS FLFSSDGSSG GGGVLQGTTC EAILCTLTAA RDKMLNKIGR ENINKLVVYA SDQTLSALQK AAQIAGINPK NFLAIATSKA TNFGLSPNSL QSTILADIES GLVPLFLCAT VGTTSSTAVD PIGPLCAVAK LHGIWVHIDA AYAGSACICP EFRHFIDGVE DADSFSLNAH KWFFTTLDCC CLWVKDSDSL VKALSTSPEY LKNKATDSKQ VIDYKDWQIA LSRRFRSMKL WLVLRSYGIA NLRTFLRSHV KMAKHFQGLI GMDNRFEIVV PRTFAMVCFR LKPAAIFRKK IVEDDHIEAQ TNEVNAKLLE SVNASGKIYM THAVVGGVYM IRFAVGATLT EERHVTGAWK VVQEHTDAIL GALGEDVC //