ID   TYDC3_PAPSO             Reviewed;         533 AA.
AC   P54770;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tyrosine/DOPA decarboxylase 3;
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=TYDC3;
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RC   STRAIN=cv. Marianne; TISSUE=Leaf;
RX   PubMed=9733527; DOI=10.1104/pp.118.1.69;
RA   Facchini P.J., Penzes-Yost C., Samanani N., Kowalchuk B.;
RT   "Expression patterns conferred by tyrosine/dihydroxyphenylalanine
RT   decarboxylase promoters from opium poppy are conserved in transgenic
RT   tobacco.";
RL   Plant Physiol. 118:69-81(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-533.
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: Roots. {ECO:0000269|PubMed:9733527}.
CC   -!- DEVELOPMENTAL STAGE: Seedlings and mature plants.
CC       {ECO:0000269|PubMed:9733527}.
CC   -!- INDUCTION: By fungal elicitor. {ECO:0000269|PubMed:9733527}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF025431; AAC61840.1; -; Genomic_DNA.
DR   EMBL; U08599; AAA62348.1; -; mRNA.
DR   PIR; C55066; C55066.
DR   PIR; T07970; T07970.
DR   AlphaFoldDB; P54770; -.
DR   SMR; P54770; -.
DR   PRIDE; P54770; -.
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: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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..533
FT                   /note="Tyrosine/DOPA decarboxylase 3"
FT                   /id="PRO_0000147001"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   533 AA;  59520 MW;  EAC9C271D77CDC22 CRC64;
     MGSLNTEDVL EHSSAFGATN PLDPEEFRRQ GHMIIDFLAD YYRDVEKYPV RSQVEPGYLR
     KRLPETAPYN PESIETILQD VTSEIIPGLT HWQSPNYYAY FPSSGSVAGF LGEMLSTGFN
     VVGFNWMSSP AATELEGIVM DWFGKMLNLP KSYLFSGTGG GVLQGTTCEA ILCTLTAARD
     RKLNKIGREH IGRLVVYGSD QTHCALQKAA QIAGINPKNF RAVKTFKANS FGLAASTLRE
     VILEDIEAGL IPLFVCPTVG TTSSTAVDPI GPICEVAKEY EMWVHIDAAY AGSACICPEF
     RHFIDGVEEA DSFSLNAHKW FFTTLDCCCL WVKDPSSLVK ALSTNPEYLR NKATESRQVV
     DYKDWQIALI RRFRSMKLWM VLRSYGVTNL RNFLRSHVRM AKTFEGLVGA DRRFEITVPR
     TFAMVCFRLL PPTTVKVCGE NGVHQNGNGV IAVLRNENEE LVLANKLNQV YLRQVKATGS
     VYMTHAVVGG VYMIRFAVGS TLTEERHVIH AWEVLQEHAD LILSKFDEAN FSS