ID   TYDC3_PETCR             Reviewed;         516 AA.
AC   Q06087;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Tyrosine decarboxylase 3;
DE            EC=4.1.1.25;
GN   Name=TYRDC-3;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8420986; DOI=10.1016/s0021-9258(18)53980-6;
RA   Kawalleck P., Keller H., Hahlbrock K., Scheel D., Somssich I.E.;
RT   "A pathogen-responsive gene of parsley encodes tyrosine decarboxylase.";
RL   J. Biol. Chem. 268:2189-2194(1993).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA33862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M96071; AAA33861.1; ALT_INIT; mRNA.
DR   EMBL; M96072; AAA33862.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q06087; -.
DR   SMR; Q06087; -.
DR   PRIDE; Q06087; -.
DR   BRENDA; 4.1.1.25; 4694.
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   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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..516
FT                   /note="Tyrosine decarboxylase 3"
FT                   /id="PRO_0000146997"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  57633 MW;  5EA5BD3B6EAE2D5F CRC64;
     MGSIDNLTAQ KLTSSQFPMN TLEPEEFRRQ GHLMIDFLAD YYRKVENYPV RSQVSPGYLR
     EILPESAPYN PESLETILQD VQTKIIPGIT HWQSPNFFAY FPSSGSTAGF LGEMLSTGFN
     VVGFNWMVSP AATELENVVT DWFGKMLQLP KSFLFSGGGG GVLQGTTCEA ILCTLVAARD
     KNLRQHGMDN IGKLVVYCSD QTHSALQKAA KIAGIDPKNF RAIETTKSSN FKLCPKRLES
     AILYDLQNGL IPLYLCATVG TTSSTTVDPL PALTEVAKKY DLWVHVDAAY AGSACICPEF
     RQYLDGVENA DSFSLNAHKW FLTTLDCCCL WVRDPSALIK SLSTYPEFLK NNASETNKVV
     DYKDWQIMLS RRFRALKLWF VLRSYGVGQL REFIRGHVGM AKYFEGLVGL DKRFEVVAPR
     LFSMVCFRIK PSAMIGKNDE NEVNEINRKL LESVNDSGRI YVSHTVLGGI YVIRFAIGGT
     LTDINHVSAA WKVLQDHADA LLDDAFLPKK IVNILS