ID   TYDC4_PETCR             Reviewed;         508 AA.
AC   Q06088;
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 4;
DE            EC=4.1.1.25;
GN   Name=TYRDC-4;
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}.
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DR   EMBL; M95685; AAA33863.1; -; mRNA.
DR   AlphaFoldDB; Q06088; -.
DR   SMR; Q06088; -.
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..508
FT                   /note="Tyrosine decarboxylase 4"
FT                   /id="PRO_0000146998"
FT   MOD_RES         318
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  56771 MW;  F626236B8EF39B29 CRC64;
     MGSIDNLMAQ KLTSQFPMNT LEPEEFRRQG HLMIDFLADY YRKVENYPVR SQVSPGYLRE
     ILPESAPYNP ESLETILQDV QTKIIPGITH WQSPNFFAYF PSSGSTAGFL GEMLSTGFNV
     VGFNWMVSPA ATELENVVTD WFGKMLQLPK SFLFSGGGGG VLQGTTCEAI LCTLVAARDK
     NLRQHGMDNI GKLVVYCSDQ THSALQKAAK IAGIDPKNFR AIETTKSSNF KLCPKRLESA
     ILYDLQNGLI PLYLCATVGT TSSTTVDPLP ALTEVAKKYD LWVHVDAAYA GSACICPEFR
     QYLDGVENAD SFSLNAHKWF LTTLDCCCLW VRDPSALIKS LSTYPEFLKN NASETNKVVD
     YKDWQIMLSR RFRALKLWFV LRSYGVGQLR EFIRGHVGMA KYFEGLVGLD KRFEVVAPRL
     FSMVCFRIKP SAMIGKNDED EVNEINRKLL ESVNDSGRIY VSHTVLGGIY VIRFAIGGTL
     TDINHVSAAW KVLQDHADAL LDEAFTAN