ID   TYDC5_PAPSO             Reviewed;         523 AA.
AC   P54771;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Tyrosine/DOPA decarboxylase 5;
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=TYDC5;
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. UNL186;
RX   PubMed=8587993; DOI=10.1104/pp.110.1.43;
RA   Maldonado-Mendoza I.E., Lopez-Meyer M., Galef J.R., Burnett R.J.,
RA   Nessler C.L.;
RT   "Molecular analysis of a new member of the opium poppy tyrosine/3,4-
RT   dihydroxyphenylalanine decarboxylase gene family.";
RL   Plant Physiol. 110:43-49(1996).
CC   -!- FUNCTION: May play an important role in providing precursors for
CC       alkaloid synthesis in the roots and germinating seedlings.
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.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U16804; AAA97535.1; -; Genomic_DNA.
DR   PIR; T09615; T09615.
DR   AlphaFoldDB; P54771; -.
DR   SMR; P54771; -.
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..523
FT                   /note="Tyrosine/DOPA decarboxylase 5"
FT                   /id="PRO_0000147002"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  57304 MW;  81BA6764AC1EE8DA CRC64;
     MGSLPTDNLE SMSICSQNPL DPDEFRRQGH MIIDFLADYY KNVKVSSRSQ ANPGSQQTLP
     ETAPNHSESI ETILQDVQND IIPGITHWQS PNYFAYFPSS GSVAGFLGEM LSSGFNVVGF
     NWMSSPAATE LESIVMNWLG QMLNLPKSFL FSSDDNAGSS GGGVLQGTTC EAILCTLTAS
     RDKMLNKIGR ENINKLVVYA SDQTHCALQK AAQIAGINPK NFRAIATSKA TDFGLSPQAL
     LSTILADIES GLVPLFLCAT VGTTSSTAVD PIGPLCEVAK QFGIWVHVDA AYAGSACICP
     EFRHFIDGVE EADSFSLNAH KWFFTTLDCC CLWVKDSNAL VKALSTSPEY LKNKATDSKQ
     VIDYKDWQIA LSRRFRSMKL WLVLRSYGVA NLRSFLRSHV KMAKHFDGLI AMDKRFEIVV
     PNTFAMVCFR LKPAAIFNGK LGENGVDYNC IEEKTNEINS KLLESVNASG SIYMTHAVVG
     GVYMIRFAVG ATLTEERHVS MAWKVIQEHT DAILGTVDDS VVA