ID   TYDC2_PAPSO             Reviewed;         531 AA.
AC   P54769;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Tyrosine/DOPA decarboxylase 2;
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=TYDC2;
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 [MRNA].
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 and stems,
CC       while a lower level expression is seen in the sepals and carpels of
CC       fully expanded flowers.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U08598; AAA62347.1; -; mRNA.
DR   PIR; B55066; B55066.
DR   PDB; 6LIU; X-ray; 2.80 A; A/B/C/D/E/F=1-531.
DR   PDB; 6LIV; X-ray; 2.31 A; A/B/C/D/E/F=1-531.
DR   PDBsum; 6LIU; -.
DR   PDBsum; 6LIV; -.
DR   AlphaFoldDB; P54769; -.
DR   SMR; P54769; -.
DR   EnsemblPlants; RZC68564; RZC68564; C5167_031851.
DR   Gramene; RZC68564; RZC68564; C5167_031851.
DR   OMA; DHIRSHI; -.
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   1: Evidence at protein level;
KW   3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..531
FT                   /note="Tyrosine/DOPA decarboxylase 2"
FT                   /id="PRO_0000147000"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           24..44
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           58..62
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           107..119
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           130..146
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           151..153
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   TURN            155..158
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           167..186
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           188..193
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          194..199
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           204..212
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           235..247
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          251..255
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          258..260
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   TURN            262..264
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           270..279
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           291..296
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           298..304
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          311..316
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           317..320
FT                   /evidence="ECO:0007829|PDB:6LIU"
FT   STRAND          328..333
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           335..342
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           347..350
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           362..365
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           375..410
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          414..416
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          422..429
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           458..475
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          483..486
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   STRAND          489..495
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           503..522
FT                   /evidence="ECO:0007829|PDB:6LIV"
FT   HELIX           526..528
FT                   /evidence="ECO:0007829|PDB:6LIV"
SQ   SEQUENCE   531 AA;  59362 MW;  DCE9DB9264250581 CRC64;
     MGSLNTEDVL ENSSAFGVTN PLDPEEFRRQ GHMIIDFLAD YYRDVEKYPV RSQVEPGYLR
     KRLPETAPYN PESIETILQD VTTEIIPGLT HWQSPNYYAY FPSSGSVAGF LGEMLSTGFN
     VVGFNWMSSP AATELESVVM DWFGKMLNLP ESFLFSGSGG GVLQGTSCEA ILCTLTAARD
     RKLNKIGREH IGRLVVYGSD QTHCALQKAA QVAGINPKNF RAIKTFKENS FGLSAATLRE
     VILEDIEAGL IPLFVCPTVG TTSSTAVDPI SPICEVAKEY EMWVHVDAAY AGSACICPEF
     RHFIDGVEEA DSFSLNAHKW FFTTLDCCCL WVKDPSALVK ALSTNPEYLR NKATESRQVV
     DYKDWQIALS RRFRSLKLWM VLRSYGVTNL RNFLRSHVKM AKTFEGLICM DGRFEITVPR
     TFAMVCFRLL PPKTIKVYDN GVHQNGNGVV PLRDENENLV LANKLNQVYL ETVNATGSVY
     MTHAVVGGVY MIRFAVGSTL TEERHVIYAW KILQEHADLI LGKFSEADFS S