ID   TYDC1_NARPS             Reviewed;         515 AA.
AC   A0A2H5AIY0;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Tyrosine decarboxylase 1 {ECO:0000303|PubMed:29229969};
DE            EC=4.1.1.25 {ECO:0000305|PubMed:29229969};
GN   Name=TYDC1 {ECO:0000303|PubMed:29229969};
OS   Narcissus pseudonarcissus (Daffodil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Amaryllidoideae; Narcissus.
OX   NCBI_TaxID=39639;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP   METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. King Alfred; TISSUE=Bulb;
RX   PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA   Singh A., Desgagne-Penix I.;
RT   "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT   Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL   Sci. Rep. 7:17356-17356(2017).
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to tyramine,
CC       which is converted to norbelladine, a precursor to all Amaryllidaceae
CC       alkaloids such as galanthamine, lycorine and haemanthamine, and
CC       including haemanthamine- and crinamine-type alkaloids, promising
CC       anticancer agents. {ECO:0000303|PubMed:29229969}.
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         Evidence={ECO:0000305|PubMed:29229969};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P20711};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in bulbs, and, to a lower extent,
CC       in stems, roots, leaves and flowers. {ECO:0000269|PubMed:29229969}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; MF405171; AUG71932.1; -; mRNA.
DR   AlphaFoldDB; A0A2H5AIY0; -.
DR   SMR; A0A2H5AIY0; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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   Alkaloid metabolism; Decarboxylase; Lyase; Pyridoxal phosphate; Repeat.
FT   CHAIN           1..515
FT                   /note="Tyrosine decarboxylase 1"
FT                   /id="PRO_0000450638"
FT   REPEAT          81..138
FT                   /note="1"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   REPEAT          141..192
FT                   /note="2"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   REGION          81..192
FT                   /note="2 X approximate tandem repeats"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
FT   BINDING         169
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         170
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
FT   BINDING         264
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         318
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
SQ   SEQUENCE   515 AA;  57622 MW;  BF3354EE890E245F CRC64;
     MGSLGSDNIA ELEANGSAFN LNPLDPEEFR RQGHMVIDFL ADYYQNVHKY PVRSQVEPGY
     LKKILPESAP NQPESLETIL DDITNHIVPG ITHWMSPNYF AYFPASGSTA GFLGEMLSTG
     FNAVCFNWMS SPAATELETI VTDWLGKLLA LPEKFLFSGG GGGVLQGTTC EAILCTMTAA
     RDKVLNKIGK DQIGKLVVYG SDQTHCALQK AAQIAGIHPA NFRAVRTFKS DAFGLNPEEL
     RKVVSADVEA GLVPLYLCPT VGTTSSTAVD QLRGLCSVAE EHEMWVHVDA AYAGSACICP
     EFRHFIDGVE GATSFSFNAH KWFFTNLDCC CLWVREPQAL INALSTNPEY LRNKATESQK
     VVDYKDWQIA LSRRFRAMKL WMVMRSYGVA NLRNFLRSHV KMAKLFEGLV SADERFEIVV
     PRNFAMVCFR FNPTKKDRAT GPELDRINEF NRRLLEEVNS TGRLYMTHAV IGGEYVMRFA
     TGATLTEEKH VRCAWRAIQE HAAALMEKIY YKQRN