ID   TYDC2_NARPS             Reviewed;         500 AA.
AC   A0A2H5AIY2;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Tyrosine decarboxylase 2 {ECO:0000303|PubMed:29229969};
DE            EC=4.1.1.25 {ECO:0000305|PubMed:29229969};
GN   Name=TYDC2 {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; MF405172; AUG71933.1; -; mRNA.
DR   AlphaFoldDB; A0A2H5AIY2; -.
DR   SMR; A0A2H5AIY2; -.
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..500
FT                   /note="Tyrosine decarboxylase 2"
FT                   /id="PRO_0000450639"
FT   REPEAT          65..122
FT                   /note="1"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   REPEAT          125..176
FT                   /note="2"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   REGION          65..176
FT                   /note="2 X approximate tandem repeats"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
FT   BINDING         153
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         154
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
FT   BINDING         248
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   BINDING         302
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20711"
SQ   SEQUENCE   500 AA;  55640 MW;  FEDAD9D8911BDE0F CRC64;
     MEESLKPMDA EQLRENAHKM VDFIADYYKS IESFPVLSQV KPGYLRDLLP DSAPDHPESL
     EDVLEDIRQK IVPGVTHWQS PNYFAYYPSN SSVAGFLGEM ISAGFNIVGF NWIASPAATE
     LEVIVLDWLA KMLNLPNQFL SSGQGGGVIQ GTASEANLVV LLAARDKFLN RFGKRSLEKL
     VVYASDQTHA AMKKACQIAG IYPENFRVLN ADHTSNYALV PEALSDAISN DLSAGLIPFF
     LCATVGTTSS AAVDPLSELG KISKVNDMWF HVDAAYAGSA CICPEYRHYI DGIEEAASFN
     MNAHKWFLTN FDCSLLWIKD RSALIQSLST YPEYLKNKAS QENSVVDFKD WQIPLGRRFR
     SLKLWMVLRL YGLENLQSYI RNHIKLAGQF EQLVCSDSRF EVVVPRTFSL VCFRLLPPPN
     HQDNGYKLNH SLLDAVNSSG KIFVSHTVLS GKYVIRFAVG APLTEEEHIK QAWKVFQDQA
     TILLAGSDGS DFGASNGDII