ID   TDC2_CAMAC              Reviewed;         498 AA.
AC   P93083;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tryptophan decarboxylase TDC2 {ECO:0000305};
DE            EC=4.1.1.105 {ECO:0000269|PubMed:9225462};
GN   Name=TDC2 {ECO:0000303|PubMed:9225462};
OS   Camptotheca acuminata (Happy tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Cornales; Nyssaceae; Camptotheca.
OX   NCBI_TaxID=16922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP   METHYL JASMONATE.
RC   TISSUE=Leaf;
RX   PubMed=9225462; DOI=10.1046/j.1365-313x.1997.11061167.x;
RA   Lopez-Meyer M., Nessler C.L.;
RT   "Tryptophan decarboxylase is encoded by two autonomously regulated genes in
RT   Camptotheca acuminata which are differentially expressed during development
RT   and stress.";
RL   Plant J. 11:1167-1175(1997).
CC   -!- FUNCTION: Involved in the biosynthesis of tryptamine. Supplies
CC       tryptamine for the indole moiety of camptothecin (CPT), an anti-cancer
CC       monoterpene alkaloid. Represents a key step in monoterpene indole
CC       alkaloid biosynthesis. Is specific for tryptophan, and inactive against
CC       tyrosine, phenylalanine and 3,4-dihydroxyphenylalanine (dopa).
CC       {ECO:0000269|PubMed:9225462}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-tryptophan = CO2 + tryptamine; Xref=Rhea:RHEA:30339,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57887,
CC         ChEBI:CHEBI:57912; EC=4.1.1.105;
CC         Evidence={ECO:0000269|PubMed:9225462};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P80041};
CC   -!- INDUCTION: Induced by methyl jasmonate. {ECO:0000269|PubMed:9225462}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U73657; AAB39709.1; -; Genomic_DNA.
DR   AlphaFoldDB; P93083; -.
DR   SMR; P93083; -.
DR   KEGG; ag:AAB39709; -.
DR   BioCyc; MetaCyc:MON-15094; -.
DR   BRENDA; 4.1.1.105; 7029.
DR   GO; GO:0036469; F:L-tryptophan decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IDA:UniProtKB.
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   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..498
FT                   /note="Tryptophan decarboxylase TDC2"
FT                   /id="PRO_0000444192"
FT   MOD_RES         316
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
SQ   SEQUENCE   498 AA;  55388 MW;  FB00D93C4D4D0A43 CRC64;
     MGSIDSNYDT ESAGQCRPLE PEEFRKQAHQ MVDFIADYYK NIESYPVLSQ VEPGYLQSRL
     PETAPYRPEP FESILKDVHK DIIPGVTHWL SPNFFAYFPA TVSSAAFVGE MLCTCFNAVG
     FNWLASPAEL ELEMVVMDWL ASMLKLPNSF TFLGTGGGVI QGTTSEAILC TLIAARDRAL
     ESIGVDSIHK LVVYGSDQTH STYAKACNLA GILPCNIRSI RTEAVANFSL SPDSLHREIE
     ADVAAGMVPL YLCATVGTTS TTAIDSLSPL ADVANDYGLW FHVDAAYAGS ACICPEFRHY
     LDGIERADSL SLSPHKWLLS YLDCCCLWVK RPSVLVKALS TDPEYLKNKP SESNSVVDFK
     DWQVGTGRRF KALRLWFVMR SYGVANLQSH IRSDIQMAKM FEEFVNSDPR FEIVVPRVFS
     LVCFRLNPFS KSDPCNTELL NRKLLEWVNS TGQVYITHTK VGGVYMLRFA VGATLTEEHH
     VSAAWKLIRE GADALLCS