ID   TDC1_CAMAC              Reviewed;         502 AA.
AC   P93082; A0A1C9CX68;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tryptophan decarboxylase TDC1 {ECO:0000305};
DE            EC=4.1.1.105 {ECO:0000269|PubMed:27432874, ECO:0000269|PubMed:9225462};
GN   Name=TDC1 {ECO:0000303|PubMed:27432874, 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 TISSUE
RP   SPECIFICITY.
RC   TISSUE=Seedling;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=27432874; DOI=10.1105/tpc.16.00193;
RA   Sadre R., Magallanes-Lundback M., Pradhan S., Salim V., Mesberg A.,
RA   Jones A.D., DellaPenna D.;
RT   "Metabolite diversity in alkaloid biosynthesis: a multilane (diastereomer)
RT   highway for camptothecin synthesis in Camptotheca acuminata.";
RL   Plant Cell 28:1926-1944(2016).
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:27432874, 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:27432874, ECO:0000269|PubMed:9225462};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P80041};
CC   -!- TISSUE SPECIFICITY: Highly expressed in apex. Expressed in young stem
CC       and bark tissues. Expressed at low levels in leaves, fruits and seeds.
CC       {ECO:0000269|PubMed:9225462}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; U73656; AAB39708.1; -; mRNA.
DR   EMBL; KU842377; AON76721.1; -; mRNA.
DR   AlphaFoldDB; P93082; -.
DR   SMR; P93082; -.
DR   KEGG; ag:AAB39708; -.
DR   BioCyc; MetaCyc:MON-15093; -.
DR   BRENDA; 4.1.1.105; 7029.
DR   BRENDA; 4.1.1.28; 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..502
FT                   /note="Tryptophan decarboxylase TDC1"
FT                   /id="PRO_0000444191"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P80041"
FT   CONFLICT        59
FT                   /note="R -> L (in Ref. 2; AON76721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="G -> P (in Ref. 2; AON76721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="H -> Y (in Ref. 2; AON76721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179..183
FT                   /note="SPMHF -> RDRAL (in Ref. 2; AON76721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190..194
FT                   /note="TSTSF -> NFNKL (in Ref. 2; AON76721)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  55495 MW;  A4108BA27654F0FB CRC64;
     MGSLDSNYDT ESPASVGQFN PLDPEEFRKQ AHCIVDFIAD YYKNIESYPV LSQVDPGYRH
     SRLGKNAPYR SEPFESILKD VQKDIIPGMT HWMSPNFFAH FPATVSSAAF VGEMLCTCFN
     SVGFNWLASP AATELEMVVI DWLANMLKLP KSFMFSGTGG GVLQGTTSEA ILCTLIAASP
     MHFEIVGVKT STSFVVYGSD QTHSTYAKAC KLAGILPCNI RSIPTTADSN FSVSPLLLRR
     AIEADKAAGM VPLYICATVG TTSTTAIDPL SSLADVANDY GVWFHVDAAY AGSACICPEF
     RHYLDGIERA DSLSLSPHKW LLSYLDCCCL WVKSPSLLVK ALSTDPEYLK NQPSESKSVV
     DYKDWQVGTG RRFKALRLWF VMRSYGVANL QSHIRTDVQM AKMFEGFVKS DPRFEILVPR
     VFSLVCFRLN PISGSDPTGT EALNRKLLDW VNSTGRVYMT HTKVGGIYML RFAVGATLTE
     KRHVSSAWKL IKEGADVLLK ED