TDC_CATRO
ID TDC_CATRO Reviewed; 500 AA.
AC P17770; A0A3S7SKS7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000305};
DE Short=AADC {ECO:0000305};
DE EC=4.1.1.28 {ECO:0000269|PubMed:23204519};
DE AltName: Full=DOPA decarboxylase {ECO:0000305};
DE AltName: Full=Tryptophan decarboxylase {ECO:0000303|PubMed:23204519};
GN Name=TDC {ECO:0000303|PubMed:23204519};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2704736; DOI=10.1073/pnas.86.8.2582;
RA de Luca V., Marineau C., Brisson N.;
RT "Molecular cloning and analysis of cDNA encoding a plant tryptophan
RT decarboxylase: comparison with animal dopa decarboxylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2582-2586(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Morning mist; TISSUE=Leaf;
RX PubMed=8159173; DOI=10.1007/bf00391016;
RA Goddijn O.J.M., Lohman F.P., de Kam R.J., Schilperoort R.A., Hoge J.H.C.;
RT "Nucleotide sequence of the tryptophan decarboxylase gene of Catharanthus
RT roseus and expression of tdc-gusA gene fusions in Nicotiana tabacum.";
RL Mol. Gen. Genet. 242:217-225(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN
RP COMPLEX WITH L-TRYPTOPHAN AND PYRIDOXAL PHOSPHATE, AND SUBUNIT.
RA Torrens-Spence M.P., Chiang Y.-C., Smith T., Vicent M.A., Wang Y.,
RA Weng J.-K.;
RT "Structural basis for independent origins of new catalytic machineries in
RT plant AAAD proteins.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-348.
RX PubMed=23204519; DOI=10.1074/jbc.m112.401752;
RA Torrens-Spence M.P., Liu P., Ding H., Harich K., Gillaspy G., Li J.;
RT "Biochemical evaluation of the decarboxylation and decarboxylation-
RT deamination activities of plant aromatic amino acid decarboxylases.";
RL J. Biol. Chem. 288:2376-2387(2013).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-370.
RX PubMed=25107664; DOI=10.1016/j.phytochem.2014.07.007;
RA Torrens-Spence M.P., Lazear M., von Guggenberg R., Ding H., Li J.;
RT "Investigation of a substrate-specifying residue within Papaver somniferum
RT and Catharanthus roseus aromatic amino acid decarboxylases.";
RL Phytochemistry 106:37-43(2014).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-tryptophan to tryptamine
CC and L-5-hydroxytryptophan to serotonin, respectively.
CC {ECO:0000269|PubMed:23204519, ECO:0000269|PubMed:25107664}.
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=4.1.1.28;
CC Evidence={ECO:0000269|PubMed:23204519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30340;
CC Evidence={ECO:0000269|PubMed:23204519};
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 Evidence={ECO:0000269|PubMed:23204519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18534;
CC Evidence={ECO:0000269|PubMed:23204519};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23204519};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for L-tryptophan {ECO:0000269|PubMed:23204519};
CC Vmax=2710 nmol/min/mg enzyme with L-tryptophan as substrate
CC {ECO:0000269|PubMed:23204519};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M25151; AAA33109.1; -; mRNA.
DR EMBL; X67662; CAA47898.1; -; Genomic_DNA.
DR EMBL; MG748691; AYA72254.1; -; mRNA.
DR PIR; A32103; DCJAAP.
DR PDB; 6EEW; X-ray; 2.05 A; A/B/C/D=1-500.
DR PDBsum; 6EEW; -.
DR AlphaFoldDB; P17770; -.
DR SMR; P17770; -.
DR MINT; P17770; -.
DR KEGG; ag:CAA47898; -.
DR BioCyc; MetaCyc:MON-11583; -.
DR BRENDA; 4.1.1.105; 1211.
DR BRENDA; 4.1.1.28; 1211.
DR GO; GO:0036467; F:5-hydroxy-L-tryptophan decarboxylase activity; IEA:RHEA.
DR GO; GO:0036469; F:L-tryptophan decarboxylase activity; IEA:RHEA.
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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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..500
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /id="PRO_0000146944"
FT BINDING 102
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:6EEW"
FT BINDING 168
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:6EEW"
FT BINDING 262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:6EEW"
FT BINDING 348
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:6EEW"
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.3"
FT MUTAGEN 348
FT /note="Y->F: Acquires the capacity to produce indole-3-
FT acetaldehyde from tryptophan."
FT /evidence="ECO:0000269|PubMed:23204519"
FT MUTAGEN 370
FT /note="G->S: Acquires the capacity to produce dopamine from
FT L-dopa."
FT /evidence="ECO:0000269|PubMed:25107664"
FT CONFLICT 401
FT /note="G -> A (in Ref. 3; AYA72254)"
FT /evidence="ECO:0000305"
FT HELIX 24..44
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6EEW"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:6EEW"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 270..280
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 335..341
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 375..409
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 438..451
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:6EEW"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:6EEW"
FT HELIX 479..496
FT /evidence="ECO:0007829|PDB:6EEW"
SQ SEQUENCE 500 AA; 56207 MW; 32965957DEC566E7 CRC64;
MGSIDSTNVA MSNSPVGEFK PLEAEEFRKQ AHRMVDFIAD YYKNVETYPV LSEVEPGYLR
KRIPETAPYL PEPLDDIMKD IQKDIIPGMT NWMSPNFYAF FPATVSSAAF LGEMLSTALN
SVGFTWVSSP AATELEMIVM DWLAQILKLP KSFMFSGTGG GVIQNTTSES ILCTIIAARE
RALEKLGPDS IGKLVCYGSD QTHTMFPKTC KLAGIYPNNI RLIPTTVETD FGISPQVLRK
MVEDDVAAGY VPLFLCATLG TTSTTATDPV DSLSEIANEF GIWIHVDAAY AGSACICPEF
RHYLDGIERV DSLSLSPHKW LLAYLDCTCL WVKQPHLLLR ALTTNPEYLK NKQSDLDKVV
DFKNWQIATG RKFRSLKLWL ILRSYGVVNL QSHIRSDVAM GKMFEEWVRS DSRFEIVVPR
NFSLVCFRLK PDVSSLHVEE VNKKLLDMLN STGRVYMTHT IVGGIYMLRL AVGSSLTEEH
HVRRVWDLIQ KLTDDLLKEA
