ID TYDC3_PETCR Reviewed; 516 AA.
AC Q06087;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Tyrosine decarboxylase 3;
DE EC=4.1.1.25;
GN Name=TYRDC-3;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8420986; DOI=10.1016/s0021-9258(18)53980-6;
RA Kawalleck P., Keller H., Hahlbrock K., Scheel D., Somssich I.E.;
RT "A pathogen-responsive gene of parsley encodes tyrosine decarboxylase.";
RL J. Biol. Chem. 268:2189-2194(1993).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA33862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M96071; AAA33861.1; ALT_INIT; mRNA.
DR EMBL; M96072; AAA33862.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q06087; -.
DR SMR; Q06087; -.
DR BRENDA; 4.1.1.25; 4694.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF96; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..516
FT /note="Tyrosine decarboxylase 3"
FT /id="PRO_0000146997"
FT MOD_RES 319
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 516 AA; 57633 MW; 5EA5BD3B6EAE2D5F CRC64;
MGSIDNLTAQ KLTSSQFPMN TLEPEEFRRQ GHLMIDFLAD YYRKVENYPV RSQVSPGYLR
EILPESAPYN PESLETILQD VQTKIIPGIT HWQSPNFFAY FPSSGSTAGF LGEMLSTGFN
VVGFNWMVSP AATELENVVT DWFGKMLQLP KSFLFSGGGG GVLQGTTCEA ILCTLVAARD
KNLRQHGMDN IGKLVVYCSD QTHSALQKAA KIAGIDPKNF RAIETTKSSN FKLCPKRLES
AILYDLQNGL IPLYLCATVG TTSSTTVDPL PALTEVAKKY DLWVHVDAAY AGSACICPEF
RQYLDGVENA DSFSLNAHKW FLTTLDCCCL WVRDPSALIK SLSTYPEFLK NNASETNKVV
DYKDWQIMLS RRFRALKLWF VLRSYGVGQL REFIRGHVGM AKYFEGLVGL DKRFEVVAPR
LFSMVCFRIK PSAMIGKNDE NEVNEINRKL LESVNDSGRI YVSHTVLGGI YVIRFAIGGT
LTDINHVSAA WKVLQDHADA LLDDAFLPKK IVNILS
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