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Database: UniProt
Entry: A0A059C504_EUCGR
LinkDB: A0A059C504_EUCGR
Original site: A0A059C504_EUCGR 
ID   A0A059C504_EUCGR        Unreviewed;       461 AA.
AC   A0A059C504;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EUGRSUZ_E01787 {ECO:0000313|EMBL:KCW73329.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW73329.1};
RN   [1] {ECO:0000313|EMBL:KCW73329.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW73329.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; KK198757; KCW73329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059C504; -.
DR   STRING; 71139.A0A059C504; -.
DR   EnsemblPlants; KCW73329; KCW73329; EUGRSUZ_E01787.
DR   Gramene; KCW73329; KCW73329; EUGRSUZ_E01787.
DR   InParanoid; A0A059C504; -.
DR   OMA; GMICARY; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   461 AA;  51398 MW;  D3C1A45F01EE6D61 CRC64;
     MVVDFLAKYY ENIEKYPVLS QVEPGYLSKR FPSSAPQDEE PMEAILDDVH QHIFPGLTHW
     QSPNFFAYYQ TNTSTAAILG EMLCAGFNVA GFNWVSSPAA TELESLVMDW LGKMLDLPRP
     FLPFGNGGGV IEGNTSEAIT CTLTAARDRV LRKLGHNSIA KLVVYGSDQT NCSFQKAARV
     VGIDPRNFRA LKTTRSTLFG LSPDSLEKAI CLDINAGLIP LYLCATVGTT SCAAVDPLEP
     LCKVASKFSM WIHVDAAYTG ASCICPEYRK FINGVEFADS FSFNAHKWLL TPLDCCCLWV
     KDPNALVNSL STDPEYLKNE ATESKQVIDY ADWQLSLSRR FRALKLWLVL RSHGVQNLRS
     HIRNHCRLAK LFEELVEEDP QFEVVFPINF ALVCFRIRPS GVAGMSNGHV DNEQGEAWKL
     NEVNRLNAQL LYAINASGRV FMSHTTVGGV YVLRFAVGRR L
//
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