ID A0A059C6J0_EUCGR Unreviewed; 462 AA.
AC A0A059C6J0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EUGRSUZ_E02458 {ECO:0000313|EMBL:KCW73864.1};
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:KCW73864.1};
RN [1] {ECO:0000313|EMBL:KCW73864.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW73864.1};
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; KCW73864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059C6J0; -.
DR EnsemblPlants; KCW73864; KCW73864; EUGRSUZ_E02458.
DR Gramene; KCW73864; KCW73864; EUGRSUZ_E02458.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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 322
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 462 AA; 51946 MW; 68E7DEFFB37E7DAD CRC64;
MGSLPKDCEH LLKNMVGDEI AMNPLDLGEF RRQEQMVVDF LVNYYKNVEK YPVLSQVEPG
YLSKCLPSSA PEDEEPLEAI LDDVHRYIVP GLTHWQSPTF FAYFQTNTST AAILGEMLCA
GFSVAGFNWV SSPAATELES LVMDWLGKML DLPRPFLFSG NGGGVIEGNT TEAMICTLIA
ARERVLRRSG HDSITKLVVY GSDQTHCSFQ KAARVVGIDP RNIRALKTTQ STLFGLSPDL
LRKAIRLDID GGLIPLYLCT TVGTTSVTAV DPLEPLCKVA SEFGMWVHVD AAYAGSSCIC
PEYRKFLNGV EFADSFCFNA HKWLLTSLDC CCLWVKDPNA LVKSLSTDPE YLKNEATESK
QVVDYKDWQL SLSRRFRALK LWLVLRIYGV RNLRSHIRND CRLAKLFEEL VVKDGRFEVV
FPRNFALVCF RIRPSAVTGM ANGQAMEDEN REAWKLNEGQ FW
//