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Database: UniProt
Entry: A0A0D3HDD8_9ORYZ
LinkDB: A0A0D3HDD8_9ORYZ
Original site: A0A0D3HDD8_9ORYZ 
ID   A0A0D3HDD8_9ORYZ        Unreviewed;       428 AA.
AC   A0A0D3HDD8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART10G09130.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART10G09130.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART10G09130.1};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART10G09130.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D3HDD8; -.
DR   STRING; 65489.A0A0D3HDD8; -.
DR   PaxDb; 65489-OBART10G09130-1; -.
DR   EnsemblPlants; OBART10G09130.1; OBART10G09130.1; OBART10G09130.
DR   Gramene; OBART10G09130.1; OBART10G09130.1; OBART10G09130.
DR   eggNOG; KOG0628; Eukaryota.
DR   HOGENOM; CLU_011856_3_1_1; -.
DR   Proteomes; UP000026960; Chromosome 10.
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   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999:SF148; OS10G0400500 PROTEIN; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   428 AA;  46408 MW;  FCE5C92B6AA38AC2 CRC64;
     MGSLPLDALQ PLDPDTFAAD SSAVVDFLAG YYRDVDKYPV RAADLEPGRL RRLLPEAAPE
     FGEPAERILA DVRRDVLPGL THWQSPSFFA YFPMNASAAG FAGEMLSVGL NVVPFMWVAS
     PAAVELEATH ATFQKGARLV GISPANFRVV PTAAASGYAL TGAAVRAAVE GDVARGLVPL
     YLCATVGTTG IGAVDPVREL GEVARRHGMW LHVDAAYAGS AAICPEYQGY LDGAELADSV
     SMNPHKWFLT NMDCCCLWVA SPAALTAALS TDPEYLKNAG GGKPQAAAGA GAIDYKDWQI
     SLSRRFRAMK LWFVLRRYGA AGMRAHIRRH VAMAEWFERA VSADERFEVV AKRRFSLVCF
     RLRGGGDAMN RELLAAVNAS GRVFMTHFVV EGKFVIRLAV GGAMTEMRHV GDAWELVQRT
     AEQLLQRR
//
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