ID A0A0E0LR37_ORYPU Unreviewed; 523 AA.
AC A0A0E0LR37;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC08G02340.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC08G02340.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC08G02340.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0LR37; -.
DR STRING; 4537.A0A0E0LR37; -.
DR EnsemblPlants; OPUNC08G02340.1; OPUNC08G02340.1; OPUNC08G02340.
DR Gramene; OPUNC08G02340.1; OPUNC08G02340.1; OPUNC08G02340.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_1_1; -.
DR OMA; MKREDSC; -.
DR Proteomes; UP000026962; Chromosome 8.
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:SF170; OS08G0140500 PROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 523 AA; 56448 MW; DEE376983D16DAC2 CRC64;
MGSLDTNPAA YAAFAADVEG FQPLNADDVR SYLHKAVDFV YDYYKSVESL PVLPGVEPGY
LLRLLQSAPP SSSAPFDIAM KELREAVVPG MTHWASPNFF AFFPATNSAA AIAGELIASA
MNTVGFTWQA APAATELEVL ALDWLAQLLR LPPGFMNRTV AGGRGTGGGV ILGTTSEAML
VTLVAARDAA LRRSGSNGVA GITRLTVYAA DQTHSTFFKA CRLAGFDPAN IRSIPTGAET
DYGLDPAKLL ELMQADADAG LVPTYVCATV GTTSSNAVDP VGAVADVAAR FNAWVHVDAA
YAGSACICPE FRHHLDGVER VDSISMSPHK WLMTCLDCTC LYVRDTHRLT GSLETNPEYL
KNHASDSGEV TDLKDMQVGV GRRFRGLKLW MVMRTYGAGK LQEHIRSDVA MAKTFEDLVR
SDDRFEVVVP RNFALVCFRI RPRKSGTTTI AGGEAEAEKA NRELMERLNK TGKAYVAHTV
VGGRFVLRFA VGSSLQEERH VRSAWELIKK TTAEIVAVAG EDK
//