ID   M8AW96_AEGTA            Unreviewed;       419 AA.
AC   M8AW96;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EnsemblPlants:EMT08722};
OS   Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT08722};
RN   [1] {ECO:0000313|EnsemblPlants:EMT08722}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-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; M8AW96; -.
DR   EnsemblPlants; EMT08722; EMT08722; F775_18331.
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; 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:SF173; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE 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         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   419 AA;  45248 MW;  C09DC03565BA32CD CRC64;
     MGSLDTNPMS SALPNDKAAF EPLNFFAFFP STNSAAAIAG DLIASAMNTV GFTWQASPAA
     TEMEVLALDW LARLLRLPTT FMNRTSTGRG TGGGVILGTT SEAMLVTLVA ARDAALRRTG
     SVGVSDIPRL TVYAADQTHS TFFKACRLAG FDPANIRSIP TGSETSYGFD PAKLLEVMQA
     DADAGLVTTY VCATVGTTSS NAVDPVHVDA AYAGSACICP EFRHHLDGVE RVDSISMSPH
     KWLLTCLDCT CLYVRDAHRL SDSLETNPEY LKNDATDSGE VTDLKDMQVG VGRRFRGLKL
     WMVMRTYGTA KLQEHIRSDV AIAKMFEDFV RADDRFEVVV PRNFALVCFR IKASGAMTEK
     DADEVNRVLM ENLNKTGKAY LAHTVVGDKF VLRFAVVAAR GETCALVGKG AFTPVHKGL
//