ID   A0A238XZ52_9ACTN        Unreviewed;       475 AA.
AC   A0A238XZ52;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SNR64326.1};
GN   ORFNames=SAMN06265355_105119 {ECO:0000313|EMBL:SNR64326.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNR64326.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNR64326.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNR64326.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNP01000005; SNR64326.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238XZ52; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000198420; Unassembled WGS sequence.
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   PANTHER; PTHR11999:SF70; 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.
PE   3: Inferred from homology;
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         297
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   475 AA;  50322 MW;  6A0010A62DF72113 CRC64;
     MSDPLDERDV AGAPLAVVAR AAEPYLASLP DRPVHDRAQD PLLDELDGPL PDTGDGAVAA
     VERLVRIGTG AATHSSGPRF FHFVVGGSTP AAMAGDWAAS LLDQAAGLWL TSPLAARAET
     VVLRWLKELF GLPAGFGGVL TPSATLAHVA GLAAARHWWA AGHGVDVASQ GLAGLPAMPV
     FTSGLVHVST RKALQILGCG RDTLRTFARD DAGRVDLEAM DAALAGAGGP AVIVANLGEV
     NTGDSDPIAE LADLAERHGA WLHVDGAFGL FAALSPRTAR LARGVERADS VTADGHKWLN
     VPYESGFAFV RDPASLSRAF GAWGAAYLPD ADEERVNYNM LGPESSRRAR ALPIWATLRA
     YGRDGYREMV ERHLDVAAHL GGLVEAAPDL ELLAPVRLCI ACFRYRPAGV AEEDLNELNA
     RLGEALLADG RVYAGTSTYR GMTVFRPAPL NWRTTKPDVE RLVDVLRELG ARLTR
//