ID   A0A344L793_9PSEU        Unreviewed;       475 AA.
AC   A0A344L793;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:AXB43917.1};
GN   ORFNames=A4R43_16450 {ECO:0000313|EMBL:AXB43917.1};
OS   Amycolatopsis albispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB43917.1, ECO:0000313|Proteomes:UP000250434};
RN   [1] {ECO:0000313|EMBL:AXB43917.1, ECO:0000313|Proteomes:UP000250434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:AXB43917.1,
RC   ECO:0000313|Proteomes:UP000250434};
RA   Wang H., Chen S., Wu Q.;
RT   "Complete genome sequence and analysis of deep-sea sediment isolate,
RT   Amycolatopsis sp. WP1.";
RL   Submitted (APR-2016) 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; CP015163; AXB43917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344L793; -.
DR   KEGG; aab:A4R43_16450; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000250434; Chromosome.
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;  50784 MW;  5CFF8ECBD5A6C296 CRC64;
     MSDPLTEREA TAEALRLVAD AAGPYLATLS DRLVQDPAGA PLLDELDGPL PERGDGTLPS
     VRELLRIGTG AATHSSGPRF FHFVVGGSTP AAQAGDWVTS LLDQVAGLWP ASPFAARVET
     VVLGWLKDLF GLPASYGGVL TPSATLANLT GLAAARHWWA ERHGVDVSAD GMLGLPRLPV
     LSSGYVHPSS RKALQILGCG RDTVRVFARD DAGRVDLGAM ETELAAVAGP AVLIANAGEV
     NAGDFDPVGE LADLAEAYGA WLHVDGAFGL FAAVSPKTAH LVHGVERADS VAADGHKWLN
     VPYESGFAFL REPRRLVQAF AMPDAAYLPV GDEARINYNS LGPESSRRAR ALPIWATLRA
     YGREGYRAMV ERHHDLARLL GELVDEAPDL EPLAPPGLNV VCFRYRRDGL GDERLDELNR
     RLGAELLEDG RVYAGTTVYR GRLALRPAIV NWRTGEADIE LLVSVVREIG ARLTA
//