ID A0A1G6VZ19_9PSEU Unreviewed; 467 AA.
AC A0A1G6VZ19;
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:SDD58693.1};
DE SubName: Full=Glutamate/tyrosine decarboxylase-like PLP-dependent enzyme {ECO:0000313|EMBL:PWV73908.1};
GN ORFNames=DES30_10881 {ECO:0000313|EMBL:PWV73908.1}, SAMN05421630_11081
GN {ECO:0000313|EMBL:SDD58693.1};
OS Prauserella marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=530584 {ECO:0000313|EMBL:SDD58693.1, ECO:0000313|Proteomes:UP000199494};
RN [1] {ECO:0000313|EMBL:SDD58693.1, ECO:0000313|Proteomes:UP000199494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDD58693.1,
RC ECO:0000313|Proteomes:UP000199494};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWV73908.1, ECO:0000313|Proteomes:UP000246674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV73908.1,
RC ECO:0000313|Proteomes:UP000246674};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; QGTN01000008; PWV73908.1; -; Genomic_DNA.
DR EMBL; FMZE01000010; SDD58693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6VZ19; -.
DR STRING; 530584.SAMN05421630_11081; -.
DR Proteomes; UP000199494; Unassembled WGS sequence.
DR Proteomes; UP000246674; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199494}.
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 467 AA; 48285 MW; C591B9AAC4F1651C CRC64;
MSEMVETAEL LRTAANEITR YLASLPERPV AAPVEPEALR AGFGSALPAG PSPPHTVLAA
LCAAAEPGLV ATAGPRYFGF VTGGSLPSAT AADLLAVGWD QNAFNRVLSP AADAAEHCAG
RWLKELLGIP ATASTGFVTG GQAANTVGLA AARHRVLADA GWDVESRGLA GAPPVRIVAS
EERHATIDRA LRLLGFGTSA VTEVRADPTG AIDLDDLARV LDQGSGPLIG CLQAGNVNTG
ACDDLRAATD LLHQHGGWAH VDGAFGLWAS ANPDTATLVD GVELADSWAC DGHKWLNVPY
DSGFAFCADP EAHAAAVSYT AAYLVGSGGE AALADFTLES SRRARGFAVW AALRELGRSG
VAELVGRTCA LTRRFASALA EGGAEIGNDI VLNQALVRFS SDEHTDRVIA EVQREGTCWL
GGTTWRGRRY IRVSVSNWST KESDVDRSAE AVLRAAASVG AVAGSAG
//
