ID   A0A1G9T8P7_9FIRM        Unreviewed;       474 AA.
AC   A0A1G9T8P7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SDM44027.1};
GN   ORFNames=SAMN04515677_11211 {ECO:0000313|EMBL:SDM44027.1};
OS   Romboutsia lituseburensis DSM 797.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Romboutsia.
OX   NCBI_TaxID=1121325 {ECO:0000313|EMBL:SDM44027.1, ECO:0000313|Proteomes:UP000199068};
RN   [1] {ECO:0000313|EMBL:SDM44027.1, ECO:0000313|Proteomes:UP000199068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 797 {ECO:0000313|EMBL:SDM44027.1,
RC   ECO:0000313|Proteomes:UP000199068};
RA   de Groot N.N.;
RL   Submitted (OCT-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|RuleBase:RU000382}.
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DR   EMBL; FNGW01000012; SDM44027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9T8P7; -.
DR   STRING; 1121325.SAMN04515677_11211; -.
DR   Proteomes; UP000199068; Unassembled WGS sequence.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 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; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000199068}.
FT   MOD_RES         288
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   474 AA;  53506 MW;  AF8E32F89EF2670E CRC64;
     MNNTQIKEYL NYFIEQYFQE IENLPSSDIL KIADSSQLEK IKNINIPNEG RKIQEVINEM
     IEDVYDYRGK VDHPRFFGFV PGPADITSWI GDVMTSAYNL HTASWMISSG ASCIEKKLIE
     WLSKKVGYDT TKSVGLFVSG GSMANITALV TARDNKLSPE TFHLGVAYVS DQTHSSIKKA
     LKIAGISPQN IRKISSDLNY KMNISELERT IQEDILKGLK PFVIIASAGT TNTGSIDPMY
     KISNVCSKYK LWMHVDGAYG ASILLSQNYN NLLNGIENAD SLSWDAHKWL FQTYACGVVI
     VKDKNNSVNS FSENPEYLRD LDVDNGLINY GNIGMELTRP ARYLKLWTTL QTLGTDEISR
     RIEYGINITE YVEELLEGLD NWEIISKPSL AIINFRYAPC GISQKQIEDI NNNISKLMLQ
     SNYAGIFTTV LNNKVVLRMC CINHETTKED IKNTIAKLDE FAKKLLEDMV TLVI
//