ID   A0A1G8BRC2_9RHOO        Unreviewed;       495 AA.
AC   A0A1G8BRC2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SDH35742.1};
GN   ORFNames=SAMN05660652_01576 {ECO:0000313|EMBL:SDH35742.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDH35742.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDH35742.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDH35742.1,
RC   ECO:0000313|Proteomes:UP000198607};
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; FNCY01000005; SDH35742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8BRC2; -.
DR   STRING; 83767.SAMN05660652_01576; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000198607; 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; 3.90.1150.170; -; 1.
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: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:UP000198607}.
FT   MOD_RES         309
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   495 AA;  52944 MW;  582A3B5BEF2A582E CRC64;
     MQEQGKRSAQ FSPSPLDPAD WQTFRADAHR LLDACIDQLS SARQHPWQPV GEADKAALAL
     GEALEGEESG ALVDELVRKV LPFHTGNTHP RFFGWVHGTG LAAGLLAEMV AATMNSNCGG
     RDHGAVYVER EVIDWCRRCF GFPESASGVL VGGTSQATVI ALAAARTRAL GAASRRDGIQ
     GAQRLAAYAL QGVHNATVKS LELLGVGAAA LRTIPAGVDG GMSLERLAEA VAKDRADGML
     PFCIVATAGS VDLGVFDDID AIADFCAREG IWLHVDGAFG AWSRLADSPW RDLSRGIERA
     DSLAFDFHKW MYVQYDCGVV LIRDEAAHRQ AFAARPAYLA KQDQGLGGGE PWYCDYGVDL
     SRGFRALKVW AALRNYGSKA LGASITDNCR LAERMGVLVG ATPGLRLAAP VRLNVCCFSA
     APSDWEGAAQ DRLNERITHV LQLAGDVVFS TTRVEGRTVI RAAITNHRTC AADIDEAISA
     VMRVRCGEIA NAGTQ
//