ID   A0A1R3XMS1_9MICO        Unreviewed;       460 AA.
AC   A0A1R3XMS1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SIT93152.1};
GN   ORFNames=SAMN05880579_2941 {ECO:0000313|EMBL:SIT93152.1};
OS   Microbacterium sp. RU1D.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1907411 {ECO:0000313|EMBL:SIT93152.1, ECO:0000313|Proteomes:UP000187105};
RN   [1] {ECO:0000313|EMBL:SIT93152.1, ECO:0000313|Proteomes:UP000187105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1D {ECO:0000313|EMBL:SIT93152.1,
RC   ECO:0000313|Proteomes:UP000187105};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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|RuleBase:RU000382}.
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DR   EMBL; FTPQ01000003; SIT93152.1; -; Genomic_DNA.
DR   RefSeq; WP_076677287.1; NZ_FTPQ01000003.1.
DR   AlphaFoldDB; A0A1R3XMS1; -.
DR   Proteomes; UP000187105; 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:0019752; P:carboxylic 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; 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   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}.
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   460 AA;  49477 MW;  445617D006DFA009 CRC64;
     MTHSPAARMH EVSDETRAIV DMVLEYSRGR LTSEDTPLDK PLPAAELRRL AGRTIDEKGI
     GARKALGVFE HVLAPACITT DDPRYLSFIP SAPTKAAAAF DLVVSASALY GGSWLEGAGA
     VHAENEVLRW LAAEFGLPEG AGGVFVQGGT LGNLSALVAA REAARDRLAD AGTPRPDAWR
     VVCSVEAHSS IASAARVMDV EVVGVPVGED GVLRGDAVRA ALEEHGHSVF AVVATAGSTN
     FGIVDDIADI ARAVAGSGVW LHVDGAYGLT GMLSPRTRPL FAGVEHADSL VVDPHKWLFA
     PFDACALIYR DPELGRRAHT QHAEYLDTLT ETSDWSPSDF AAHLTRRARG LPLWFSLATY
     GAAVYREAIT SAIDLAQRIA EDIERRPELT LVRRPQLGVV VFERVGWSKA DYDRWSSHLL
     DAQHAFVTPS SHAGRVNARF AILNPRTTFD DLVGILDTMI
//