ID   A0A3G2JBQ8_9ACTN        Unreviewed;       518 AA.
AC   A0A3G2JBQ8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:AYN39041.1};
GN   ORFNames=D9753_09075 {ECO:0000313|EMBL:AYN39041.1};
OS   Streptomyces dangxiongensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1442032 {ECO:0000313|EMBL:AYN39041.1, ECO:0000313|Proteomes:UP000268329};
RN   [1] {ECO:0000313|EMBL:AYN39041.1, ECO:0000313|Proteomes:UP000268329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z022 {ECO:0000313|EMBL:AYN39041.1,
RC   ECO:0000313|Proteomes:UP000268329};
RA   Zhang B.;
RT   "The genome of Streptomyces dangxiongensis Z022.";
RL   Submitted (OCT-2018) 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; CP033073; AYN39041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G2JBQ8; -.
DR   KEGG; sdd:D9753_09075; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000268329; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000268329}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   518 AA;  54679 MW;  A35DEE31D681310C CRC64;
     MRSVNHSTPA TTGTGHRVAL AGTPDGLEQL GTLVTAALDA VSAAAAERTG PLPAGGPDAA
     IAAVRDLVRD GGFLTDAPGP HRVEELFEAY AGWAADLTHP AAVSRMQCAP TPAAAAAELL
     AAVLNQSLHS WESGPFALEL ERRLIAEMAD WVGYGETASG TLTPGGSISN LMGLLLSRDH
     VLGGLTGDDI SHTGLAGRAI RPRILCSTAA HFSVARAAGF LGLGRDAVVR VPADERGRMI
     PEEARRLLDG FAPDEVPIAL VATAGTTDHG SFDPLPELAA LAAERRIWFH VDAAYGIGAL
     FSDTLRPLFD GLAEADSIAF DLHKFGWTPA SSSILLVRDR ARMSPLGQQA VYLNPPDDEA
     EGYTALLGTS LQTTRRADAF KIAASLLALG REGMGEWVDA CHSQARYAAA RITRDPDLEL
     LAEPILSTVV FRCRAGAAIE DESTWNAAVR RHLMAEGKAL LARTKVRRQD GQAQVHLKLV
     FLNPATTTQD IDALLDDVVA AAAEVRQSPK ARTPQTAH
//