ID   F8JJH7_STREN            Unreviewed;       510 AA.
AC   F8JJH7; G8XGD9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:AEW98696.1};
GN   OrderedLocusNames=SCATT_p05030 {ECO:0000313|EMBL:AEW98696.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OG   Plasmid pSCATT {ECO:0000313|EMBL:AEW98696.1,
OG   ECO:0000313|Proteomes:UP000007842}.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW98696.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RC   PLASMID=Plasmid pSCATT {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) 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; CP003229; AEW98696.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8JJH7; -.
DR   KEGG; scy:SCATT_p05030; -.
DR   PATRIC; fig|1003195.11.peg.1183; -.
DR   HOGENOM; CLU_011856_0_4_11; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
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   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 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   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Plasmid {ECO:0000313|EMBL:AEW98696.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   510 AA;  55574 MW;  1AF71CDB528927DC CRC64;
     MISQADLIES APDGAATAAD SRSHLLGDQT AERYRRSLTE GVTRLAERFA TTGRPFTGIS
     PEALTPEVAA IDLDRPLGDT TAALDELEDV YLRDAVYFHH PRYLAHLNCP VVIPAVLGEA
     VLSAVNSSLD TWDQSAGGTL IERRLIDWTA ERIGLGPHAD GVFTSGGTQS NLHALLLARE
     EAGAEPGRLR ILASACGHFS VRKSAKLLGL GEDSVIEVEC DADRRMRPDA LARELRRCAE
     RDLVPMAVVA TAGTTDFGSI DPLPRIADLC ARYGAWFHVD AAYGCGLLVS RTRRHLLDGV
     ERADSVTVDF HKSFFQPVSS SAVLVRDRAT LRHATYHADY LNPARMAKRR IPNQVDKSLQ
     TTRRFDALKL WLTLRVMGAD AIGDLFDEVV GRAADAWRLL AADPRYEVVT RPQLSTLVFR
     YLPSGDHDDA TVDRANLHAR DALFASGEAI VAGTVVDGRH HLKFTLLNPH TTLHDIATVL
     DLIAGHAEAH LAEQSATTRH HGELTGSLAR
//