ID   A0A0F7NDG7_9ACTN        Unreviewed;       462 AA.
AC   A0A0F7NDG7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AA958_04320 {ECO:0000313|EMBL:AKH86540.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH86540.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH86540.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH86540.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT   of Meroterpenoid Chemistry.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP011492; AKH86540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7NDG7; -.
DR   STRING; 444103.AA958_04320; -.
DR   KEGG; strc:AA958_04320; -.
DR   PATRIC; fig|444103.5.peg.907; -.
DR   Proteomes; UP000034283; 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; 3.90.1150.170; -; 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; 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; 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.
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:UP000034283}.
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   462 AA;  48785 MW;  22B24B0810482D32 CRC64;
     MEAVELVAHH AEAVAEGPVA PAEPDSGRIR DWLAGHDFSG PRPAGEVLAE VTAALRRWGV
     HATHPRYLGL FVPTPTWWGV AGELVAAGVN PQLAAYEHAP AAVEIERHVL RFLAGRLGLP
     SAADGSFTTG GAEANLTAVV VALTRHFPAY PNAGLTALRG QPVLYASAES HLAWLKIAQM
     TGLGRRAVRL VPVDSAGRMD IARLRMLYDG DVAAGRTPFL LVGTAGTTGG GAVDPLPELA
     RLAAAWGLHF HVDAAWAGAA ALSDRLRPLL AGVERADSVT VDAHKWLSAP MGAGLFLTAH
     PGALAESFRV STGYMPPDSD TAPDPYRTGV QWSRRFAGLK VFLALAAAGR GAFARQVERD
     TELGNLLARR LAEDGWPRIN DSPLPVVCVA DPGAEAHGPD RSDAWHAAVV AHVVRGGRAW
     ISRVRLDGRP AIRLCVTSHR TRAHDIETAV AALGEARAAT PY
//