ID   A0A0N0XWZ0_9ACTN        Unreviewed;       461 AA.
AC   A0A0N0XWZ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KPC62816.1};
GN   ORFNames=ADL29_17250 {ECO:0000313|EMBL:KPC62816.1};
OS   Streptomyces chattanoogensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC62816.1, ECO:0000313|Proteomes:UP000037982};
RN   [1] {ECO:0000313|Proteomes:UP000037982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPC62816.1}.
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DR   EMBL; LGKG01000136; KPC62816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0XWZ0; -.
DR   PATRIC; fig|66876.3.peg.3769; -.
DR   Proteomes; UP000037982; 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   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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; 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.
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:UP000037982}.
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   461 AA;  49901 MW;  9E53C256CF6C4599 CRC64;
     MIAHWQALAA REVPVTPQCA PGSLRTALPS AAPEQPESLG EMLADTWKFV VPGLTHWQHP
     AFLGYFPTNN SPASVLAEFV TAGLGVQGMM WSTSPAATEL EQVVTDWLAQ ALGLPEAFRH
     SSGRGGGVIQ DSASSAVLVA TAAALHRASQ GRWRAAGTEG RYRMYCTERA HSSVFKGCRI
     AGLGEPQLIA TLPGTGRMDP DALGARIDSD RKDGFVPALV VATVGTTDTC AVDPVPDIGR
     RCRQEDVWLH VDAAYAGSAA LCPEYRHLHD GIDLADSYAV NAHKWMRTGT PCDVLWTSDS
     AALTDAMSIA PAYLRNAATD SGRVVDFRDW QVPLGRPMRA LKLWYVMRAH GVQGLREAIR
     HDIGLADRLA RLITAEPGFH LEVHELGLVI FRRDTDEDTR DLISRLQTDP TLLCTPATVG
     GRPAVRAAFG SPYADADTVR YVWERIRTHA QDPEQLSACG V
//