ID   A0A117IXJ4_9ACTN        Unreviewed;       493 AA.
AC   A0A117IXJ4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KUH40625.1};
GN   ORFNames=ATE80_01660 {ECO:0000313|EMBL:KUH40625.1};
OS   Streptomyces kanasensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH40625.1, ECO:0000313|Proteomes:UP000054011};
RN   [1] {ECO:0000313|EMBL:KUH40625.1, ECO:0000313|Proteomes:UP000054011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX01 {ECO:0000313|EMBL:KUH40625.1,
RC   ECO:0000313|Proteomes:UP000054011};
RA   Zhang G., Han L., Feng J., Zhang X.;
RT   "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT   kanasensis ZX01.";
RL   Submitted (NOV-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|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:KUH40625.1}.
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DR   EMBL; LNSV01000002; KUH40625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117IXJ4; -.
DR   STRING; 936756.ATE80_01660; -.
DR   OrthoDB; 3335676at2; -.
DR   Proteomes; UP000054011; Unassembled WGS sequence.
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:UP000054011}.
FT   MOD_RES         297
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   493 AA;  50045 MW;  6058A4F939FA663D CRC64;
     MPRAGEVDLA VAGGADGAYA LGKLTSVVLD ALADGATARG GPLPDGGPTA VAERLRAACA
     PVLPERGTGA EEALRTVVRA VAEGAADPAH PWCAAHLHCP PLAVAAAADL AAAALNPSMD
     SWDQAPAAAV LEQDVTAALA DLVYPGRAAA DALVTSGGTE SNLVALLLAR ERARAAGAAT
     VRVVCGANAH HSVRRAAWLL DLPEPVTVAA PGGRLDPDAV DRALARTTGP ALVVATAGTT
     DEGLVDPLPE LGSVAARHGA ELHVDAAYGG PLLFSERLAP RLDGLTAATS VTFDLHKLGW
     QPVAAGVLAV ADGAALAPLA LRADYLNADD DGEAGLPDLL GRSIRTTRRP DVLKVAATLR
     ALGRDGLGAL VEHCVDAAHA FAALVDAHPR LRRRPGDIGI STVLFRPTAA DAAAPADGDA
     LVAEVRRRLL TEGRAVVGRA VAEDADGTRR LWLKATLLHP RAAGEDLAGL LDLVAATAAR
     TSTTHPQEPE GPR
//