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Database: UniProt
Entry: A0A1V2RCY8_9ACTN
LinkDB: A0A1V2RCY8_9ACTN
Original site: A0A1V2RCY8_9ACTN 
ID   A0A1V2RCY8_9ACTN        Unreviewed;       488 AA.
AC   A0A1V2RCY8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:ONK10232.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:ONK10232.1};
GN   ORFNames=STBA_09540 {ECO:0000313|EMBL:ONK10232.1};
OS   Streptomyces sp. MP131-18.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1857892 {ECO:0000313|EMBL:ONK10232.1, ECO:0000313|Proteomes:UP000189065};
RN   [1] {ECO:0000313|EMBL:ONK10232.1, ECO:0000313|Proteomes:UP000189065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP131-18 {ECO:0000313|EMBL:ONK10232.1,
RC   ECO:0000313|Proteomes:UP000189065};
RA   Paulus C., Rebets Y., Tokovenko B., Nadmid S., Terekhova L.P.,
RA   Myronovskyi M., Zotchev S.B., Rueckert C., Kalinowski J., Luzhetskyy A.;
RT   "New natural products identified by combined genomics-metabolomics
RT   profiling of marine Streptomyces sp. MP131-18.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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:ONK10232.1}.
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DR   EMBL; LZNS01000001; ONK10232.1; -; Genomic_DNA.
DR   RefSeq; WP_077058016.1; NZ_LZNS01000001.1.
DR   AlphaFoldDB; A0A1V2RCY8; -.
DR   STRING; 1857892.STBA_09540; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000189065; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ONK10232.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189065}.
FT   DOMAIN          7..301
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          410..472
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   488 AA;  51818 MW;  5A9EE06BA4C58DD2 CRC64;
     MDHARAPVLE ALAAYHDGGQ LPFTPPGHKQ GRGADPRVRA VLGDAVFRSD VLAIAGLDDR
     TSSHGVLDEA QRLMADAVSA EHTFFSTCGS SLSVKAAMLS VAGPHEKLVI GRDAHKSVVS
     GLILSGVRPI WVDPQWDPDL HLAHPPAPEA FEAAFAAHPD ARGALVTSPT PYGTCTDLAA
     VAAVCHARGR PLIVDEAWGA HLPFHPGLPT WAMDAGADVC VTSVHKMGSG LEQGSVFHLG
     GDLIAPAILK ARADLLGTTS PSVLLYAALD GWRRQMVQHG RALYDDALDR AARVRRRIED
     IDGLHVHGRA DFCAPGRAAD LDPLQVIIDV GGLGTSGYRA ADWLREHHRI NLHVSDHRRA
     SVQLTHADDE ASAAALLAAL RDLAAHAGTL RPAPRVDVPD PAHLRLDQVM LPRDAFFGRA
     EQVPSDKAAG RVTAEMLTPY PPGIPAALPG ERLTDDVLRY LRTGVEAGMV VPDAADATVR
     GIRVVAED
//
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