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Database: UniProt
Entry: A0A069K594_9ACTN
LinkDB: A0A069K594_9ACTN
Original site: A0A069K594_9ACTN 
ID   A0A069K594_9ACTN        Unreviewed;       493 AA.
AC   A0A069K594;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Ornithine decarboxylase {ECO:0000313|EMBL:KDQ71375.1};
GN   ORFNames=DT87_30515 {ECO:0000313|EMBL:KDQ71375.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ71375.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ71375.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ71375.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) 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:KDQ71375.1}.
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DR   EMBL; JJOB01000001; KDQ71375.1; -; Genomic_DNA.
DR   RefSeq; WP_037881808.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069K594; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000027475; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          9..304
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          420..474
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   493 AA;  52831 MW;  8EC56E4A2C05050F CRC64;
     MRMDHTQAPV LEALAAYQER KQLGFSPPGH KHARGAAPEV RAVLGDAVFF GDVLASGGLD
     DRRTGSGVLQ RAEELMADAV HAEHTFFSTC GSSLSVKAAM LSVAWHGEKL LIGRDAHKSV
     VAGLVLSGIE PVWIDPQWDA GRHLAHAPSA EAYEQAFLEH PDARGALVTS PTPYGSAADL
     AAIAEVCHRR GRPLVVDEAW GAHLPFHPEL PSWAMDAGAD VCVTSIHKMG SGLEQGSVFH
     LRGDLVDHDT LASRADLLGT TSPSVLLYAG IDGWRRQMAL NGRALLAGAL DLAARVRREI
     EGVDGMRVND RADFCGPGAG TEFDPLPVVI DVSGLGTSGY RAADWLREHH HIDMHLVDHR
     RISAQLTHAD DAETAGRLLT GLRDLARTAH TLGPAPDMVL PSPTELRQPQ VCLPRDAYFS
     ATEDIPVEEA VGRVAAEMMT PYPPGIPAVV PGERLTEPVL RYLRTGIEAG MNVPDPADPL
     LRTVRVRADG EGP
//
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