ID   A0A1I1RNI2_9CLOT        Unreviewed;       470 AA.
AC   A0A1I1RNI2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Arginine/lysine/ornithine decarboxylase {ECO:0000313|EMBL:SFD35899.1};
GN   ORFNames=SAMN05421842_13615 {ECO:0000313|EMBL:SFD35899.1};
OS   Clostridium uliginosum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=119641 {ECO:0000313|EMBL:SFD35899.1, ECO:0000313|Proteomes:UP000199263};
RN   [1] {ECO:0000313|EMBL:SFD35899.1, ECO:0000313|Proteomes:UP000199263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12992 {ECO:0000313|EMBL:SFD35899.1,
RC   ECO:0000313|Proteomes:UP000199263};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOMG01000036; SFD35899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1RNI2; -.
DR   STRING; 119641.SAMN05421842_13615; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000199263; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF3; LYSINE 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199263}.
FT   DOMAIN          6..303
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          388..453
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   470 AA;  53471 MW;  14130B1A4C1CF90B CRC64;
     MNTKLPLLNE LLKYHEEKNL ILSMPGNKSG IGFLRDSIGK KFAENLGYID ITEVEPLDNL
     HCPEGVIKEA QELLSKTYNV KKAYFMINGS SGGNLVSIFD AFNEGDEVVV ERNCHKSIYN
     GLILRKLKVT YIEPVIDYEN DLFFPPNKEN IYDAIKKCQN PKGIILTYPN YFGICYDIEE
     IIKDLKQKGL KIIIDAAHGA HFGINDRLPK SVASLGDYVI LSAHKTLPAL TQGSYLLVNN
     ECGNIEFYLK AFMTTSPSYL IMASLDYARY YLDKYGKGDY ELLIAVCEKW REKINKINKV
     HIISKEDLKE DYDIDITRYI MMLPKGFSGH KLLDYLRTKK IQAEMSFSRG VVLILSPFNT
     ERDFNTIYDA IVGLNLSLLK DDNKAKYFSI IPKKVLEPYE TFKLQGKLCF IEESEGKISK
     EMIVPYPPGI PLICAGEVIT KDAINIIKDY IKNERSIIGV VDNKIEVVIP
//