ID   A0A1I6W6S0_9BACI        Unreviewed;       469 AA.
AC   A0A1I6W6S0;
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:SFT21642.1};
GN   ORFNames=SAMN04488145_12254 {ECO:0000313|EMBL:SFT21642.1};
OS   Bacillus sp. 103mf.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761751 {ECO:0000313|EMBL:SFT21642.1, ECO:0000313|Proteomes:UP000198993};
RN   [1] {ECO:0000313|EMBL:SFT21642.1, ECO:0000313|Proteomes:UP000198993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103MF {ECO:0000313|EMBL:SFT21642.1,
RC   ECO:0000313|Proteomes:UP000198993};
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; FPAF01000022; SFT21642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6W6S0; -.
DR   STRING; 1761751.SAMN04488145_12254; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000198993; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 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}.
FT   DOMAIN          7..307
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          367..457
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   469 AA;  52552 MW;  B9BE564035C82EF1 CRC64;
     MDQRKMPLYE ALKTFASKKP ISFHVPGHKN GTNFPHEVQK YFHDILSIDV TELTGLDDLH
     GPFECIEEAQ CLLAELYAVQ KSHFLINGST VGNLAMLLAC CNEHDTVLVQ RNAHKSIING
     LKLTGARPVF LKPWIDEKSG VPVGVPYETI EDAILQYPQT KALILTHPNY YGVGVDLEKS
     IALAHKNGIP VLVDEAHGAH FCIGEPFPTS ALAYGADIVV HSAHKTLPAM TMGSYLHVNS
     SLVDEEKVSF YLNMLQSSSP SYPIMASLDI ARFVLAKIRE EGGKEIAAFT QRFRETLNRI
     PQLAVLDYPI QDALKVTVQT RCKLSGYELQ RLFEEIGIYV EMADPYNVLL ILPLQVNEDY
     IQVIDKIQDV LCSYDVEDSK PHINYPYKDN LSSLSFTYKQ LEKYKKKVVP LREALGMIAA
     DMIIPYPPGI PLVMYGEEIT LEHINQISGL EETGARFQGN IKNITVYDI
//