ID   A0A0H4PFL8_9BACI        Unreviewed;       489 AA.
AC   A0A0H4PFL8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:AKP46702.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:AKP46702.1};
GN   ORFNames=BSM4216_1421 {ECO:0000313|EMBL:AKP46702.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP46702.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP46702.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP46702.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-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   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP012024; AKP46702.1; -; Genomic_DNA.
DR   RefSeq; WP_048623067.1; NZ_CP012024.1.
DR   AlphaFoldDB; A0A0H4PFL8; -.
DR   STRING; 1479.BSM4216_1421; -.
DR   KEGG; bsm:BSM4216_1421; -.
DR   eggNOG; COG1982; Bacteria.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000036353; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd00615; Orn_deC_like; 1.
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.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:AKP46702.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          221..235
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   489 AA;  53664 MW;  9F7CEF7F4061D325 CRC64;
     MSQFDTPLFT SLVQHAKKNP VQFHIPGHKK GAGMDPKFRE FIGENALSID LINIAPLDDL
     HNPKGVIHQA QKLAAEAFGA DYSFFSVQGT SGAIMAMVMS VCGPGDKIII PRNVHKSIMS
     AIIFSGAVPI FIHPEIDGRL GISHGITADA VEKALKQHPD AKGVLVINPT YFGVSGDLKK
     IVEIAHSYNV PVLVDEAHGA HIHFHDDLPI SAMQAGADLA ATSVHKLGGS LTQSSILNIR
     EGLVSVNKVQ SIMSMLTTTS TSYLLLASLD VARKRLATEG KELLDRTIAL AENIRKQINE
     IPYLYCVGEE ILDSEAVFDY DPTKLTISVK DLGITGHDAE KWLREVYQIE VELSDLYNIL
     CIITPGDTEK EGTILVNALK HLSETFQHDA EEKHIEVLLP DIPHLALTPR DAFYAETEII
     PFEKSAGRII AEFVMVYPPG IPIFIPGEII TEENLAYIRK NMEAGLPVQG PEDPELKTLR
     VIKEFEAIR
//