ID   SPEA_BACCR              Reviewed;         460 AA.
AC   Q819L4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Arginine decarboxylase;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=BC_3962;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Catalyzes the formation of agmatine from arginine.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000305}.
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; AE016877; AAP10882.1; -; Genomic_DNA.
DR   RefSeq; NP_833681.1; NC_004722.1.
DR   AlphaFoldDB; Q819L4; -.
DR   SMR; Q819L4; -.
DR   STRING; 226900.BC_3962; -.
DR   KEGG; bce:BC3962; -.
DR   PATRIC; fig|226900.8.peg.4086; -.
DR   HOGENOM; CLU_025925_2_1_9; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Putrescine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Spermidine biosynthesis.
FT   CHAIN           1..460
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000201145"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  50324 MW;  92EB8987F823C839 CRC64;
     MSQYETPLFT ALVEHSKRNP IQFHIPGHKK GQGMDPTFRE FIGHNALAID LINIAPLDDL
     HHPKGMIKEA QDLAAAAFGA DHTFFSIQGT SGAIMTMVMS VCGPGDKILV PRNVHKSVMS
     AIIFSGAKPI FMHPEIDPKL GISHGITIQS VKKALEEHSD AKGLLVINPT YFGFAADLEQ
     IVQLAHSYDI PVLVDEAHGV HIHFHDELPM SAMQAGADMA ATSVHKLGGS LTQSSILNVK
     EGLVNVKHVQ SIISMLTTTS TSYILLASLD VARKRLATEG TALIEQTIQL AEHVRDAINS
     IEHLYCPGKE MLGTDATFNY DPTKIIVSVK DLGITGHQAE VWLREQYNIE VELSDLYNIL
     CLITLGDTES DTNTLIAALQ DLAATFRNRA DKGVQVQVEI PEIPVLALSP RDAFYSETEV
     IPFENAAGRI IADFVMVYPP GIPIFTPGGN YYTRKLRVYS
//