ID   SPEA_ALKHC              Reviewed;         491 AA.
AC   Q9K9K5;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Arginine decarboxylase;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=BH2640;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
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DR   EMBL; BA000004; BAB06359.1; -; Genomic_DNA.
DR   PIR; H83979; H83979.
DR   AlphaFoldDB; Q9K9K5; -.
DR   SMR; Q9K9K5; -.
DR   STRING; 272558.10175261; -.
DR   EnsemblBacteria; BAB06359; BAB06359; BAB06359.
DR   KEGG; bha:BH2640; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_025925_2_1_9; -.
DR   OMA; WSTLLTE; -.
DR   OrthoDB; 485164at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001258; 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; 3.40.640.10; -; 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   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   SUPFAM; SSF55904; SSF55904; 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..491
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000201146"
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  53449 MW;  3C2ACC55C3C57F5D CRC64;
     MSRQEQTPLF SGVVAHAKHN PVQFHIPGHK KGAGMDPAFR SFIGDNALSI DLINIGPLDD
     LHHPHGIIKE AQELAAEAFG ADHTFFSVQG TSGAIMTMIM SVVGPGEKII VPRNVHKSIM
     SAIVFSGATP VFIHPEIDPL LGISHGITIE AVEKALDAHP DAKGLLVINP TYFGIAANLK
     KIVELCHSRD VPVLVDEAHG VHIHFHEALP LSAMQAGADM AATSVHKLGG SLTQSSILNV
     REGLVSAKRV QTIISMLTTT STSYLLLASL DAARKHLATN GRDLIGYTIQ LADQARDQIN
     AIDGLYCVGK EILGTIATYD YDPTKLIISV KNLGITGYDA EVWLREHYQI EVELSDLYNI
     LCIVSFGDTE REMDLLVKAL SELADLHKHG ICERSPVSVY VPNIPTLAMS PRDAFYAETE
     VVPFEDSVGR TIAEFIMVYP PGIPILIPGE IITESNLAYI RENNRAGLPV QGPEDDTFRT
     LRVIKEHEAI R