ID   SPEA_BACAN              Reviewed;         493 AA.
AC   Q81MS2; Q6HU64; Q6KNE9;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Arginine decarboxylase;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=BA_4172, GBAA_4172, BAS3874;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP27896.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33294.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56175.1; -; Genomic_DNA.
DR   RefSeq; NP_846410.1; NC_003997.3.
DR   RefSeq; WP_011053233.1; NZ_LHUO01000006.1.
DR   RefSeq; YP_030124.1; NC_005945.1.
DR   AlphaFoldDB; Q81MS2; -.
DR   SMR; Q81MS2; -.
DR   IntAct; Q81MS2; 5.
DR   STRING; 260799.BAS3874; -.
DR   DNASU; 1089028; -.
DR   EnsemblBacteria; AAP27896; AAP27896; BA_4172.
DR   EnsemblBacteria; AAT33294; AAT33294; GBAA_4172.
DR   GeneID; 45023849; -.
DR   KEGG; ban:BA_4172; -.
DR   KEGG; bar:GBAA_4172; -.
DR   KEGG; bat:BAS3874; -.
DR   PATRIC; fig|198094.11.peg.4143; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_025925_2_1_9; -.
DR   OMA; WSTLLTE; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   Gene3D; 3.90.1150.10; -; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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..493
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000201144"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  54215 MW;  06215C0D777A73E8 CRC64;
     MYRLSQYETP LFTALVEHSK RNPIQFHIPG HKKGQGMDPE FREFIGHNAL AIDLINIAPL
     DDLHHPKGMI KEAQDLAAAA FGADHTFFSI QGTSGAIMTM VMSVCGPGDK ILVPRNVHKS
     VMSAIIFSGA KPIFMHPEID PKLGISHGIT IQSVKKALEE HSDAKGLLVI NPTYFGFAAD
     LEQIVQLAHS YDIPVLVDEA HGVHIHFHDE LPMSAMQAGA DMAATSVHKL GGSLTQSSIL
     NVKEGLVNVK HVQSIISMLT TTSTSYILLA SLDVARKRLA TEGKALIEQT IQLAEQVRNA
     INDIEHLYCP GKEMLGTDAT FNYDPTKIIV SVKDLGITGH QAEVWLREQY NIEVELSDLY
     NILCLVTFGD TESETNTLIA ALQDLSAIFK NKADKGVRIQ VEIPEIPVLA LSPRDAFYSE
     TEVIPFENAA GRIIADFVMV YPPGIPIFTP GEIITQDNLE YIRKNLEAGL PVQGPEDMTL
     QTLRVIKEYK PIS