ID   SPEA_BACSU              Reviewed;         490 AA.
AC   P21885; P26934;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Arginine decarboxylase;
DE            EC=4.1.1.19;
GN   Name=speA; Synonyms=cad; OrderedLocusNames=BSU14630;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Hemilae H., Koivula T., Paulin L.;
RT   "Cloning and sequencing the lysine decarboxylase of Bacillus subtilis.";
RL   Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA   Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT   "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT   168 chromosome: sequencing of a 27 kb segment and identification of several
RT   genes in the area.";
RL   Microbiology 142:3033-3037(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-490.
RC   STRAIN=168;
RX   PubMed=1697575; DOI=10.1128/jb.172.9.5052-5063.1990;
RA   Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.;
RT   "Secretory S complex of Bacillus subtilis: sequence analysis and identity
RT   to pyruvate dehydrogenase.";
RL   J. Bacteriol. 172:5052-5063(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 485-490.
RX   PubMed=1936936; DOI=10.1016/0378-1097(91)90417-9;
RA   Hemilae H.O.;
RT   "Sequence of a PAL-related lipoprotein from Bacillus subtilis.";
RL   FEMS Microbiol. Lett. 66:37-41(1991).
RN   [6]
RP   CHARACTERIZATION OF POLYAMINE PATHWAY.
RX   PubMed=9723923; DOI=10.1046/j.1365-2958.1998.00979.x;
RA   Sekowska A., Bertin P., Danchin A.;
RT   "Characterization of polyamine synthesis pathway in Bacillus subtilis
RT   168.";
RL   Mol. Microbiol. 29:851-858(1998).
CC   -!- FUNCTION: Catalyzes the formation of agmatine from arginine.
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   -!- 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   -!- CAUTION: Was originally (Ref.1) thought to be a lysine decarboxylase
CC       and was consequently named cad. {ECO:0000305}.
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DR   EMBL; X58433; CAA41337.1; -; Genomic_DNA.
DR   EMBL; AF012285; AAC24937.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13336.1; -; Genomic_DNA.
DR   EMBL; M57435; AAA62686.1; -; Genomic_DNA.
DR   PIR; A54546; A54546.
DR   RefSeq; NP_389346.1; NC_000964.3.
DR   RefSeq; WP_003244780.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P21885; -.
DR   SMR; P21885; -.
DR   STRING; 224308.BSU14630; -.
DR   jPOST; P21885; -.
DR   PaxDb; P21885; -.
DR   PRIDE; P21885; -.
DR   DNASU; 936002; -.
DR   EnsemblBacteria; CAB13336; CAB13336; BSU_14630.
DR   GeneID; 936002; -.
DR   KEGG; bsu:BSU14630; -.
DR   PATRIC; fig|224308.179.peg.1596; -.
DR   eggNOG; COG1982; Bacteria.
DR   InParanoid; P21885; -.
DR   OMA; WSTLLTE; -.
DR   PhylomeDB; P21885; -.
DR   BioCyc; BSUB:BSU14630-MON; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Putrescine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Spermidine biosynthesis.
FT   CHAIN           1..490
FT                   /note="Arginine decarboxylase"
FT                   /id="PRO_0000201147"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   490 AA;  53583 MW;  1AC7ACAE24F4F6D2 CRC64;
     MSQHETPLYT GLKKHASRQP VQFHIPGHKK GAGMDPEFRQ FIGENALSID LINIEPLDDL
     HAPKGIIKQA QDLAAEAFGA DHTFFSVQGT SGAIMTMVMA VCGPGDKIII PRNVHKSIMT
     AIVFSGAVPI FIHPEIDNEL GISHGITLES AKRALTEHPD AKGLLVINPT YFGVAADLKS
     IVELAHSFDV PVLVDEAHGV HIHFHDELPL SAMQAGADIA ATSVHKLGGS LTQSSILNMR
     EGLVSKDRVQ SILSMLTTTS TSYLLLASLD VARKRLATEG RQLAEETLKL ANQTRDRLNQ
     IEGIYCVGSE ILGSKAAYSY DPTKLIISVK SLGLTGHDVE KWLRESFNIE VELSDLYNIL
     CIFTPGDSQN DADRLVEALT EIAQQMSEQD VTHQQTEVLL PEIPLLAMTP RDAFYANTEV
     IPLKEASGRI IAEFVMVYPP GIPIFIPGEI ITEENISYIF KNLDAGLPVQ GPEDSTLHMI
     RVIKEQKAIQ