ID   SPEA_PASMU              Reviewed;         644 AA.
AC   Q9CL60;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000255|HAMAP-Rule:MF_01417}; OrderedLocusNames=PM1382;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000255|HAMAP-Rule:MF_01417}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}.
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DR   EMBL; AE004439; AAK03466.1; -; Genomic_DNA.
DR   RefSeq; WP_005757582.1; NC_002663.1.
DR   AlphaFoldDB; Q9CL60; -.
DR   SMR; Q9CL60; -.
DR   STRING; 747.DR93_235; -.
DR   EnsemblBacteria; AAK03466; AAK03466; PM1382.
DR   KEGG; pmu:PM1382; -.
DR   PATRIC; fig|272843.6.peg.1394; -.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01417; SpeA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR040634; Arg_decarb_HB.
DR   InterPro; IPR041128; Arg_decarbox_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022657; De-COase2_CS.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; PTHR43295; 1.
DR   Pfam; PF17810; Arg_decarb_HB; 1.
DR   Pfam; PF17944; Arg_decarbox_C; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..644
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149966"
FT   BINDING         293..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   644 AA;  72707 MW;  F6A7FEB0B8DE3D82 CRC64;
     MEQVTLTSDG TSSVFAENTV REVCNINYWG MRYYNVDEKG DIFVCPDPDK PQNRVSLAAL
     AEKVQREQGA HLPTLFCFPQ IIQHRLRSIN QAFKRAREDF GYEGNYFLVY PIKVNQHRRI
     VESLISSGQP LGLEAGSKAE LMAVLAHAGI TQTVIVCNGY KDREYVRFAL MGEKLGHKVY
     LVIEKLSEIQ LVLEEAAKLN VKPRLGVRAR LASQGSGKWQ SSGGEKSKFG LSASQVLSLV
     QMLKEHECLD CLQLLHFHLG SQLGNIRDVA TGVRESARFY VELHKLGVNI QCFDVGGGLG
     VDYEGNRTQS DCSVNYGLNE YADTVVWGIG QACREHGLPH PTIITESGRG VTAHHAVLVS
     NVIGVERYKF ETLAAPAKDA PSVLHSMWET WVDIQSSREK RSLRSWIHES QFDLSDVHNQ
     YNVGLLNLEQ RAWAEQLYLN ICHEVGQLFN EKHRSHRTII DELQERFADK LYVNFSLFQS
     LPDAWGIDQL FPVCPISNLN QPVSRRAVLL DITCDSDGTI DHYIDGDGIT TTMPMPHYEE
     DNPPLLGFFM VGAYQEILGN MHNLFGDTST VDVLVHEQDK AYIVDYDEGN TVADMLEYVY
     LDPKKLLDRY REQIEHSNLP ASEAIQFLNE LEVGLNGYTY LEDE