ID   SPEA_DEIRA              Reviewed;         662 AA.
AC   Q9RXR4;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=DR_0243;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF09826.1; -; Genomic_DNA.
DR   PIR; B75544; B75544.
DR   RefSeq; NP_293967.1; NC_001263.1.
DR   RefSeq; WP_010886889.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RXR4; -.
DR   SMR; Q9RXR4; -.
DR   STRING; 243230.DR_0243; -.
DR   EnsemblBacteria; AAF09826; AAF09826; DR_0243.
DR   KEGG; dra:DR_0243; -.
DR   PATRIC; fig|243230.17.peg.407; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_0; -.
DR   InParanoid; Q9RXR4; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 164471at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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; 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..662
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149959"
FT   BINDING         308..318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         126
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   662 AA;  73528 MW;  88DDA5636BD83E6A CRC64;
     MCPARLRTPR TASLPTHRRS AMTTANPLNT SFTSADAAEL YQVPNWSGGW FRVSDKGLME
     ATPAPGLHAS LRAIVDEIVD RGESLPVILR FPQVLAGRVK HLNEAFQAAI NEYNYSGHYQ
     GVFPIKVNQR RAVVETVAAA GYDYAHGLEA GSKAELALCL AQKMHPDALL CCNGFKDDGF
     IKLALWGRTL GKNVVITIEK FTELDRILKQ AKALGVKPAV GVRFKLHARG SGQWEESGGD
     QAKFGLNAYE LLRVVERLKE ENMLDSLVML HTHIGSQITD IRRVKVAVRE AAQTYAGLIA
     AGADLKYLNV GGGLGVDYDG SKTTFYASMN YTVKEYAADI VYTVQEVCKA REVPEPVIVS
     ESGRALTAHH AVLILPVVDV TGPTRNLEDQ ELTVPGEDSH QIVRDMYETL ENISMRNYRE
     SYNDAVGDKQ TLHNLFDLGY VTLEDRARGE ALFNAILRKI AKLIQGEKYV PDELEDLQKV
     LADKFICNFS LFQSLPDNWA IGALFPIVPL DRLNEQPTRQ ATLVDITCDS DGKVEKFIDL
     RDVKATLPLH EPGDRPYYLG AFLMGAYQDV LGSAHNLFGK VSEAHVTVRP GGRFNIDLFV
     RGQKARRMIE SMGYEEPMLR DAIEDQADAA IGRGTLTQEQ EHELLEDYGE ELLGYTYLEY
     ES