ID   SPEA_SYNR3              Reviewed;         640 AA.
AC   A5GWM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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};
GN   OrderedLocusNames=SynRCC307_2378;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {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; CT978603; CAK29281.1; -; Genomic_DNA.
DR   RefSeq; WP_011936790.1; NC_009482.1.
DR   AlphaFoldDB; A5GWM2; -.
DR   SMR; A5GWM2; -.
DR   STRING; 316278.SynRCC307_2378; -.
DR   EnsemblBacteria; CAK29281; CAK29281; SynRCC307_2378.
DR   KEGG; syr:SynRCC307_2378; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_3; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 164471at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001115; 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..640
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000024276"
FT   BINDING         291..301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         109
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   640 AA;  69862 MW;  B62EFE2DF8DD1705 CRC64;
     MVVAPSQVEQ QNWTPAASAQ LYGLDQWGDP YFSVNARGHV LVQPRGDRGG SLDLVELVEG
     LQSRDLQLPL LIRFEDILED RLERLHGAFE RAIAQYGYGG HYQGVFPVKC NQQRHVVEQL
     VESGRRWHFG LEAGSKAELL IALSLLDDPK ALLICNGYKD QRYIETAILA RQLGRQPVVV
     IEQADEVPRI IEASRNLGAA PLIGVRAKLS TRSTGRWGSS VGEKAKFGLS IPDLLATVEA
     LRDADLLGDL RLLHFHVGSQ ICDIAVLKDA LQEAGQLYVQ LASLGAPMGF LDVGGGLGVD
     YDGSRSATAA STNYSLQNYA NDVVATIREC CEPQGIVVPT LVSESGRAIA SHFSVLVFNV
     LGQSGVNQPS IPEAVEGEAL IVRNLRETLS GIGPDNLQEA WNDALKFKDD ALAAFRLGYL
     SLTERGKAEQ LYWACCSAIA DLLPGEEELP DELKGLKAAF ASTYYANLSV FRSAPDTWAI
     DQLFPVMPIH RLEEQPRELG SFADLTCDSD GKLARFIASG SAKPLLELHE LKDGEPYWIG
     LFLGGAYQEV MGNLHNLFGS TNAVSIRLSP GGPYRVEHVV RGQTNSDVLE AMEHNPEALL
     ERLRQASEEA IGSGDLSISA ARRLMQHLEG SLRQTTYLEE