AC MF_01417; DC Protein; auto TR HAMAP; MF_01417; -; 1; level=0 XX Names: SpeA XX ID SPEA DE RecName: Full=Biosynthetic arginine decarboxylase; DE Short=ADC; DE EC=4.1.1.19; GN Name=speA; XX CC -!- FUNCTION: Catalyzes the biosynthesis 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=Mg(2+); Xref=ChEBI:CHEBI:18420; 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 -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. CC SpeA subfamily. XX DR Pfam; PF02784; Orn_Arg_deC_N; 1; trigger=no DR Pfam; PF00278; Orn_DAP_Arg_deC; 1; trigger=no DR PRINTS; PR01179; ODADCRBXLASE; 1; trigger=no DR NCBIfam; TIGR01273; SpeA; 1; trigger=no DR PROSITE; PS00878; ODR_DC_2_1; 1; trigger=no DR PROSITE; PS00879; ODR_DC_2_2; 1; trigger=no XX KW Polyamine biosynthesis KW Spermidine biosynthesis case or KW Putrescine biosynthesis end case KW Lyase KW Decarboxylase KW Pyridoxal phosphate KW Metal-binding KW Magnesium XX GO GO:0008792; F:arginine decarboxylase activity case or GO GO:0009446; P:putrescine biosynthetic process end case GO GO:0008295; P:spermidine biosynthetic process XX FT From: SPEA_ECOLI (P21170) FT BINDING 307..317 FT /ligand="substrate" FT Condition: [FIVLC]-[DN]-[IV]-G-G-G-L-[GA]-[VI]-D-[YF] FT MOD_RES 127 FT /note="N6-(pyridoxal phosphate)lysine" FT Condition: K XX Size: 626-695; Related: None; Template: P21170; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in SYNY3 Plasmid: None Comments: None XX # Revision 1.28 2023/06/01 //