ID ARGDC_PYRCJ Reviewed; 126 AA. AC A3MTU5; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Arginine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_01298}; DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01298}; DE Short=ArgDC {ECO:0000255|HAMAP-Rule:MF_01298}; DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01298}; DE AltName: Full=Pyruvoyl-dependent arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01298}; DE Contains: DE RecName: Full=Arginine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_01298}; DE Contains: DE RecName: Full=Arginine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_01298}; DE Flags: Precursor; GN OrderedLocusNames=Pcal_0636; OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=410359; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21063 / JCM 11548 / VA1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E., RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.; RT "Complete sequence of Pyrobaculum calidifontis JCM 11548."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to CC agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) CC activity. {ECO:0000255|HAMAP-Rule:MF_01298}. 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_01298}; CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01298}; CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01298}; CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; CC agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01298}. CC -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a CC tetramer of alpha/beta heterodimers. {ECO:0000255|HAMAP-Rule:MF_01298}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of CC the active enzyme involves a self-maturation process in which the CC active site pyruvoyl group is generated from an internal serine residue CC via an autocatalytic post-translational modification. Two non-identical CC subunits are generated from the proenzyme in this reaction, and the CC pyruvate is formed at the N-terminus of the alpha chain, which is CC derived from the carboxyl end of the proenzyme. The post-translation CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, CC in which the side chain hydroxyl group of the serine supplies its CC oxygen atom to form the C-terminus of the beta chain, while the CC remainder of the serine residue undergoes an oxidative deamination to CC produce ammonia and the pyruvoyl group blocking the N-terminus of the CC alpha chain. {ECO:0000255|HAMAP-Rule:MF_01298}. CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01298}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000561; ABO08062.1; -; Genomic_DNA. DR AlphaFoldDB; A3MTU5; -. DR SMR; A3MTU5; -. DR STRING; 410359.Pcal_0636; -. DR KEGG; pcl:Pcal_0636; -. DR eggNOG; arCOG00279; Archaea. DR HOGENOM; CLU_125470_2_1_2; -. DR OrthoDB; 114016at2157; -. DR UniPathway; UPA00186; UER00284. DR Proteomes; UP000001431; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006527; P:arginine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1. DR HAMAP; MF_00464; AdoMetDC_1; 1. DR HAMAP; MF_01298; ArgDC; 1. DR InterPro; IPR003826; AdoMetDC_fam_prok. DR InterPro; IPR027549; ArgDC. DR InterPro; IPR016067; S-AdoMet_deCO2ase_core. DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz. DR NCBIfam; TIGR03330; SAM_DCase_Bsu; 1. DR PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1. DR PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1. DR Pfam; PF02675; AdoMet_dc; 1. DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis; KW Pyruvate; Schiff base; Zymogen. FT CHAIN 1..73 FT /note="Arginine decarboxylase beta chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT /id="PRO_0000364121" FT CHAIN 74..126 FT /note="Arginine decarboxylase alpha chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT /id="PRO_0000364122" FT ACT_SITE 74 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT ACT_SITE 79 FT /note="Proton acceptor; for processing activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT ACT_SITE 94 FT /note="Proton donor; for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT SITE 73..74 FT /note="Cleavage (non-hydrolytic); by autolysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" FT MOD_RES 74 FT /note="Pyruvic acid (Ser); by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298" SQ SEQUENCE 126 AA; 14324 MW; 8D4073B4DFF84F26 CRC64; MQATAQVQTP VVGRHVYGEL YGVDESLLKD EERLRRIVIE AAHIANMHLV EVNSWKFKGG DKEGVSVIAL VLESHIAIHT WPVYNFATVD VYTCGEHSDP MAAFRYIVSQ LNPKRFTVNY SDRSYK //