ID PDAD_METMP Reviewed; 164 AA. AC Q6LWX2; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01404}; DE Short=PvlArgDC {ECO:0000255|HAMAP-Rule:MF_01404}; DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01404}; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta {ECO:0000255|HAMAP-Rule:MF_01404}; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01404}; GN Name=pdaD {ECO:0000255|HAMAP-Rule:MF_01404}; GN OrderedLocusNames=MMP1582; OS Methanococcus maripaludis (strain S2 / LL). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=267377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2 / LL; RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004; RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., RA Olson M.V., Leigh J.A.; RT "Complete genome sequence of the genetically tractable hydrogenotrophic RT methanogen Methanococcus maripaludis."; RL J. Bacteriol. 186:6956-6969(2004). 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_01404}; CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01404}; CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01404}; CC -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000255|HAMAP- CC Rule:MF_01404}. 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; BX950229; CAF31138.1; -; Genomic_DNA. DR RefSeq; WP_011171526.1; NC_005791.1. DR AlphaFoldDB; Q6LWX2; -. DR SMR; Q6LWX2; -. DR STRING; 267377.MMP1582; -. DR EnsemblBacteria; CAF31138; CAF31138; MMP1582. DR GeneID; 2761980; -. DR KEGG; mmp:MMP1582; -. DR PATRIC; fig|267377.15.peg.1620; -. DR eggNOG; arCOG04490; Archaea. DR HOGENOM; CLU_114389_2_0_2; -. DR OrthoDB; 30748at2157; -. DR Proteomes; UP000000590; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR Gene3D; 3.30.60.30; -; 1. DR Gene3D; 3.50.20.10; Pyruvoyl-Dependent Histidine Decarboxylase, subunit B; 1. DR HAMAP; MF_01404; PvlArgDC; 1. DR InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase. DR InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand. DR InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase. DR NCBIfam; TIGR00286; arginine decarboxylase, pyruvoyl-dependent; 1. DR PANTHER; PTHR40438; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1. DR PANTHER; PTHR40438:SF1; PYRUVOYL-DEPENDENT ARGININE DECARBOXYLASE; 1. DR Pfam; PF01862; PvlArgDC; 1. DR PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1. DR SFLD; SFLDF00471; Pyruvoyl-dependent_arginine_de; 1. DR SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1. DR SFLD; SFLDS00055; Pyruvoyl-Dependent_Histidine/A; 1. DR SUPFAM; SSF56271; Pyruvoyl-dependent histidine and arginine decarboxylases; 1. PE 3: Inferred from homology; KW Decarboxylase; Lyase; Pyruvate; Reference proteome. FT CHAIN 1..51 FT /note="Pyruvoyl-dependent arginine decarboxylase subunit FT beta" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT /id="PRO_0000023322" FT CHAIN 52..164 FT /note="Pyruvoyl-dependent arginine decarboxylase subunit FT alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT /id="PRO_0000023323" FT SITE 51..52 FT /note="Cleavage (non-hydrolytic)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT MOD_RES 52 FT /note="Pyruvic acid (Ser)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" SQ SEQUENCE 164 AA; 17584 MW; FA47E589857389A8 CRC64; MIKSSAIHSP FEAPNTISLV AGTGDANNPL NAFDMSLLKS GIGNLNLIRI SSIMPPKADI IPLPKIPQGS LVPTAYGYQI SEIKGETVAA GISVAIPKDK ELCGLIMEYE CIGGKKECED TVRNMAKEGF EMRGWEIDEI ISIASEHTVE NIGCAFAAAA LWYK //