ID PDAD_THESM Reviewed; 158 AA. AC C6A2R5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 71. 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=TSIB_0849; OS Thermococcus sibiricus (strain DSM 12597 / MM 739). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=604354; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12597 / MM 739; RX PubMed=19447963; DOI=10.1128/aem.00718-09; RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome RT analysis."; RL Appl. Environ. Microbiol. 75:4580-4588(2009). 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; CP001463; ACS89910.1; -; Genomic_DNA. DR RefSeq; WP_015849130.1; NC_012883.1. DR AlphaFoldDB; C6A2R5; -. DR SMR; C6A2R5; -. DR STRING; 604354.TSIB_0849; -. DR GeneID; 8095840; -. DR KEGG; tsi:TSIB_0849; -. DR eggNOG; arCOG04490; Archaea. DR HOGENOM; CLU_114389_2_0_2; -. DR OrthoDB; 30748at2157; -. DR Proteomes; UP000009079; 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..43 FT /note="Pyruvoyl-dependent arginine decarboxylase subunit FT beta" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT /id="PRO_1000215198" FT CHAIN 44..158 FT /note="Pyruvoyl-dependent arginine decarboxylase subunit FT alpha" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT /id="PRO_1000215199" FT SITE 43..44 FT /note="Cleavage (non-hydrolytic)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" FT MOD_RES 44 FT /note="Pyruvic acid (Ser)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404" SQ SEQUENCE 158 AA; 17071 MW; 97831E53ABC8F769 CRC64; MSWTTPKKAI LLAASAEGST KLNAFDNALL KMGIGNVNLV KLSSVIPAYI EWIDELPKNI PVGMLLPTVY AHIESDEPGS TITAALGVGI SEGNEGGLIY EYSGYCTKEE AEKMVHKMVE EGFKVRGWKL KEFKAAVAEI TVKDRPVAAI AAVVMLPY //