PDAD_THEKO
ID PDAD_THEKO Reviewed; 157 AA.
AC Q5JFI4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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}; OrderedLocusNames=TK0149;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; AP006878; BAD84338.1; -; Genomic_DNA.
DR RefSeq; WP_011249104.1; NC_006624.1.
DR AlphaFoldDB; Q5JFI4; -.
DR SMR; Q5JFI4; -.
DR IntAct; Q5JFI4; 1.
DR MINT; Q5JFI4; -.
DR STRING; 69014.TK0149; -.
DR EnsemblBacteria; BAD84338; BAD84338; TK0149.
DR GeneID; 3234595; -.
DR KEGG; tko:TK0149; -.
DR PATRIC; fig|69014.16.peg.149; -.
DR eggNOG; arCOG04490; Archaea.
DR HOGENOM; CLU_114389_2_0_2; -.
DR InParanoid; Q5JFI4; -.
DR OMA; AAALWYK; -.
DR OrthoDB; 98606at2157; -.
DR PhylomeDB; Q5JFI4; -.
DR BioCyc; MetaCyc:MON-16731; -.
DR BRENDA; 4.1.1.19; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR Gene3D; 3.50.20.10; -; 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 PANTHER; PTHR40438; PTHR40438; 1.
DR Pfam; PF01862; PvlArgDC; 1.
DR PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR SFLD; SFLDG01170; Pyruvoyl-dependent_arginine_de; 1.
DR SUPFAM; SSF56271; SSF56271; 1.
DR TIGRFAMs; TIGR00286; TIGR00286; 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_0000023334"
FT CHAIN 44..157
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023335"
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 157 AA; 17062 MW; 9D91137305B1126E CRC64;
MSWTTPKRAF IGAATAEGGT KLNAFDNALL KLGIGNVNLV KLSSVIPAHI EWMEKVHDVP
IGMLLPTVYA HIESDEPGMT ISAALGVGIS KNNEGGLIYE YSGYCTKEEA EEMVRKMVEE
GFRQRGWELG EFKVASAEIT VKDKPAAAIA VVVMFPY