PDAD_METM6
ID PDAD_METM6 Reviewed; 164 AA.
AC A9A979;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=MmarC6_1088;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP000867; ABX01902.1; -; Genomic_DNA.
DR RefSeq; WP_012193846.1; NC_009975.1.
DR AlphaFoldDB; A9A979; -.
DR SMR; A9A979; -.
DR STRING; 444158.MmarC6_1088; -.
DR EnsemblBacteria; ABX01902; ABX01902; MmarC6_1088.
DR GeneID; 5738080; -.
DR KEGG; mmx:MmarC6_1088; -.
DR eggNOG; arCOG04490; Archaea.
DR HOGENOM; CLU_114389_2_0_2; -.
DR OMA; AAALWYK; -.
DR OrthoDB; 98606at2157; -.
DR PhylomeDB; A9A979; -.
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.
FT CHAIN 1..51
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_1000145470"
FT CHAIN 52..164
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_1000145471"
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; 17631 MW; E03A3FA47FEDC183 CRC64;
MMKTSAIHSP FEAPNTISLV AGTGDAKNPL NAFDMSLLES GIGNLNLIRI SSIMPPKADI
IPLPKIPQGS LVPTAYGYQI SELKGETVAA GISVAIPKDK ELCGLIMEYE CIGGKKECED
TVRNMAKEGF EMRGWEIDEI ISIASEHTVE NIGCAFAAAA LWYK
