PDAD2_METMA
ID PDAD2_METMA Reviewed; 183 AA.
AC P58890;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2;
DE Short=PvlArgDC 2;
DE EC=4.1.1.19;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2 subunit beta;
DE Contains:
DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase 2 subunit alpha;
GN Name=pdaD2; OrderedLocusNames=MM_2595;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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;
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000250};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000305}.
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DR EMBL; AE008384; AAM32291.1; -; Genomic_DNA.
DR RefSeq; WP_011034508.1; NC_003901.1.
DR AlphaFoldDB; P58890; -.
DR SMR; P58890; -.
DR STRING; 192952.MM_2595; -.
DR EnsemblBacteria; AAM32291; AAM32291; MM_2595.
DR GeneID; 44088096; -.
DR GeneID; 66134588; -.
DR KEGG; mma:MM_2595; -.
DR PATRIC; fig|192952.21.peg.2981; -.
DR eggNOG; arCOG04490; Archaea.
DR HOGENOM; CLU_114389_0_0_2; -.
DR OMA; SEHHSFG; -.
DR Proteomes; UP000000595; 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..40
FT /note="Pyruvoyl-dependent arginine decarboxylase 2 subunit
FT beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023320"
FT CHAIN 41..183
FT /note="Pyruvoyl-dependent arginine decarboxylase 2 subunit
FT alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023321"
FT SITE 40..41
FT /note="Cleavage (non-hydrolytic)"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20211 MW; EC848E8E644A2360 CRC64;
MIPRKAFLTK GTGVHKDRLA SFELALRDAK IEKYNLVSVS SILPPNCKLV PREEGLAELK
PGAIVHCVLA RNDTNEPHRL MASAIGTAVP VNEENYGYIS EHHSFGEEEI IAGEYAEDLA
ATMLATTLGI EFDAEMAWHE REQVYKASGH IFDTFHMCQT AKGDKDGKWT TTVAAMVFVT
SKC
