PDAD_METKA
ID PDAD_METKA Reviewed; 150 AA.
AC Q8TXD4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=MK0740;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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; 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; AE009439; AAM01954.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXD4; -.
DR SMR; Q8TXD4; -.
DR STRING; 190192.MK0740; -.
DR EnsemblBacteria; AAM01954; AAM01954; MK0740.
DR KEGG; mka:MK0740; -.
DR HOGENOM; CLU_114389_2_0_2; -.
DR Proteomes; UP000001826; 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.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyruvate; Reference proteome.
FT CHAIN 1..41
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023316"
FT CHAIN 42..150
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023317"
FT SITE 41..42
FT /note="Cleavage (non-hydrolytic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT MOD_RES 42
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
SQ SEQUENCE 150 AA; 15596 MW; 8FBA7ED4CCB07181 CRC64;
MGVPKKYALV SGTGEADTSL AAFDAALIDA GIGDCNLVEL SSILPPNAEE DDLPEFPPGS
IVPAVVAKAV GRGLVSSCIC VGRLESGLGI VSERAATDSV ETVRRLAKRD VEEMARLRGE
KLVEVRTVTA STEPEDAEWA AAVAAVVFWG