ID   PDAD_NITMS              Reviewed;         183 AA.
AC   A9A5S1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Nmar_1180;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX13076.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A5S1; -.
DR   SMR; A9A5S1; -.
DR   STRING; 436308.Nmar_1180; -.
DR   EnsemblBacteria; ABX13076; ABX13076; Nmar_1180.
DR   KEGG; nmr:Nmar_1180; -.
DR   eggNOG; arCOG04490; Archaea.
DR   HOGENOM; CLU_114389_0_0_2; -.
DR   OMA; SEHHSFG; -.
DR   PhylomeDB; A9A5S1; -.
DR   Proteomes; UP000000792; 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_1000145472"
FT   CHAIN           44..183
FT                   /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT                   alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT                   /id="PRO_1000145473"
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   183 AA;  20507 MW;  0E5D71CB24A68451 CRC64;
     MLDLVAKKLF LTRGKGIHED RLTSFEYALR DAGIAGTNLV LISSIFPPKA KLISRKEGLQ
     QIKPGQILFT IYSKNQTNEP HRMCSASVGI AQPKDKDRYG YLSEYEAFGQ TETQAGDYAE
     DIAAQMLASS LGIPFDVDKN WDEKRQQWKI SGEIYKTQNI TQQTRGDKDG KWTTVFAAAV
     LLV