PDAD_PYRHO
ID PDAD_PYRHO Reviewed; 158 AA.
AC O59240;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
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=PH1609;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30721.1; -; Genomic_DNA.
DR PIR; A71040; A71040.
DR RefSeq; WP_010885682.1; NC_000961.1.
DR AlphaFoldDB; O59240; -.
DR SMR; O59240; -.
DR STRING; 70601.3258038; -.
DR EnsemblBacteria; BAA30721; BAA30721; BAA30721.
DR GeneID; 1442461; -.
DR KEGG; pho:PH1609; -.
DR eggNOG; arCOG04490; Archaea.
DR OMA; AAALWYK; -.
DR OrthoDB; 98606at2157; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..43
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023332"
FT CHAIN 44..158
FT /note="Pyruvoyl-dependent arginine decarboxylase subunit
FT alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01404"
FT /id="PRO_0000023333"
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 158 AA; 17124 MW; 7D9CE49C99E8D7FB CRC64;
MTWITPKKAI MLAAAAEGGT KLNAFDNALL KMGIGNVNLV KLSSVIPAHI EWLDELPKNI
PIGMLLPTVY AHIESDEPGS TISAALGVGI SEGNEGGLIY EYAGYCKREE AEDMVRKMVE
EGFKVRGWKL KEFKVVSAEI TVKEKPAAAV AAVIMFPY