ARGDC_SULTO
ID ARGDC_SULTO Reviewed; 128 AA.
AC Q971K9; F9VP27;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Arginine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_01298};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01298};
DE Short=ArgDC {ECO:0000255|HAMAP-Rule:MF_01298};
DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01298};
DE AltName: Full=Pyruvoyl-dependent arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01298};
DE Contains:
DE RecName: Full=Arginine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_01298};
DE Contains:
DE RecName: Full=Arginine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_01298};
DE Flags: Precursor;
GN OrderedLocusNames=STK_13480;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to
CC agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC)
CC activity. {ECO:0000255|HAMAP-Rule:MF_01298}.
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_01298};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01298};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01298};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC tetramer of alpha/beta heterodimers. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC alpha chain. {ECO:0000255|HAMAP-Rule:MF_01298}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01298}.
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DR EMBL; BA000023; BAK54535.1; -; Genomic_DNA.
DR RefSeq; WP_010979389.1; NC_003106.2.
DR AlphaFoldDB; Q971K9; -.
DR SMR; Q971K9; -.
DR STRING; 273063.STK_13480; -.
DR EnsemblBacteria; BAK54535; BAK54535; STK_13480.
DR GeneID; 54123231; -.
DR KEGG; sto:STK_13480; -.
DR PATRIC; fig|273063.9.peg.1543; -.
DR eggNOG; arCOG00279; Archaea.
DR OMA; VYTCGEH; -.
DR OrthoDB; 106151at2157; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006527; P:arginine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00464; AdoMetDC_1; 1.
DR HAMAP; MF_01298; ArgDC; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR027549; ArgDC.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR PANTHER; PTHR33866; PTHR33866; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; Schiff base; Zymogen.
FT CHAIN 1..75
FT /note="Arginine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000030153"
FT CHAIN 76..128
FT /note="Arginine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000030154"
FT ACT_SITE 76
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 81
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 96
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT SITE 75..76
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT MOD_RES 76
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
SQ SEQUENCE 128 AA; 14559 MW; F1B2775903D3430B CRC64;
MSSQLISLVN TDRIIGKHVF GNLYDIDPKI LNDKDFLHNL VLEAVKIANM KLVEIKSWNF
GGKKGGVSVI ALVEESHIAL HTWTEYNYAT LDVYTCGENS NPQAAFEYIV SQLKPKRYQM
FYADRSSE
