ARGDC_STAMF
ID ARGDC_STAMF Reviewed; 127 AA.
AC A3DLU8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Smar_0500;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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; CP000575; ABN69608.1; -; Genomic_DNA.
DR RefSeq; WP_011838799.1; NC_009033.1.
DR AlphaFoldDB; A3DLU8; -.
DR SMR; A3DLU8; -.
DR STRING; 399550.Smar_0500; -.
DR EnsemblBacteria; ABN69608; ABN69608; Smar_0500.
DR GeneID; 4907823; -.
DR KEGG; smr:Smar_0500; -.
DR eggNOG; arCOG00279; Archaea.
DR HOGENOM; CLU_125470_2_1_2; -.
DR OMA; VYTCGEH; -.
DR OrthoDB; 106151at2157; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000254; 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..71
FT /note="Arginine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000364125"
FT CHAIN 72..127
FT /note="Arginine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000364126"
FT ACT_SITE 72
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 77
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 92
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT SITE 71..72
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT MOD_RES 72
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
SQ SEQUENCE 127 AA; 14547 MW; AA1932B4F767B069 CRC64;
MDNTLIDPRI IGKHVYGNLY EIPEEIAGDE EYLRNVVVEA AKLANMTLLE VKSWKLGGEK
GGVSVIALVL ESHIAIHTWI NYRYATVDVY TCGEKSDPWR AFNYIVEKLK PKEYTVNYAD
RTQLLKQ
