ARGDC_CALMQ
ID ARGDC_CALMQ Reviewed; 134 AA.
AC A8MBV3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Cmaq_0451;
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW01296.1; -; Genomic_DNA.
DR RefSeq; WP_012185516.1; NC_009954.1.
DR AlphaFoldDB; A8MBV3; -.
DR SMR; A8MBV3; -.
DR STRING; 397948.Cmaq_0451; -.
DR PRIDE; A8MBV3; -.
DR EnsemblBacteria; ABW01296; ABW01296; Cmaq_0451.
DR GeneID; 5709779; -.
DR KEGG; cma:Cmaq_0451; -.
DR eggNOG; arCOG00279; Archaea.
DR HOGENOM; CLU_125470_2_1_2; -.
DR OMA; VYTCGEH; -.
DR OrthoDB; 106151at2157; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000001137; Chromosome.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:InterPro.
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:0008295; P:spermidine biosynthetic process; IEA:InterPro.
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..81
FT /note="Arginine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000364111"
FT CHAIN 82..134
FT /note="Arginine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT /id="PRO_0000364112"
FT ACT_SITE 82
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 87
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT ACT_SITE 102
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT SITE 81..82
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT MOD_RES 82
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
SQ SEQUENCE 134 AA; 15053 MW; BFFCD14C36EE792E CRC64;
MLQQQESPIP RLGVGEEGVV GRHVFGEVWG VNDKLLQDDE YLKNLVIKAA EVANMHLVDV
KVWRFGGGDK GGVSVIALVL ESHIAIHTWP AYNYATIDVY TCGEHSRPWD AYDYIIKQLN
PKTFTKTIVD RSSK
