ID   ARGDC_IGNH4             Reviewed;         144 AA.
AC   A8AAB6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, 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=Igni_0686;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000816; ABU81868.1; -; Genomic_DNA.
DR   RefSeq; WP_011998720.1; NC_009776.1.
DR   AlphaFoldDB; A8AAB6; -.
DR   SMR; A8AAB6; -.
DR   STRING; 453591.Igni_0686; -.
DR   GeneID; 5562345; -.
DR   KEGG; iho:Igni_0686; -.
DR   eggNOG; arCOG00279; Archaea.
DR   HOGENOM; CLU_125470_2_1_2; -.
DR   OrthoDB; 114016at2157; -.
DR   PhylomeDB; A8AAB6; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000000262; 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   Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
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   NCBIfam; TIGR03330; SAM_DCase_Bsu; 1.
DR   PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR   Pfam; PF02675; AdoMet_dc; 1.
DR   SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; Reference proteome; Schiff base; Zymogen.
FT   CHAIN           1..79
FT                   /note="Arginine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT                   /id="PRO_0000364115"
FT   CHAIN           80..144
FT                   /note="Arginine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT                   /id="PRO_0000364116"
FT   ACT_SITE        80
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   ACT_SITE        85
FT                   /note="Proton acceptor; for processing activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   ACT_SITE        100
FT                   /note="Proton donor; for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   SITE            79..80
FT                   /note="Cleavage (non-hydrolytic); by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
FT   MOD_RES         80
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01298"
SQ   SEQUENCE   144 AA;  16426 MW;  5471D495C23A939F CRC64;
     MKTVELTNGS KKKVEDRIVG RHVYGNLYGV DPAKLWDEEG LKELVREAAE VANMKLVEVR
     SWKFTGYHGG VSVMALVLES HITIHTWPDY EYATVDVYTC GERSDPWRAF ELIVERLEPE
     DYVVHYSDRS SPKRPLGGTA GRIQ
//