ARGDC_SACS2
ID ARGDC_SACS2 Reviewed; 134 AA.
AC Q9UWU1;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Arginine decarboxylase proenzyme;
DE Short=ADC;
DE Short=ArgDC;
DE EC=4.1.1.19;
DE AltName: Full=Pyruvoyl-dependent arginine decarboxylase;
DE Contains:
DE RecName: Full=Arginine decarboxylase beta chain;
DE Contains:
DE RecName: Full=Arginine decarboxylase alpha chain;
DE Flags: Precursor;
GN OrderedLocusNames=SSO0536; ORFNames=C22_015;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, MASS
RP SPECTROMETRY, SELF-PROCESSING, CLEAVAGE SITE, AND PYRUVATE FORMATION AT
RP SER-82.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18650422; DOI=10.1074/jbc.m802674200;
RA Giles T.N., Graham D.E.;
RT "Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine
RT decarboxylase enzyme.";
RL J. Biol. Chem. 283:25829-25838(2008).
CC -!- FUNCTION: Specifically catalyzes the decarboxylation of L-arginine to
CC agmatine. Is also able to decarboxylate L-canavanine, although less
CC efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC)
CC activity. {ECO:0000269|PubMed:18650422}.
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;
CC Evidence={ECO:0000269|PubMed:18650422};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:18650422};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:18650422};
CC -!- ACTIVITY REGULATION: Highly competitively inhibited by L-argininamide
CC and L-arginine methyl ester. Also inhibited by alpha-
CC difluoromethylarginine. Is not stimulated by potassium chloride as
CC observed for other decarboxylases. {ECO:0000269|PubMed:18650422}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 uM for L-arginine {ECO:0000269|PubMed:18650422};
CC Vmax=1.1 umol/min/mg enzyme {ECO:0000269|PubMed:18650422};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:18650422};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Highly thermostable.
CC Retains 80% activity after incubation at 90 degrees Celsius for 10
CC minutes. {ECO:0000269|PubMed:18650422};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta chains arranged as a
CC tetramer of alpha/beta heterodimers. {ECO:0000269|PubMed:18650422}.
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:0000269|PubMed:18650422}.
CC -!- MASS SPECTROMETRY: [Arginine decarboxylase alpha chain]: Mass=6123;
CC Method=Electrospray; Note=Pyruvoyl group-containing alpha subunit.;
CC Evidence={ECO:0000269|PubMed:18650422};
CC -!- MISCELLANEOUS: A chimeric protein containing the beta subunit of
CC SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity and
CC no AdoMetDC activity, implicating residues responsible for substrate
CC specificity in the beta subunit. But additional factors in the alpha
CC subunit are required for efficient cleavage and turnover.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y18930; CAB57763.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40855.1; -; Genomic_DNA.
DR PIR; H90199; H90199.
DR RefSeq; WP_009991039.1; NC_002754.1.
DR AlphaFoldDB; Q9UWU1; -.
DR SMR; Q9UWU1; -.
DR STRING; 273057.SSO0536; -.
DR EnsemblBacteria; AAK40855; AAK40855; SSO0536.
DR GeneID; 44129543; -.
DR KEGG; sso:SSO0536; -.
DR PATRIC; fig|273057.12.peg.534; -.
DR eggNOG; arCOG00279; Archaea.
DR HOGENOM; CLU_125470_2_1_2; -.
DR InParanoid; Q9UWU1; -.
DR OMA; VYTCGEH; -.
DR PhylomeDB; Q9UWU1; -.
DR BRENDA; 4.1.1.19; 6163.
DR SABIO-RK; Q9UWU1; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 1: Evidence at protein level;
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 /id="PRO_0000030149"
FT CHAIN 82..134
FT /note="Arginine decarboxylase alpha chain"
FT /id="PRO_0000030150"
FT ACT_SITE 82
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250"
FT ACT_SITE 87
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 102
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 81..82
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT MOD_RES 82
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18650422"
SQ SEQUENCE 134 AA; 15247 MW; E88793740CBA829D CRC64;
MSEREVLQKI NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA VDIAHMKLVE
IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY TCGEDSDPQS AFAHIVNALN
PKRYQMFYAD RSSQ
