Q9UWU1 (ARGDC_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine decarboxylase proenzyme
Short name=ADC
Short name=ArgDC
EC=4.1.1.19

Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase

Cleaved into the following 2 chains:

1. Arginine decarboxylase beta chain
2. Arginine decarboxylase alpha chain

Gene names

Ordered Locus Names:	SSO0536
ORF Names:	C22_015

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically catalyzes the decarboxylation of L-arginine to agmatine. Is also able to decarboxylate L-canavanine, although less efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. Ref.3
Catalytic activity	L-arginine = agmatine + CO2. Ref.3
Cofactor	Pyruvoyl group. Ref.3
Enzyme regulation	Highly competitively inhibited by L-argininamide and L-arginine methyl ester. Also inhibited by alpha-difluoromethylarginine. Is not stimulated by potassium chloride as observed for other decarboxylases. Ref.3
Pathway	Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01298
Subunit structure	Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers. Ref.3
Post-translational modification	Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. HAMAP MF_01298
Miscellaneous	A chimeric protein containing the beta subunit of SSO0536 and the alpha subunit of SSO0585 (speH) has ArgDC activity and no AdoMetDC activity, implicating residues responsible for substrate specificity in the beta subunit. But additional factors in the alpha subunit are required for efficient cleavage and turnover. HAMAP MF_01298
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=150 µM for L-arginine Ref.3 Vmax=1.1 µmol/min/mg enzyme pH dependence: Optimum pH is 6. Temperature dependence: Optimum temperature is 80 degrees Celsius. Highly thermostable. Retains 80% activity after incubation at 90 degrees Celsius for 10 minutes.
Mass spectrometry	Molecular mass is 6123 Da from positions 82 - 134. Determined by ESI. Pyruvoyl group-containing alpha subunit. Ref.3

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyruvate Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	spermidine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: InterPro arginine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 81	81	Arginine decarboxylase beta chain HAMAP MF_01298		PRO_0000030149
	Chain	82 – 134	53	Arginine decarboxylase alpha chain HAMAP MF_01298		PRO_0000030150
Sites
	Active site	82	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	87	1	Proton acceptor; for processing activity By similarity
	Active site	102	1	Proton donor; for catalytic activity By similarity
	Site	81 – 82	2	Cleavage (non-hydrolytic); by autolysis
Amino acid modifications
	Modified residue	82	1	Pyruvic acid (Ser); by autocatalysis HAMAP MF_01298

Sequences

	Sequence		Length	Mass (Da)
	Q9UWU1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: E88793740CBA829D	FASTA	134	15,247
	10 20 30 40 50 60 MSEREVLQKI NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA VDIAHMKLVE 70 80 90 100 110 120 IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY TCGEDSDPQS AFAHIVNALN 130 PKRYQMFYAD RSSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon, Sulfolobus solfataricus P2." Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C., Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T., Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E., Medina N. , Peng X., Penny S.L., She Q., St Jean A., van der Oost J., Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W. Genome 43:116-136(2000) [PubMed: 10701121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]	"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed: 11427726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]	"Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme." Giles T.N., Graham D.E. J. Biol. Chem. 283:25829-25838(2008) [PubMed: 18650422] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, MASS SPECTROMETRY, SELF-PROCESSING, CLEAVAGE SITE. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y18930 Genomic DNA. Translation: CAB57763.1. AE006641 Genomic DNA. Translation: AAK40855.1.
PIR	H90199.
RefSeq	NP_342065.1. NC_002754.1.
3D structure databases
ProteinModelPortal	Q9UWU1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1454822.
GenomeReviews	Gene locus SSO0536 in contig AE006641_GR.
KEGG	sso:SSO0536.
NMPDR	fig|273057.1.peg.488.
Phylogenomic databases
HOGENOM	HBG485559.
OMA	FKAMEYI.
ProtClustDB	PRK00458.
Enzyme and pathway databases
BioCyc	SSOL273057:SSO0536-MONOMER.
Family and domain databases
HAMAP	MF_01298. ArgDC. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR016067. S-AdoMet_deCO2ase_core. IPR017716. S-AdoMet_deCOase_pro-enz. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGDC_SULSO

Accession

Primary (citable) accession number: Q9UWU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	May 1, 2000
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program