Reviewed, UniProtKB/Swiss-Prot Q971K9 (ARGDC_SULTO)

Names and origin

Protein names

Recommended name:
    Arginine decarboxylase proenzyme
      Short name=ArgDC
      Short name=ADC
    EC=4.1.1.19
Alternative name(s):
    Pyruvoyl-dependent arginine decarboxylase
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine decarboxylase beta chain
    2- Recommended name:
            Arginine decarboxylase alpha chain

Gene names

Ordered Locus Names:

ST1348

Organism

Sulfolobus tokodaii [Complete proteome] [HAMAP]

Taxonomic identifier

111955 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus

Protein attributes

Sequence length	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity By similarity.
Catalytic activity	L-arginine = agmatine + CO2. HAMAP MF_01298
Cofactor	Pyruvoyl group By similarity.
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 By similarity.
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 By similarity.
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Polyamine biosynthesis
Ligand	Pyruvate Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 75	75	Arginine decarboxylase beta chain By similarity		PRO_0000030153
	Chain	76 – 128	53	Arginine decarboxylase alpha chain By similarity		PRO_0000030154
Sites
	Active site	76	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	81	1	Proton acceptor; for processing activity By similarity
	Active site	96	1	Proton donor; for catalytic activity By similarity
	Site	75 – 76	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	76	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q971K9-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F1B2775903D3430B	FASTA	128	14,559
	10 20 30 40 50 60 MSSQLISLVN TDRIIGKHVF GNLYDIDPKI LNDKDFLHNL VLEAVKIANM KLVEIKSWNF 70 80 90 100 110 120 GGKKGGVSVI ALVEESHIAL HTWTEYNYAT LDVYTCGENS NPQAAFEYIV SQLKPKRYQM FYADRSSE

References

[1]

"Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7." Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H. DNA Res. 8:123-140(2001) [PubMed: 11572479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000023 Genomic DNA. Translation: BAB66411.1.
RefSeq	NP_377302.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1459371.
GenomeReviews	Gene locus ST1348 in contig BA000023_GR.
KEGG	sto:ST1348.
NMPDR	fig|273063.1.peg.1470.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q971K9.
OMA	SHIALHT.
Enzyme and pathway databases
BRENDA	4.1.1.50. 261167.
Family and domain databases
HAMAP	MF_01298. [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.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGDC_SULTO

Accession

Primary (citable) accession number: Q971K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)