Reviewed, UniProtKB/Swiss-Prot A8AAB6 (ARGDC_IGNH4)

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:

Igni_0686

Organism

Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125) [Complete proteome] [HAMAP]

Taxonomic identifier

453591 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Ignicoccus

Protein attributes

Sequence length	144 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 – 79	79	Arginine decarboxylase beta chain By similarity		PRO_0000364115
	Chain	80 – 144	65	Arginine decarboxylase alpha chain By similarity		PRO_0000364116
Sites
	Active site	80	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	85	1	Proton acceptor; for processing activity By similarity
	Active site	100	1	Proton donor; for catalytic activity By similarity
	Site	79 – 80	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	80	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8AAB6-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 5471D495C23A939F	FASTA	144	16,426
	10 20 30 40 50 60 MKTVELTNGS KKKVEDRIVG RHVYGNLYGV DPAKLWDEEG LKELVREAAE VANMKLVEVR 70 80 90 100 110 120 SWKFTGYHGG VSVMALVLES HITIHTWPDY EYATVDVYTC GERSDPWRAF ELIVERLEPE 130 140 DYVVHYSDRS SPKRPLGGTA GRIQ

References

[1]

"Unicellular symbiosis at high temperature: genomic insights into the Ignicoccus hospitalis - Naoarchaeum equitans relationship." Podar M., Anderson I., Ivanova N., Wall M., Mavrommatis K., Lykidis A., Chen J., Hudson M., Deciu C., Hutchison D., Eads J., Fernandes F., Tamang D., Szeto E., Land M., Lapidus A., Kyrpides N., Chang C. , Saier M., Eisen J., Rachel R., Huber H., Keller M., Richardson P., Stetter K. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000816 Genomic DNA. Translation: ABU81868.1.
RefSeq	YP_001435275.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8AAB6.
Genome annotation databases
GeneID	5562345.
GenomeReviews	Gene locus Igni_0686 in contig CP000816_GR.
KEGG	iho:Igni_0686.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	FHTWPEY.
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_IGNH4

Accession

Primary (citable) accession number: A8AAB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 17 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)