Q9YG22 (ARGDC_AERPE) 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:

APE_0079

Organism

Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]

Taxonomic identifier

272557 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	132 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. HAMAP MF_01298
Catalytic activity	L-arginine = agmatine + CO2. HAMAP MF_01298
Cofactor	Pyruvoyl group By similarity. HAMAP MF_01298
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. HAMAP MF_01298
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	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 – 69	69	Arginine decarboxylase beta chain By similarity		PRO_0000030129
	Chain	70 – 132	63	Arginine decarboxylase alpha chain By similarity		PRO_0000030130
Sites
	Active site	70	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	75	1	Proton acceptor; for processing activity By similarity
	Active site	90	1	Proton donor; for catalytic activity By similarity
	Site	69 – 70	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	70	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YG22 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 566D7112E65FD9FC	FASTA	132	15,015
	10 20 30 40 50 60 MERREDVIVG KHVYGSLYGV PREKATDEEY LRGVVVRAAE SAGATVHAVN SWTIPGEKGG 70 80 90 100 110 120 VSVIVLVLES HLALHTWPEY DYATFDIYTC GEHTDPWKAF ELLLSELKPR KYTVHYVDRS 130 QEKTVLEAQP RR

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000002 Genomic DNA. Translation: BAA78988.1.
PIR	B72761.
RefSeq	NP_146946.1. NC_000854.2.
3D structure databases
ProteinModelPortal	Q9YG22.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1445629.
GenomeReviews	Gene locus APE_0079 in contig BA000002_GR.
KEGG	ape:APE_0079.
NMPDR	fig|272557.1.peg.53.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG485559.
OMA	NILKPER.
ProtClustDB	PRK00458.
Enzyme and pathway databases
BioCyc	APER272557:APE0079-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_AERPE

Accession

Primary (citable) accession number: Q9YG22

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	November 1, 1999
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program