Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9YG22 (ARGDC_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine decarboxylase proenzyme

Short name=ADC
Short name=ArgDC
EC=4.1.1.19
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase
Gene names
Ordered Locus Names:APE_0079
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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-Rule MF_01298

Catalytic activity

L-arginine = agmatine + CO2. HAMAP-Rule MF_01298

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_01298

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule 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-Rule MF_01298

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   LigandPyruvate
Schiff base
   Molecular functionDecarboxylase
Lyase
   PTMAutocatalytic cleavage
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

polyamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionarginine decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6969Arginine decarboxylase beta chain By similarity
PRO_0000030129
Chain70 – 13263Arginine decarboxylase alpha chain By similarity
PRO_0000030130

Sites

Active site701Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site751Proton acceptor; for processing activity By similarity
Active site901Proton donor; for catalytic activity By similarity
Site69 – 702Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue701Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YG22 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 566D7112E65FD9FC

FASTA13215,015
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA78988.1.
PIRB72761.
RefSeqNP_146946.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YG22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_0079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA78988; BAA78988; APE_0079.
GeneID1445629.
KEGGape:APE_0079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMAFIRTTIT.

Enzyme and pathway databases

BioCycAPER272557:GJD6-49-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. SSF56276. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARGDC_AERPE
AccessionPrimary (citable) accession number: Q9YG22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways