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A8AAB6 (ARGDC_IGNH4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Igni_0686
OrganismIgnicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125) [Complete proteome] [HAMAP]
Taxonomic identifier453591 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeIgnicoccus

Protein attributes

Sequence length144 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 – 7979Arginine decarboxylase beta chain By similarity
PRO_0000364115
Chain80 – 14465Arginine decarboxylase alpha chain By similarity
PRO_0000364116

Sites

Active site801Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site851Proton acceptor; for processing activity By similarity
Active site1001Proton donor; for catalytic activity By similarity
Site79 – 802Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue801Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A8AAB6 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 5471D495C23A939F

FASTA14416,426
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000816 Genomic DNA. Translation: ABU81868.1.
RefSeqYP_001435275.1. NC_009776.1.

3D structure databases

ProteinModelPortalA8AAB6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING453591.Igni_0686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU81868; ABU81868; Igni_0686.
GeneID5562345.
KEGGiho:Igni_0686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMACGEHSDP.
ProtClustDBCLSK964544.

Enzyme and pathway databases

BioCycIHOS453591:GHYN-708-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_IGNH4
AccessionPrimary (citable) accession number: A8AAB6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 43 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