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Q971K9 (ARGDC_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:STK_13480
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length128 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 – 7575Arginine decarboxylase beta chain By similarity
PRO_0000030153
Chain76 – 12853Arginine decarboxylase alpha chain By similarity
PRO_0000030154

Sites

Active site761Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site811Proton acceptor; for processing activity By similarity
Active site961Proton donor; for catalytic activity By similarity
Site75 – 762Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue761Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q971K9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F1B2775903D3430B

FASTA12814,559
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAK54535.1.
RefSeqNP_377302.1. NC_003106.2.

3D structure databases

ProteinModelPortalQ971K9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273063.ST1348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAK54535; BAK54535; STK_13480.
GeneID1459371.
KEGGsto:ST1348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMAHIANMHL.

Enzyme and pathway databases

BioCycSTOK273063:GJC7-1507-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_SULTO
AccessionPrimary (citable) accession number: Q971K9
Secondary accession number(s): F9VP27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 80 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