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Protein

Arginine decarboxylase proenzyme

Gene

SSO0536

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically catalyzes the decarboxylation of L-arginine to agmatine. Is also able to decarboxylate L-canavanine, although less efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.1 Publication

Catalytic activityi

L-arginine = agmatine + CO2.1 Publication

Cofactori

pyruvate1 PublicationNote: Binds 1 pyruvoyl group covalently per subunit.1 Publication

Enzyme regulationi

Highly competitively inhibited by L-argininamide and L-arginine methyl ester. Also inhibited by alpha-difluoromethylarginine. Is not stimulated by potassium chloride as observed for other decarboxylases.1 Publication

Kineticsi

  1. KM=150 µM for L-arginine1 Publication

Vmax=1.1 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.1 Publication

Temperature dependencei

Optimum temperature is 80 degrees Celsius. Highly thermostable. Retains 80% activity after incubation at 90 degrees Celsius for 10 minutes.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei81 – 822Cleavage (non-hydrolytic); by autolysis
Active sitei82 – 821Schiff-base intermediate with substrate; via pyruvic acidBy similarity
Active sitei87 – 871Proton acceptor; for processing activityBy similarity
Active sitei102 – 1021Proton donor; for catalytic activityBy similarity

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine catabolic process Source: UniProtKB-HAMAP
  2. polyamine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis

Keywords - Ligandi

Pyruvate, Schiff base

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-515-MONOMER.
BRENDAi4.1.1.19. 6163.
SABIO-RKQ9UWU1.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine decarboxylase proenzyme (EC:4.1.1.19)
Short name:
ADC
Short name:
ArgDC
Alternative name(s):
Pyruvoyl-dependent arginine decarboxylase
Cleaved into the following 2 chains:
Gene namesi
Ordered Locus Names:SSO0536
ORF Names:C22_015
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8181Arginine decarboxylase beta chainPRO_0000030149Add
BLAST
Chaini82 – 13453Arginine decarboxylase alpha chainPRO_0000030150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Pyruvic acid (Ser); by autocatalysis

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO0536.

Structurei

3D structure databases

ProteinModelPortaliQ9UWU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
InParanoidiQ9UWU1.
KOiK01611.
OMAiCGEHSDP.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UWU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEREVLQKI NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA
60 70 80 90 100
VDIAHMKLVE IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY
110 120 130
TCGEDSDPQS AFAHIVNALN PKRYQMFYAD RSSQ
Length:134
Mass (Da):15,247
Last modified:April 30, 2000 - v1
Checksum:iE88793740CBA829D
GO

Mass spectrometryi

Molecular mass is 6123 Da from positions 82 - 134. Determined by ESI. Pyruvoyl group-containing alpha subunit.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18930 Genomic DNA. Translation: CAB57763.1.
AE006641 Genomic DNA. Translation: AAK40855.1.
PIRiH90199.
RefSeqiNP_342065.1. NC_002754.1.
WP_009991039.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40855; AAK40855; SSO0536.
GeneIDi1454822.
KEGGisso:SSO0536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18930 Genomic DNA. Translation: CAB57763.1.
AE006641 Genomic DNA. Translation: AAK40855.1.
PIRiH90199.
RefSeqiNP_342065.1. NC_002754.1.
WP_009991039.1. NC_002754.1.

3D structure databases

ProteinModelPortaliQ9UWU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40855; AAK40855; SSO0536.
GeneIDi1454822.
KEGGisso:SSO0536.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
InParanoidiQ9UWU1.
KOiK01611.
OMAiCGEHSDP.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciSSOL273057:GCH2-515-MONOMER.
BRENDAi4.1.1.19. 6163.
SABIO-RKQ9UWU1.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
MF_01298. ArgDC.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR027549. ArgDC.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme."
    Giles T.N., Graham D.E.
    J. Biol. Chem. 283:25829-25838(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, MASS SPECTROMETRY, SELF-PROCESSING, CLEAVAGE SITE.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Entry informationi

Entry nameiARGDC_SULSO
AccessioniPrimary (citable) accession number: Q9UWU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2001
Last sequence update: April 30, 2000
Last modified: March 31, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

A chimeric protein containing the beta subunit of SSO0536 and the alpha subunit of SSO0585 (SpeH) has ArgDC activity and no AdoMetDC activity, implicating residues responsible for substrate specificity in the beta subunit. But additional factors in the alpha subunit are required for efficient cleavage and turnover.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.