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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: -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

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.

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
  1. 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: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.
Proteins known to be involved in this subpathway in this organism are:
  1. Arginine decarboxylase proenzyme (SSO0536)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei82Schiff-base intermediate with substrate; via pyruvic acidBy similarity1
Active sitei87Proton acceptor; for processing activityBy similarity1
Active sitei102Proton donor; for catalytic activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis
LigandPyruvate, Schiff base

Enzyme and pathway databases

BRENDAi4.1.1.19 6163
SABIO-RKiQ9UWU1
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
Proteomesi
  • UP000001974 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000301491 – 81Arginine decarboxylase beta chainAdd BLAST81
ChainiPRO_000003015082 – 134Arginine decarboxylase alpha chainAdd BLAST53

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82Pyruvic acid (Ser); by autocatalysis1 Publication1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei81 – 82Cleavage (non-hydrolytic); by autolysis2

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
SMRiQ9UWU1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00279 Archaea
COG1586 LUCA
HOGENOMiHOG000216579
InParanoidiQ9UWU1
KOiK01611
OMAiVYTCGEH
OrthoDBiPOG093Z0GPL

Family and domain databases

HAMAPiMF_00464 AdoMetDC_1, 1 hit
MF_01298 ArgDC, 1 hit
InterProiView protein in InterPro
IPR003826 AdoMetDC_fam_prok
IPR027549 ArgDC
IPR016067 S-AdoMet_deCO2ase_core
IPR017716 S-AdoMet_deCOase_pro-enz
PANTHERiPTHR33866 PTHR33866, 1 hit
PfamiView protein in Pfam
PF02675 AdoMet_dc, 1 hit
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:May 1, 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
RefSeqiWP_009991039.1, NC_002754.1

Genome annotation databases

EnsemblBacteriaiAAK40855; AAK40855; SSO0536
GeneIDi27426844
KEGGisso:SSO0536
PATRICifig|273057.12.peg.534

Similar proteinsi

Entry informationi

Entry nameiARGDC_SULSO
AccessioniPrimary (citable) accession number: Q9UWU1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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