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Q9UWU1

- ARGDC_SULSO

UniProt

Q9UWU1 - ARGDC_SULSO

Protein

Arginine decarboxylase proenzyme

Gene

SSO0536

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Pyruvoyl group.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

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis

    Keywords - Ligandi

    Pyruvate, Schiff base

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-515-MONOMER.
    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: 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.
    KOiK01611.
    OMAiHIANMHL.

    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

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    MSEREVLQKI NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA    50
    VDIAHMKLVE IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY 100
    TCGEDSDPQS AFAHIVNALN PKRYQMFYAD RSSQ 134
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18930 Genomic DNA. Translation: CAB57763.1.
    AE006641 Genomic DNA. Translation: AAK40855.1.
    PIRiH90199.
    RefSeqiNP_342065.1. NC_002754.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18930 Genomic DNA. Translation: CAB57763.1 .
    AE006641 Genomic DNA. Translation: AAK40855.1 .
    PIRi H90199.
    RefSeqi NP_342065.1. NC_002754.1.

    3D structure databases

    ProteinModelPortali Q9UWU1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO0536.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK40855 ; AAK40855 ; SSO0536 .
    GeneIDi 1454822.
    KEGGi sso:SSO0536.

    Phylogenomic databases

    eggNOGi COG1586.
    HOGENOMi HOG000216579.
    KOi K01611.
    OMAi HIANMHL.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci SSOL273057:GCH2-515-MONOMER.
    SABIO-RK Q9UWU1.

    Family and domain databases

    Gene3Di 3.60.90.10. 1 hit.
    HAMAPi MF_00464. AdoMetDC_1.
    MF_01298. ArgDC.
    InterProi IPR003826. AdoMetDC_fam_prok.
    IPR027549. ArgDC.
    IPR016067. S-AdoMet_deCO2ase_core.
    IPR017716. S-AdoMet_deCOase_pro-enz.
    [Graphical view ]
    Pfami PF02675. AdoMet_dc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56276. SSF56276. 1 hit.
    TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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(2008) [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 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 91 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