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C3MQN7

- ARGDC_SULIL

UniProt

C3MQN7 - ARGDC_SULIL

Protein

Arginine decarboxylase proenzyme

Gene

LS215_1696

Organism
Sulfolobus islandicus (strain L.S.2.15 / Lassen #1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.UniRule annotation

    Catalytic activityi

    L-arginine = agmatine + CO2.UniRule annotation

    Cofactori

    Pyruvoyl group.UniRule annotation

    Pathwayi

    Sites

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

    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

    BioCyciSISL429572:GHOW-1757-MONOMER.
    UniPathwayiUPA00186; UER00284.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine decarboxylase proenzymeUniRule annotation (EC:4.1.1.19UniRule annotation)
    Short name:
    ADCUniRule annotation
    Short name:
    ArgDCUniRule annotation
    Alternative name(s):
    Pyruvoyl-dependent arginine decarboxylaseUniRule annotation
    Cleaved into the following 2 chains:
    Arginine decarboxylase beta chainUniRule annotation
    Arginine decarboxylase alpha chainUniRule annotation
    Gene namesi
    Ordered Locus Names:LS215_1696
    OrganismiSulfolobus islandicus (strain L.S.2.15 / Lassen #1)
    Taxonomic identifieri429572 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001747: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 8181Arginine decarboxylase beta chainUniRule annotationPRO_1000214229Add
    BLAST
    Chaini82 – 13453Arginine decarboxylase alpha chainUniRule annotationPRO_1000214230Add
    BLAST

    Amino acid modifications

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

    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.UniRule annotation

    Keywords - PTMi

    Autocatalytic cleavage, Zymogen

    Interactioni

    Subunit structurei

    Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.UniRule annotation

    Protein-protein interaction databases

    STRINGi429572.LS215_1696.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

    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.

    C3MQN7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQEVLQKN NSPEGKEDRI IGKHVFGNLY DIDAERLNDK EFLEKLVLEA    50
    VNIAHMKLVE IKAWSFGGKK GGVSVIALVE ESHIALHTWN EYNYATLDVY 100
    TCGEDSDPQS AFAHIVNALN PKRYQMFYAD RSSQ 134
    Length:134
    Mass (Da):15,219
    Last modified:June 16, 2009 - v1
    Checksum:iB1489B1B0017E590
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001399 Genomic DNA. Translation: ACP35700.1.
    RefSeqiYP_002832345.1. NC_012589.1.

    Genome annotation databases

    EnsemblBacteriaiACP35700; ACP35700; LS215_1696.
    GeneIDi7799331.
    KEGGisis:LS215_1696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001399 Genomic DNA. Translation: ACP35700.1 .
    RefSeqi YP_002832345.1. NC_012589.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 429572.LS215_1696.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACP35700 ; ACP35700 ; LS215_1696 .
    GeneIDi 7799331.
    KEGGi sis:LS215_1696.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci SISL429572:GHOW-1757-MONOMER.

    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: L.S.2.15 / Lassen #1.

    Entry informationi

    Entry nameiARGDC_SULIL
    AccessioniPrimary (citable) accession number: C3MQN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 31 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

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

    External Data

    Dasty 3