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A1RV83

- ARGDC_PYRIL

UniProt

A1RV83 - ARGDC_PYRIL

Protein

Arginine decarboxylase proenzyme

Gene

Pisl_1714

Organism
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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
    Sitei73 – 742Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei74 – 741Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei79 – 791Proton acceptor; for processing activityUniRule annotation
    Active sitei94 – 941Proton 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

    BioCyciPISL384616:GC8H-1749-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:Pisl_1714
    OrganismiPyrobaculum islandicum (strain DSM 4184 / JCM 9189)
    Taxonomic identifieri384616 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
    ProteomesiUP000002595: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7373Arginine decarboxylase beta chainUniRule annotationPRO_0000364123Add
    BLAST
    Chaini74 – 12653Arginine decarboxylase alpha chainUniRule annotationPRO_0000364124Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741Pyruvic 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

    STRINGi384616.Pisl_1714.

    Structurei

    3D structure databases

    ProteinModelPortaliA1RV83.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    A1RV83-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTTTQVKTP IVGKHVYGEL YGVDEALLRD EEKLRRIVIE AAHIAKMHLV    50
    EVNSWRFKGG DKEGVSVIAL VLESHIAIHT WPVYNYATVD VYTCGEHSDP 100
    MAAFRYIVSQ LAPKRFTVNY SDRSYK 126
    Length:126
    Mass (Da):14,369
    Last modified:February 6, 2007 - v1
    Checksum:iEB5C0DDDC4D49CDE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000504 Genomic DNA. Translation: ABL88865.1.
    RefSeqiYP_931208.1. NC_008701.1.

    Genome annotation databases

    EnsemblBacteriaiABL88865; ABL88865; Pisl_1714.
    GeneIDi4617816.
    KEGGipis:Pisl_1714.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000504 Genomic DNA. Translation: ABL88865.1 .
    RefSeqi YP_931208.1. NC_008701.1.

    3D structure databases

    ProteinModelPortali A1RV83.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 384616.Pisl_1714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL88865 ; ABL88865 ; Pisl_1714 .
    GeneIDi 4617816.
    KEGGi pis:Pisl_1714.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci PISL384616:GC8H-1749-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. "Complete sequence of Pyrobaculum islandicum DSM 4184."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 4184 / JCM 9189.

    Entry informationi

    Entry nameiARGDC_PYRIL
    AccessioniPrimary (citable) accession number: A1RV83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 51 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