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A4YH98

- ARGDC_METS5

UniProt

A4YH98 - ARGDC_METS5

Protein

Arginine decarboxylase proenzyme

Gene

Msed_1645

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (29 May 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
    Sitei75 – 762Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei76 – 761Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei81 – 811Proton acceptor; for processing activityUniRule annotation
    Active sitei96 – 961Proton 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

    BioCyciMSED399549:GH1O-1665-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:Msed_1645
    OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
    Taxonomic identifieri399549 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
    ProteomesiUP000000242: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7575Arginine decarboxylase beta chainUniRule annotationPRO_0000364117Add
    BLAST
    Chaini76 – 12853Arginine decarboxylase alpha chainUniRule annotationPRO_0000364118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Pyruvic 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

    STRINGi399549.Msed_1645.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YH98.
    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.

    A4YH98-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQVTFQSH EDRIVGKHVF GNLYDIDPED LNNEQLLKDL VLKAVEIAHM    50
    NLVEAKSWSF GGKKGGVSVI ALIEESHIAL HTWNEYNYAT LDVYTCGEDS 100
    DPQAAFKFIV EALKPRRYQV FFADRSSS 128
    Length:128
    Mass (Da):14,523
    Last modified:May 29, 2007 - v1
    Checksum:i1CAC28ABABA66EE3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP95800.1.
    RefSeqiYP_001191724.1. NC_009440.1.

    Genome annotation databases

    EnsemblBacteriaiABP95800; ABP95800; Msed_1645.
    GeneIDi5104850.
    KEGGimse:Msed_1645.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP95800.1 .
    RefSeqi YP_001191724.1. NC_009440.1.

    3D structure databases

    ProteinModelPortali A4YH98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 399549.Msed_1645.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP95800 ; ABP95800 ; Msed_1645 .
    GeneIDi 5104850.
    KEGGi mse:Msed_1645.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci MSED399549:GH1O-1665-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. "The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
      Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
      Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51363 / DSM 5348.

    Entry informationi

    Entry nameiARGDC_METS5
    AccessioniPrimary (citable) accession number: A4YH98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 50 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, 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