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Q9YG22

- ARGDC_AERPE

UniProt

Q9YG22 - ARGDC_AERPE

Protein

Arginine decarboxylase proenzyme

Gene

APE_0079

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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
    Sitei69 – 702Cleavage (non-hydrolytic); by autolysisUniRule annotation
    Active sitei70 – 701Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
    Active sitei75 – 751Proton acceptor; for processing activityUniRule annotation
    Active sitei90 – 901Proton 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

    BioCyciAPER272557:GJD6-49-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:APE_0079
    OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
    Taxonomic identifieri272557 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
    ProteomesiUP000002518: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6969Arginine decarboxylase beta chainUniRule annotationPRO_0000030129Add
    BLAST
    Chaini70 – 13263Arginine decarboxylase alpha chainUniRule annotationPRO_0000030130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701Pyruvic 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

    STRINGi272557.APE_0079.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YG22.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1586.
    HOGENOMiHOG000216579.
    KOiK01611.
    OMAiFIRTTIT.

    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.

    Q9YG22-1 [UniParc]FASTAAdd to Basket

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    MERREDVIVG KHVYGSLYGV PREKATDEEY LRGVVVRAAE SAGATVHAVN    50
    SWTIPGEKGG VSVIVLVLES HLALHTWPEY DYATFDIYTC GEHTDPWKAF 100
    ELLLSELKPR KYTVHYVDRS QEKTVLEAQP RR 132
    Length:132
    Mass (Da):15,015
    Last modified:November 1, 1999 - v1
    Checksum:i566D7112E65FD9FC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000002 Genomic DNA. Translation: BAA78988.1.
    PIRiB72761.
    RefSeqiNP_146946.1. NC_000854.2.
    WP_010865472.1. NC_000854.2.

    Genome annotation databases

    EnsemblBacteriaiBAA78988; BAA78988; APE_0079.
    GeneIDi1445629.
    KEGGiape:APE_0079.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000002 Genomic DNA. Translation: BAA78988.1 .
    PIRi B72761.
    RefSeqi NP_146946.1. NC_000854.2.
    WP_010865472.1. NC_000854.2.

    3D structure databases

    ProteinModelPortali Q9YG22.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272557.APE_0079.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAA78988 ; BAA78988 ; APE_0079 .
    GeneIDi 1445629.
    KEGGi ape:APE_0079.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci APER272557:GJD6-49-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: ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1.

    Entry informationi

    Entry nameiARGDC_AERPE
    AccessioniPrimary (citable) accession number: Q9YG22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 90 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