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Protein

Guanidinopropionase

Gene

gpuA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of 3-guanidinopropanoate to beta-alanine and urea. Possesses low activity against 4-guanidinobutanoate. Has no activity against arginine and agmatine.1 Publication

Catalytic activityi

3-guanidinopropanoate + H2O = beta-alanine + urea.1 Publication

Cofactori

Mn2+PROSITE-ProRule annotation1 PublicationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation1 Publication

Kineticsi

kcat is 106 s(-1) with 3-guanidinopropanoate as substrate. kcat is 57.6 s(-1) for 4-guanidinobutanoate as substrate.

  1. KM=12.8 mM for 3-guanidinopropanoate1 Publication
  2. KM=37.3 mM for 4-guanidinobutanoate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi126 – 1261Manganese 1By similarity
    Metal bindingi126 – 1261Manganese 1; via pros nitrogenPROSITE-ProRule annotation1 Publication
    Metal bindingi148 – 1481Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi148 – 1481Manganese 2PROSITE-ProRule annotation1 Publication
    Metal bindingi150 – 1501Manganese 2By similarity
    Metal bindingi150 – 1501Manganese 2; via pros nitrogenPROSITE-ProRule annotation1 Publication
    Metal bindingi152 – 1521Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi240 – 2401Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi240 – 2401Manganese 2PROSITE-ProRule annotation1 Publication
    Metal bindingi242 – 2421Manganese 2PROSITE-ProRule annotation1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.5.3.17. 5087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanidinopropionase (EC:3.5.3.171 Publication)
    Gene namesi
    Name:gpuA
    Ordered Locus Names:PA0288
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA0288.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571Y → M: Reduces substrate affinity 10-fold and catalytic efficiency 3-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318GuanidinopropionasePRO_0000429142Add
    BLAST

    Proteomic databases

    PaxDbiQ9I6K2.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA0288.

    Structurei

    Secondary structure

    1
    318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 133Combined sources
    Helixi23 – 253Combined sources
    Helixi32 – 343Combined sources
    Beta strandi36 – 427Combined sources
    Beta strandi49 – 513Combined sources
    Helixi54 – 563Combined sources
    Helixi57 – 648Combined sources
    Helixi65 – 673Combined sources
    Turni73 – 753Combined sources
    Helixi79 – 824Combined sources
    Beta strandi85 – 906Combined sources
    Helixi98 – 11417Combined sources
    Beta strandi118 – 1258Combined sources
    Helixi126 – 1283Combined sources
    Helixi129 – 1368Combined sources
    Beta strandi138 – 1403Combined sources
    Beta strandi142 – 1476Combined sources
    Turni158 – 1603Combined sources
    Helixi168 – 1747Combined sources
    Beta strandi178 – 18811Combined sources
    Beta strandi192 – 1954Combined sources
    Helixi199 – 2046Combined sources
    Beta strandi207 – 2104Combined sources
    Helixi211 – 23020Combined sources
    Beta strandi235 – 2406Combined sources
    Helixi241 – 2433Combined sources
    Turni246 – 2483Combined sources
    Helixi262 – 2709Combined sources
    Turni271 – 2744Combined sources
    Beta strandi277 – 2837Combined sources
    Helixi287 – 2893Combined sources
    Helixi294 – 31724Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NIPX-ray2.50A/B/C/D/E/F1-318[»]
    3NIQX-ray2.07A/B1-318[»]
    ProteinModelPortaliQ9I6K2.
    SMRiQ9I6K2. Positions 3-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9I6K2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105CYW. Bacteria.
    COG0010. LUCA.
    InParanoidiQ9I6K2.
    KOiK18459.
    OMAiQLPLTGW.
    PhylomeDBiQ9I6K2.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01230. agmatinase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9I6K2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNDHPQPLD AAEIPRFAGI PTFMRLPAFT DPAALQVGLI GVPWDGGTTN
    60 70 80 90 100
    RAGARHGPRE VRNLSSLMRK VHHVSRIAPY DLVRVGDLGD APVNPIDLLD
    110 120 130 140 150
    SLRRIEGFYR QVHAAGTLPL SVGGDHLVTL PIFRALGRER PLGMVHFDAH
    160 170 180 190 200
    SDTNDRYFGD NPYTHGTPFR RAIEEGLLDP LRTVQIGIRG SVYSPDDDAF
    210 220 230 240 250
    ARECGIRVIH MEEFVELGVE ATLAEARRVV GAGPTYVSFD VDVLDPAFAP
    260 270 280 290 300
    GTGTPEIGGM TSLQAQQLVR GLRGLDLVGA DVVEVSPPFD VGGATALVGA
    310
    TMMFELLCLL AESAARSA
    Length:318
    Mass (Da):34,189
    Last modified:March 1, 2001 - v1
    Checksum:i5617D78C4AD626C3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG03677.1.
    PIRiH83610.
    RefSeqiNP_248979.1. NC_002516.2.
    WP_003112934.1. NZ_ASJY01000065.1.

    Genome annotation databases

    EnsemblBacteriaiAAG03677; AAG03677; PA0288.
    GeneIDi880781.
    KEGGipae:PA0288.
    PATRICi19834802. VBIPseAer58763_0302.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG03677.1.
    PIRiH83610.
    RefSeqiNP_248979.1. NC_002516.2.
    WP_003112934.1. NZ_ASJY01000065.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NIPX-ray2.50A/B/C/D/E/F1-318[»]
    3NIQX-ray2.07A/B1-318[»]
    ProteinModelPortaliQ9I6K2.
    SMRiQ9I6K2. Positions 3-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA0288.

    Proteomic databases

    PaxDbiQ9I6K2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG03677; AAG03677; PA0288.
    GeneIDi880781.
    KEGGipae:PA0288.
    PATRICi19834802. VBIPseAer58763_0302.

    Organism-specific databases

    PseudoCAPiPA0288.

    Phylogenomic databases

    eggNOGiENOG4105CYW. Bacteria.
    COG0010. LUCA.
    InParanoidiQ9I6K2.
    KOiK18459.
    OMAiQLPLTGW.
    PhylomeDBiQ9I6K2.

    Enzyme and pathway databases

    BRENDAi3.5.3.17. 5087.

    Miscellaneous databases

    EvolutionaryTraceiQ9I6K2.

    Family and domain databases

    Gene3Di3.40.800.10. 1 hit.
    InterProiIPR005925. Agmatinase-rel.
    IPR006035. Ureohydrolase.
    IPR023696. Ureohydrolase_domain.
    IPR020855. Ureohydrolase_Mn_BS.
    [Graphical view]
    PANTHERiPTHR11358. PTHR11358. 1 hit.
    PfamiPF00491. Arginase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036979. Arginase. 1 hit.
    PRINTSiPR00116. ARGINASE.
    TIGRFAMsiTIGR01230. agmatinase. 1 hit.
    PROSITEiPS01053. ARGINASE_1. 1 hit.
    PS51409. ARGINASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGPUA_PSEAE
    AccessioniPrimary (citable) accession number: Q9I6K2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: March 1, 2001
    Last modified: September 7, 2016
    This is version 98 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.