Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Metal bindingi126Manganese 1By similarity1
    Metal bindingi126Manganese 1; via pros nitrogenPROSITE-ProRule annotation1 Publication1
    Metal bindingi148Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi148Manganese 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi150Manganese 2By similarity1
    Metal bindingi150Manganese 2; via pros nitrogenPROSITE-ProRule annotation1 Publication1
    Metal bindingi152Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi240Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi240Manganese 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi242Manganese 2PROSITE-ProRule annotation1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi157Y → M: Reduces substrate affinity 10-fold and catalytic efficiency 3-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004291421 – 318GuanidinopropionaseAdd BLAST318

    Proteomic databases

    PaxDbiQ9I6K2.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA0288.

    Structurei

    Secondary structure

    1318
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni11 – 13Combined sources3
    Helixi23 – 25Combined sources3
    Helixi32 – 34Combined sources3
    Beta strandi36 – 42Combined sources7
    Beta strandi49 – 51Combined sources3
    Helixi54 – 56Combined sources3
    Helixi57 – 64Combined sources8
    Helixi65 – 67Combined sources3
    Turni73 – 75Combined sources3
    Helixi79 – 82Combined sources4
    Beta strandi85 – 90Combined sources6
    Helixi98 – 114Combined sources17
    Beta strandi118 – 125Combined sources8
    Helixi126 – 128Combined sources3
    Helixi129 – 136Combined sources8
    Beta strandi138 – 140Combined sources3
    Beta strandi142 – 147Combined sources6
    Turni158 – 160Combined sources3
    Helixi168 – 174Combined sources7
    Beta strandi178 – 188Combined sources11
    Beta strandi192 – 195Combined sources4
    Helixi199 – 204Combined sources6
    Beta strandi207 – 210Combined sources4
    Helixi211 – 230Combined sources20
    Beta strandi235 – 240Combined sources6
    Helixi241 – 243Combined sources3
    Turni246 – 248Combined sources3
    Helixi262 – 270Combined sources9
    Turni271 – 274Combined sources4
    Beta strandi277 – 283Combined sources7
    Helixi287 – 289Combined sources3
    Helixi294 – 317Combined sources24

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NIPX-ray2.50A/B/C/D/E/F1-318[»]
    3NIQX-ray2.07A/B1-318[»]
    ProteinModelPortaliQ9I6K2.
    SMRiQ9I6K2.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NIPX-ray2.50A/B/C/D/E/F1-318[»]
    3NIQX-ray2.07A/B1-318[»]
    ProteinModelPortaliQ9I6K2.
    SMRiQ9I6K2.
    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: November 2, 2016
    This is version 100 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.