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Protein

Guanidinobutyrase

Gene

gbuA

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 specifically the hydrolysis of 4-guanidinobutanoate to 4-aminobutanoate and urea. Has no activity against arginine, agmatine, 3-guanidinopropionate and guanidinoacetate.2 Publications

Catalytic activityi

4-guanidinobutanoate + H2O = 4-aminobutanoate + urea.2 Publications

Cofactori

Mn2+PROSITE-ProRule annotation2 PublicationsNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation2 Publications

Kineticsi

kcat is 1012 s(-1) (PubMed:12029055) and 94.7 s(-1) (PubMed:21600989).2 Publications

  1. KM=49 mM for 4-guanidinobutanoate2 Publications
  2. KM=10.7 mM for 4-guanidinobutanoate2 Publications

    pH dependencei

    Optimum pH is 9.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi129 – 1291Manganese 1By similarity
    Metal bindingi129 – 1291Manganese 1; via pros nitrogenPROSITE-ProRule annotation1 Publication
    Metal bindingi152 – 1521Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi152 – 1521Manganese 2PROSITE-ProRule annotation1 Publication
    Metal bindingi154 – 1541Manganese 2By similarity
    Metal bindingi154 – 1541Manganese 2; via pros nitrogenPROSITE-ProRule annotation1 Publication
    Metal bindingi156 – 1561Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi243 – 2431Manganese 1PROSITE-ProRule annotation1 Publication
    Metal bindingi243 – 2431Manganese 2PROSITE-ProRule annotation1 Publication
    Metal bindingi245 – 2451Manganese 2PROSITE-ProRule annotation1 Publication

    GO - Molecular functioni

    • guanidinobutyrase activity Source: PseudoCAP
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • arginine catabolic process Source: PseudoCAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11558.
    SABIO-RKQ9I3S3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanidinobutyrase (EC:3.5.3.72 Publications)
    Gene namesi
    Name:gbuA
    Ordered Locus Names:PA1421
    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

    PseudoCAPiPA1421.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi161 – 1611M → Y: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 319319GuanidinobutyrasePRO_0000429141Add
    BLAST

    Proteomic databases

    PaxDbiQ9I3S3.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA1421.

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 133Combined sources
    Helixi23 – 253Combined sources
    Helixi32 – 354Combined sources
    Beta strandi39 – 446Combined sources
    Helixi57 – 593Combined sources
    Helixi60 – 678Combined sources
    Helixi68 – 703Combined sources
    Beta strandi73 – 753Combined sources
    Turni76 – 783Combined sources
    Helixi82 – 843Combined sources
    Beta strandi88 – 936Combined sources
    Helixi101 – 11717Combined sources
    Beta strandi121 – 1255Combined sources
    Helixi129 – 1313Combined sources
    Helixi132 – 14312Combined sources
    Beta strandi145 – 1517Combined sources
    Turni168 – 1703Combined sources
    Helixi171 – 1777Combined sources
    Beta strandi181 – 19111Combined sources
    Beta strandi193 – 1975Combined sources
    Helixi199 – 2079Combined sources
    Beta strandi210 – 2134Combined sources
    Helixi214 – 2163Combined sources
    Turni217 – 2193Combined sources
    Helixi223 – 23311Combined sources
    Beta strandi235 – 2439Combined sources
    Helixi244 – 2463Combined sources
    Turni249 – 2513Combined sources
    Beta strandi255 – 2573Combined sources
    Helixi265 – 2739Combined sources
    Turni274 – 2774Combined sources
    Beta strandi278 – 2869Combined sources
    Helixi290 – 2923Combined sources
    Beta strandi294 – 2963Combined sources
    Helixi297 – 31115Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NIOX-ray2.00A/B/C/D/E/F1-319[»]
    ProteinModelPortaliQ9I3S3.
    SMRiQ9I3S3. Positions 4-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105CYW. Bacteria.
    COG0010. LUCA.
    HOGENOMiHOG000204320.
    InParanoidiQ9I3S3.
    KOiK12255.
    OMAiGNDMPRF.
    PhylomeDBiQ9I3S3.

    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.

    Q9I3S3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDKNLHQPLG GNEMPRFGGI ATMMRLPHVQ SPAELDALDA AFVGVPLDIG
    60 70 80 90 100
    TSLRSGTRFG PREIRAESVM IRPYNMATGA APFDSLNVAD IGDVAINTFN
    110 120 130 140 150
    LLEAVRIIEQ EYDRILGHGI LPLTLGGDHT ITLPILRAIK KKHGKVGLVH
    160 170 180 190 200
    VDAHADVNDH MFGEKIAHGT TFRRAVEEDL LDCDRVVQIG LRAQGYTAED
    210 220 230 240 250
    FNWSRKQGFR VVQAEECWHK SLEPLMAEVR EKVGGGPVYL SFDIDGIDPA
    260 270 280 290 300
    WAPGTGTPEI GGLTTIQAME IIRGCQGLDL IGCDLVEVSP PYDTTGNTSL
    310
    LGANLLYEML CVLPGVVRR
    Length:319
    Mass (Da):34,728
    Last modified:March 1, 2001 - v1
    Checksum:iE119C5DD35CE9089
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04810.1.
    PIRiH83468.
    RefSeqiNP_250112.1. NC_002516.2.
    WP_003082966.1. NZ_ASJY01000213.1.

    Genome annotation databases

    EnsemblBacteriaiAAG04810; AAG04810; PA1421.
    GeneIDi881747.
    KEGGipae:PA1421.
    PATRICi19837168. VBIPseAer58763_1470.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04810.1.
    PIRiH83468.
    RefSeqiNP_250112.1. NC_002516.2.
    WP_003082966.1. NZ_ASJY01000213.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NIOX-ray2.00A/B/C/D/E/F1-319[»]
    ProteinModelPortaliQ9I3S3.
    SMRiQ9I3S3. Positions 4-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA1421.

    Proteomic databases

    PaxDbiQ9I3S3.

    Protocols and materials databases

    DNASUi881747.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG04810; AAG04810; PA1421.
    GeneIDi881747.
    KEGGipae:PA1421.
    PATRICi19837168. VBIPseAer58763_1470.

    Organism-specific databases

    PseudoCAPiPA1421.

    Phylogenomic databases

    eggNOGiENOG4105CYW. Bacteria.
    COG0010. LUCA.
    HOGENOMiHOG000204320.
    InParanoidiQ9I3S3.
    KOiK12255.
    OMAiGNDMPRF.
    PhylomeDBiQ9I3S3.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11558.
    SABIO-RKQ9I3S3.

    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 nameiGBUA_PSEAE
    AccessioniPrimary (citable) accession number: Q9I3S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: March 1, 2001
    Last modified: September 7, 2016
    This is version 95 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, Direct protein sequencing, 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.