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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Metal bindingi129Manganese 1By similarity1
    Metal bindingi129Manganese 1; via pros nitrogenPROSITE-ProRule annotation1 Publication1
    Metal bindingi152Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi152Manganese 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi154Manganese 2By similarity1
    Metal bindingi154Manganese 2; via pros nitrogenPROSITE-ProRule annotation1 Publication1
    Metal bindingi156Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi243Manganese 1PROSITE-ProRule annotation1 Publication1
    Metal bindingi243Manganese 2PROSITE-ProRule annotation1 Publication1
    Metal bindingi245Manganese 2PROSITE-ProRule annotation1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi161M → Y: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004291411 – 319GuanidinobutyraseAdd BLAST319

    Proteomic databases

    PaxDbiQ9I3S3.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA1421.

    Structurei

    Secondary structure

    1319
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni11 – 13Combined sources3
    Helixi23 – 25Combined sources3
    Helixi32 – 35Combined sources4
    Beta strandi39 – 44Combined sources6
    Helixi57 – 59Combined sources3
    Helixi60 – 67Combined sources8
    Helixi68 – 70Combined sources3
    Beta strandi73 – 75Combined sources3
    Turni76 – 78Combined sources3
    Helixi82 – 84Combined sources3
    Beta strandi88 – 93Combined sources6
    Helixi101 – 117Combined sources17
    Beta strandi121 – 125Combined sources5
    Helixi129 – 131Combined sources3
    Helixi132 – 143Combined sources12
    Beta strandi145 – 151Combined sources7
    Turni168 – 170Combined sources3
    Helixi171 – 177Combined sources7
    Beta strandi181 – 191Combined sources11
    Beta strandi193 – 197Combined sources5
    Helixi199 – 207Combined sources9
    Beta strandi210 – 213Combined sources4
    Helixi214 – 216Combined sources3
    Turni217 – 219Combined sources3
    Helixi223 – 233Combined sources11
    Beta strandi235 – 243Combined sources9
    Helixi244 – 246Combined sources3
    Turni249 – 251Combined sources3
    Beta strandi255 – 257Combined sources3
    Helixi265 – 273Combined sources9
    Turni274 – 277Combined sources4
    Beta strandi278 – 286Combined sources9
    Helixi290 – 292Combined sources3
    Beta strandi294 – 296Combined sources3
    Helixi297 – 311Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NIOX-ray2.00A/B/C/D/E/F1-319[»]
    ProteinModelPortaliQ9I3S3.
    SMRiQ9I3S3.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3NIOX-ray2.00A/B/C/D/E/F1-319[»]
    ProteinModelPortaliQ9I3S3.
    SMRiQ9I3S3.
    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: November 2, 2016
    This is version 97 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.