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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: -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 sec(-1) (PubMed:12029055). kcat is 94.7 sec(-1) (PubMed:21600989).2 Publications
  1. KM=49 mM for 4-guanidinobutanoate1 Publication
  2. KM=10.7 mM for 4-guanidinobutanoate1 Publication

    pH dependencei

    Optimum pH is 9.5.1 Publication

    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

    Keywordsi

    Molecular functionHydrolase
    LigandManganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11558
    PAER208964:G1FZ6-1447-MONOMER
    SABIO-RKiQ9I3S3

    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 – 139Combined sources8
    Beta strandi147 – 151Combined sources5
    Turni168 – 170Combined sources3
    Helixi171 – 177Combined sources7
    Helixi183 – 185Combined sources3
    Beta strandi186 – 191Combined sources6
    Beta strandi193 – 197Combined sources5
    Helixi199 – 205Combined sources7
    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
    OMAiCIDAGFV
    PhylomeDBiQ9I3S3

    Family and domain databases

    InterProiView protein in InterPro
    IPR005925 Agmatinase-rel
    IPR006035 Ureohydrolase
    IPR023696 Ureohydrolase_dom_sf
    IPR020855 Ureohydrolase_Mn_BS
    PfamiView protein in Pfam
    PF00491 Arginase, 1 hit
    PIRSFiPIRSF036979 Arginase, 1 hit
    PRINTSiPR00116 ARGINASE
    SUPFAMiSSF52768 SSF52768, 1 hit
    TIGRFAMsiTIGR01230 agmatinase, 1 hit
    PROSITEiView protein in PROSITE
    PS01053 ARGINASE_1, 1 hit
    PS51409 ARGINASE_2, 1 hit

    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, NC_002516.2

    Genome annotation databases

    EnsemblBacteriaiAAG04810; AAG04810; PA1421
    GeneIDi881747
    KEGGipae:PA1421
    PATRICifig|208964.12.peg.1470

    Similar proteinsi

    Entry informationi

    Entry nameiGBUA_PSEAE
    AccessioniPrimary (citable) accession number: Q9I3S3
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 14, 2014
    Last sequence update: March 1, 2001
    Last modified: March 28, 2018
    This is version 104 of the entry and version 1 of the sequence. See 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health