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Protein

Multifunctional alkaline phosphatase superfamily protein pRL90232

Gene

pRL90232

Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolytic enzyme with a broad substrate specificity acting on phosphate diesters and phosphonate monoesters.1 Publication

Cofactori

Mn2+1 PublicationNote: Mn2+ is probably the active metal ion. Other metals such as Zn, Ca and Fe can also act as cofactors.1 Publication

Kineticsi

kcat is 16 s(-1) with p-nitrophenyl phenyl phosphonate as substrate. kcat is 9.5 s(-1) with p-nitrophenyl ethyl phosphate as substrate.1 Publication
  1. KM=3.0 mM for phosphonate monoester p-nitrophenyl phenyl phosphonate (at 30 degrees Celsius and pH 7.5)1 Publication
  2. KM=2.3 mM for phosphate diester p-nitrophenyl ethyl phosphate (at 30 degrees Celsius and pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi12ManganeseCombined sources1 Publication1
    Active sitei57Nucleophile1 Publication1
    Metal bindingi57Manganese; via 3-oxoalanine1 Publication1
    Metal bindingi324ManganeseCombined sources1 Publication1
    Metal bindingi325Manganese; via tele nitrogenCombined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase
    LigandCalcium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciRLEG216596:GKE5-6838-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional alkaline phosphatase superfamily protein pRL90232Curated
    Alternative name(s):
    Phosphodiesterase1 Publication (EC:3.1.4.-1 Publication)
    Phosphonate monoester hydrolase1 Publication (EC:3.1.3.-1 Publication)
    Short name:
    RlPMH1 Publication
    Gene namesi
    Ordered Locus Names:pRL90232Imported
    Encoded oniPlasmid pRL9Imported
    OrganismiRhizobium leguminosarum bv. viciae (strain 3841)Imported
    Taxonomic identifieri216596 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
    Proteomesi
    • UP000006575 Componenti: Plasmid pRL9

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi13Q → A: Kcat increases 1.6-fold and affinity reduces 14-fold with phosphonate monoester as substrate. kcat increases 1.9-fold and affinity reduces 21.7-fold with phosphate diester as substrate. 1
    Mutagenesisi57C → A: Kcat reduces 1818-fold and affinity increases 1.1-fold with phosphonate monoester as substrate. kcat reduces 2021-fold and affinity reduces 1.3-fold with phosphate diester as substrate. 1
    Mutagenesisi57C → S: Kcat reduces 4.8-fold and affinity reduces 1.3-fold with phosphonate monoester as substrate. kcat reduces 5.9-fold and affinity increases 1.4-fold with phosphate diester as substrate. 1
    Mutagenesisi78N → A: Kcat reduces 10.7-fold and affinity reduces 1.3-fold with phosphonate monoester as substrate. kcat reduces 8.6-fold and affinity reduces 19.6-fold with phosphate diester as substrate. 1
    Mutagenesisi105Y → A: Kcat reduces 5.9-fold and affinity reduces 9.3-fold with phosphonate monoester as substrate. kcat reduces over 55.9-fold and affinity reduces over 30.4-fold with phosphate diester as substrate. 1
    Mutagenesisi107T → A: Kcat reduces 6.7-fold and affinity increases 9.7-fold with phosphonate monoester as substrate. kcat reduces 16.7-fold and affinity reduces 2.1-fold with phosphate diester as substrate. 1
    Mutagenesisi218H → A: Kcat reduces 16.0-fold and affinity reduces 5-fold with phosphonate monoester as substrate. kcat reduces 31.7-fold and affinity reduces 24.8-fold with phosphate diester as substrate. 1
    Mutagenesisi337K → A: Kcat reduces 1.3-fold and affinity reduces 4.7-fold with phosphonate monoester as substrate. kcat reduces 3.3-fold and affinity reduces 31.7-fold with phosphate diester as substrate. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004427191 – 514Multifunctional alkaline phosphatase superfamily protein pRL90232Add BLAST514

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei573-oxoalanine (Cys)UniRule annotation1 Publication1

    Post-translational modificationi

    The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.UniRule annotation1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2VQRX-ray1.42A1-514[»]
    ProteinModelPortaliQ1M964.
    SMRiQ1M964.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ1M964.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkaline phosphatase superfamily.1 Publication

    Phylogenomic databases

    HOGENOMiHOG000230030.
    OMAiLYADDWR.
    OrthoDBiPOG091H04HA.

    Family and domain databases

    Gene3Di3.40.720.10. 1 hit.
    InterProiView protein in InterPro
    IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core_sf.
    IPR032506. DUF4976.
    IPR000917. Sulfatase_N.
    PfamiView protein in Pfam
    PF16347. DUF4976. 1 hit.
    PF00884. Sulfatase. 1 hit.
    SUPFAMiSSF53649. SSF53649. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q1M964-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRKKNVLLIV VDQWRADFVP HVLRADGKID FLKTPNLDRL CREGVTFRNH
    60 70 80 90 100
    VTTCVPCGPA RASLLTGLYL MNHRAVQNTV PLDQRHLNLG KALRGVGYDP
    110 120 130 140 150
    ALIGYTTTVP DPRTTSPNDP RFRVLGDLMD GFHPVGAFEP NMEGYFGWVA
    160 170 180 190 200
    QNGFDLPEHR PDIWLPEGED AVAGATDRPS RIPKEFSDST FFTERALTYL
    210 220 230 240 250
    KGRDGKPFFL HLGYYRPHPP FVASAPYHAM YRPEDMPAPI RAANPDIEAA
    260 270 280 290 300
    QHPLMKFYVD SIRRGSFFQG AEGSGATLDE AELRQMRATY CGLITEVDDC
    310 320 330 340 350
    LGRVFSYLDE TGQWDDTLII FTSDHGEQLG DHHLLGKIGY NDPSFRIPLV
    360 370 380 390 400
    IKDAGENARA GAIESGFTES IDVMPTILDW LGGKIPHACD GLSLLPFLSE
    410 420 430 440 450
    GRPQDWRTEL HYEYDFRDVY YSEPQSFLGL GMNDCSLCVI QDERYKYVHF
    460 470 480 490 500
    AALPPLFFDL RHDPNEFTNL ADDPAYAALV RDYAQKALSW RLKHADRTLT
    510
    HYRSGPEGLS ERSH
    Length:514
    Mass (Da):58,054
    Last modified:May 30, 2006 - v1
    Checksum:i43F86726346FB4EB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AM236083 Genomic DNA. Translation: CAK03956.1.
    RefSeqiWP_011649751.1. NC_008379.1.

    Genome annotation databases

    EnsemblBacteriaiCAK03956; CAK03956; pRL90232.
    KEGGirle:pRL90232.

    Similar proteinsi

    Entry informationi

    Entry nameiRLPMH_RHIL3
    AccessioniPrimary (citable) accession number: Q1M964
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2017
    Last sequence update: May 30, 2006
    Last modified: January 31, 2018
    This is version 81 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, Plasmid, Reference proteome

    Documents

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