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

Pseudouridine-5'-phosphate glycosidase

Gene

psuG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.UniRule annotation2 Publications

Catalytic activityi

Uracil + D-ribose 5-phosphate = pseudouridine 5'-phosphate + H2O.UniRule annotation2 Publications

Cofactori

Mn2+UniRule annotation2 Publications, Fe2+2 Publications, Co2+2 PublicationsNote: Binds 1 manganese ion per subunit. Can also use Fe2+ and Co2+. The unusual metal binding site is heavily hydrated, coordinated with an aspartate side chain and five water molecules, and likely plays a role in anchoring the PsiMP phosphate.2 Publications

Enzyme regulationi

Inhibited by Zn2+ and Ni2+.1 Publication

Kineticsi

kcat is 3.74 sec(-1) for the synthesis of PsiMP.1 Publication
  1. KM=60 µM for pseudouridine 5'-phosphate (in the presence of 0.5 mM Mn2+)1 Publication
  2. KM=169.6 µM for uracil1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei31Proton donor1 PublicationUniRule annotation1
    Binding sitei93SubstrateUniRule annotation1 Publication1
    Binding sitei113Substrate; via amide nitrogenUniRule annotation1 Publication1
    Metal bindingi145ManganeseUniRule annotation1 Publication1
    Active sitei166Nucleophile1 PublicationUniRule annotation1

    GO - Molecular functioni

    • hydrolase activity, acting on glycosyl bonds Source: EcoliWiki
    • identical protein binding Source: EcoCyc
    • manganese ion binding Source: EcoCyc
    • pseudouridylate synthase activity Source: EcoCyc

    GO - Biological processi

    • protein homotrimerization Source: EcoCyc

    Keywordsi

    Molecular functionGlycosidase, Hydrolase, Lyase
    LigandManganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12033-MONOMER
    MetaCyc:EG12033-MONOMER
    BRENDAi4.2.1.70 2026

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pseudouridine-5'-phosphate glycosidase1 PublicationUniRule annotation (EC:4.2.1.70UniRule annotation2 Publications)
    Short name:
    PsiMP glycosidase1 PublicationUniRule annotation
    Gene namesi
    Name:psuGUniRule annotationImported
    Synonyms:pscG, yeiN1 Publication
    Ordered Locus Names:b2165, JW2152
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12033 psuG

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi31E → A: 7500-fold decrease in reaction rate while little change in substrate affinity. 1 Publication1
    Mutagenesisi93K → A: 17-fold decrease in reaction rate while modest decrease in substrate affinity. 1 Publication1
    Mutagenesisi149D → A: Loss of activity. 1 Publication1
    Mutagenesisi166K → A: 2900-fold decrease in reaction rate while no change in substrate affinity. 1 Publication1
    Mutagenesisi289N → A: 17-fold decrease in reaction rate while modest decrease in substrate affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001691501 – 312Pseudouridine-5'-phosphate glycosidaseAdd BLAST312

    Proteomic databases

    PaxDbiP33025
    PRIDEiP33025

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4261702, 6 interactors
    DIPiDIP-11926N
    IntActiP33025, 13 interactors
    STRINGi316385.ECDH10B_2322

    Structurei

    Secondary structure

    1312
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni8 – 10Combined sources3
    Beta strandi11 – 13Combined sources3
    Helixi15 – 22Combined sources8
    Beta strandi27 – 30Combined sources4
    Helixi33 – 36Combined sources4
    Helixi43 – 57Combined sources15
    Beta strandi61 – 68Combined sources8
    Beta strandi71 – 75Combined sources5
    Helixi78 – 87Combined sources10
    Helixi88 – 90Combined sources3
    Beta strandi91 – 94Combined sources4
    Turni96 – 98Combined sources3
    Helixi99 – 104Combined sources6
    Beta strandi109 – 111Combined sources3
    Helixi113 – 122Combined sources10
    Beta strandi127 – 129Combined sources3
    Helixi140 – 143Combined sources4
    Helixi148 – 155Combined sources8
    Beta strandi159 – 162Combined sources4
    Helixi171 – 180Combined sources10
    Beta strandi185 – 189Combined sources5
    Beta strandi202 – 204Combined sources3
    Beta strandi206 – 209Combined sources4
    Helixi212 – 224Combined sources13
    Beta strandi231 – 234Combined sources4
    Helixi239 – 241Combined sources3
    Helixi245 – 262Combined sources18
    Helixi266 – 268Combined sources3
    Helixi269 – 280Combined sources12
    Turni281 – 283Combined sources3
    Helixi284 – 310Combined sources27

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4GIJX-ray1.94A/B/C1-312[»]
    4GIKX-ray2.19A/B/C1-312[»]
    4GILX-ray2.54A/B/C1-312[»]
    4GIMX-ray1.80A/B/C1-312[»]
    ProteinModelPortaliP33025
    SMRiP33025
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni147 – 149Substrate bindingUniRule annotation1 Publication3

    Sequence similaritiesi

    Belongs to the pseudouridine-5'-phosphate glycosidase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105D53 Bacteria
    COG2313 LUCA
    HOGENOMiHOG000064311
    InParanoidiP33025
    KOiK16329
    OMAiGEQTMDI
    PhylomeDBiP33025

    Family and domain databases

    Gene3Di3.40.1790.10, 1 hit
    HAMAPiMF_01876 PsiMP_glycosidase, 1 hit
    InterProiView protein in InterPro
    IPR022830 Indigdn_synthA-like
    IPR007342 PsuG
    PANTHERiPTHR42909 PTHR42909, 1 hit
    PfamiView protein in Pfam
    PF04227 Indigoidine_A, 1 hit
    SUPFAMiSSF110581 SSF110581, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P33025-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSELKISPEL LQISPEVQDA LKNKKPVVAL ESTIISHGMP FPQNAQTAIE
    60 70 80 90 100
    VEETIRKQGA VPATIAIIGG VMKVGLSKEE IELLGREGHN VTKVSRRDLP
    110 120 130 140 150
    FVVAAGKNGA TTVASTMIIA ALAGIKVFAT GGIGGVHRGA EHTFDISADL
    160 170 180 190 200
    QELANTNVTV VCAGAKSILD LGLTTEYLET FGVPLIGYQT KALPAFFCRT
    210 220 230 240 250
    SPFDVSIRLD SASEIARAMV VKWQSGLNGG LVVANPIPEQ FAMPEHTINA
    260 270 280 290 300
    AIDQAVAEAE AQGVIGKEST PFLLARVAEL TGGDSLKSNI QLVFNNAILA
    310
    SEIAKEYQRL AG
    Length:312
    Mass (Da):32,910
    Last modified:February 1, 1994 - v1
    Checksum:iEBD892C271404F1F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00007 Genomic DNA Translation: AAA60517.1
    U00096 Genomic DNA Translation: AAC75226.1
    AP009048 Genomic DNA Translation: BAE76642.1
    PIRiD64985
    RefSeqiNP_416670.1, NC_000913.3
    WP_001292460.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75226; AAC75226; b2165
    BAE76642; BAE76642; BAE76642
    GeneIDi946699
    KEGGiecj:JW2152
    eco:b2165
    PATRICifig|1411691.4.peg.74

    Similar proteinsi

    Entry informationi

    Entry nameiPSUG_ECOLI
    AccessioniPrimary (citable) accession number: P33025
    Secondary accession number(s): Q2MAR4
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: March 28, 2018
    This is version 126 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, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health