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Protein

Alpha-D-glucose 1-phosphate phosphatase YihX

Gene

yihX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation of alpha-D-glucose 1-phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates (PubMed:16990279) (PubMed:25484615). Has no activity with the beta form of Glc1P. In addition, YihX has significant phosphatase activity against pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity (PubMed:16990279).2 Publications

Catalytic activityi

Alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate.2 Publications

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 PublicationNote: Magnesium. Can also use other divalent metal cations such as manganese, cobalt or zinc.1 Publication

Kineticsi

kcat is 10.2 sec(-1) with alpha-Glc-1-P as substrate. kcat is 1.26 sec(-1) with alpha-Man-1-P as substrate. kcat is 0.98 sec(-1) with alpha-Gal-1-P as substrate. kcat is 0.09 sec(-1) with Glc-6-P as substrate (at pH 7.0 and 37 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=0.028 mM for imido-di-P (with magnesium ions as cofactor and at pH 9)1 Publication
  2. KM=0.24 mM for alpha-D-glucose-1-phosphate (with magnesium ions as cofactor and at pH 9)1 Publication
  3. KM=1.6 mM for alpha-fructose-1-phosphate (with manganese ions as cofactor and at pH 9)1 Publication
  4. KM=3.6 mM for acetyl-phosphate (with magnesium ions as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is 5.0-7.0.2 Publications

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei6Nucleophile1
    Metal bindingi6MagnesiumBy similarity1
    Binding sitei141Substrate1 Publication1
    Metal bindingi166MagnesiumBy similarity1
    Binding sitei166Substrate1 Publication1

    GO - Molecular functioni

    • glucose-1-phosphatase activity Source: EcoliWiki
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11850-MONOMER.
    ECOL316407:JW5566-MONOMER.
    MetaCyc:EG11850-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-D-glucose 1-phosphate phosphatase YihX (EC:3.1.3.102 Publications)
    Short name:
    Alpha-D-glucose-1-P phosphatase
    Alternative name(s):
    Alpha-D-glucose-1-phosphatase
    Haloacid dehalogenase-like phosphatase 41 Publication
    Short name:
    HAD42 Publications
    Gene namesi
    Name:yihX
    Ordered Locus Names:b3885, JW5566
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11850. yihX.

    Pathology & Biotechi

    Biotechnological usei

    Is proposed to be a useful catalyst for hydrolytic transformation (e.g. removal) of alpha-Glc-1-P from complex substrate solutions containing multiple sugar phosphates.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000662651 – 199Alpha-D-glucose 1-phosphate phosphatase YihXAdd BLAST199

    Proteomic databases

    PaxDbiP0A8Y3.
    PRIDEiP0A8Y3.

    Interactioni

    Protein-protein interaction databases

    BioGridi4260964. 8 interactors.
    DIPiDIP-47896N.
    STRINGi511145.b3885.

    Structurei

    Secondary structure

    1199
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Turni8 – 10Combined sources3
    Beta strandi11 – 15Combined sources5
    Helixi17 – 27Combined sources11
    Helixi31 – 37Combined sources7
    Helixi42 – 48Combined sources7
    Helixi54 – 65Combined sources12
    Helixi71 – 79Combined sources9
    Beta strandi82 – 85Combined sources4
    Helixi87 – 98Combined sources12
    Beta strandi102 – 107Combined sources6
    Helixi118 – 120Combined sources3
    Helixi122 – 127Combined sources6
    Beta strandi129 – 133Combined sources5
    Helixi134 – 137Combined sources4
    Helixi144 – 154Combined sources11
    Helixi158 – 160Combined sources3
    Beta strandi161 – 166Combined sources6
    Helixi168 – 175Combined sources8
    Turni176 – 178Combined sources3
    Beta strandi180 – 183Combined sources4
    Helixi189 – 195Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B0CX-ray2.00A1-199[»]
    ProteinModelPortaliP0A8Y3.
    SMRiP0A8Y3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y3.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni6 – 8Substrate binding3
    Regioni107 – 108Substrate binding2

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EJU. Bacteria.
    COG1011. LUCA.
    HOGENOMiHOG000025211.
    InParanoidiP0A8Y3.
    KOiK07025.
    OMAiTQYPDVQ.
    PhylomeDBiP0A8Y3.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A8Y3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLYIFDLGNV IVDIDFNRVL GAWSDLTRIP LASLKKSFHM GEAFHQHERG
    60 70 80 90 100
    EISDEAFAEA LCHEMALPLS YEQFSHGWQA VFVALRPEVI AIMHKLREQG
    110 120 130 140 150
    HRVVVLSNTN RLHTTFWPEE YPEIRDAADH IYLSQDLGMR KPEARIYQHV
    160 170 180 190
    LQAEGFSPSD TVFFDDNADN IEGANQLGIT SILVKDKTTI PDYFAKVLC
    Length:199
    Mass (Da):22,732
    Last modified:June 21, 2005 - v1
    Checksum:i9451EA8917DFC0D2
    GO

    Sequence cautioni

    The sequence AAB03018 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03018.1. Different initiation.
    U00096 Genomic DNA. Translation: AAD13447.2.
    AP009048 Genomic DNA. Translation: BAE77424.1.
    PIRiS40829.
    RefSeqiNP_418321.4. NC_000913.3.
    WP_001295269.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAD13447; AAD13447; b3885.
    BAE77424; BAE77424; BAE77424.
    GeneIDi948380.
    KEGGiecj:JW5566.
    eco:b3885.
    PATRICi32123273. VBIEscCol129921_3997.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L19201 Genomic DNA. Translation: AAB03018.1. Different initiation.
    U00096 Genomic DNA. Translation: AAD13447.2.
    AP009048 Genomic DNA. Translation: BAE77424.1.
    PIRiS40829.
    RefSeqiNP_418321.4. NC_000913.3.
    WP_001295269.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B0CX-ray2.00A1-199[»]
    ProteinModelPortaliP0A8Y3.
    SMRiP0A8Y3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260964. 8 interactors.
    DIPiDIP-47896N.
    STRINGi511145.b3885.

    Proteomic databases

    PaxDbiP0A8Y3.
    PRIDEiP0A8Y3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD13447; AAD13447; b3885.
    BAE77424; BAE77424; BAE77424.
    GeneIDi948380.
    KEGGiecj:JW5566.
    eco:b3885.
    PATRICi32123273. VBIEscCol129921_3997.

    Organism-specific databases

    EchoBASEiEB1796.
    EcoGeneiEG11850. yihX.

    Phylogenomic databases

    eggNOGiENOG4105EJU. Bacteria.
    COG1011. LUCA.
    HOGENOMiHOG000025211.
    InParanoidiP0A8Y3.
    KOiK07025.
    OMAiTQYPDVQ.
    PhylomeDBiP0A8Y3.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11850-MONOMER.
    ECOL316407:JW5566-MONOMER.
    MetaCyc:EG11850-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y3.
    PROiP0A8Y3.

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01509. HAD-SF-IA-v3. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiYIHX_ECOLI
    AccessioniPrimary (citable) accession number: P0A8Y3
    Secondary accession number(s): P32145, Q2M8I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: June 21, 2005
    Last modified: November 2, 2016
    This is version 91 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.