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

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

  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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei6 – 61Nucleophile
    Metal bindingi6 – 61MagnesiumBy similarity
    Binding sitei141 – 1411Substrate1 Publication
    Metal bindingi166 – 1661MagnesiumBy similarity
    Binding sitei166 – 1661Substrate1 Publication

    GO - Molecular functioni

    • glucose-1-phosphatase activity Source: EcoliWiki
    • magnesium ion binding Source: UniProtKB
    • manganese ion binding Source: UniProtKB

    GO - Biological processi

    • dephosphorylation Source: GOC
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Alpha-D-glucose 1-phosphate phosphatase YihXPRO_0000066265Add
    BLAST

    Proteomic databases

    PaxDbiP0A8Y3.
    PRIDEiP0A8Y3.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54Combined sources
    Turni8 – 103Combined sources
    Beta strandi11 – 155Combined sources
    Helixi17 – 2711Combined sources
    Helixi31 – 377Combined sources
    Helixi42 – 487Combined sources
    Helixi54 – 6512Combined sources
    Helixi71 – 799Combined sources
    Beta strandi82 – 854Combined sources
    Helixi87 – 9812Combined sources
    Beta strandi102 – 1076Combined sources
    Helixi118 – 1203Combined sources
    Helixi122 – 1276Combined sources
    Beta strandi129 – 1335Combined sources
    Helixi134 – 1374Combined sources
    Helixi144 – 15411Combined sources
    Helixi158 – 1603Combined sources
    Beta strandi161 – 1666Combined sources
    Helixi168 – 1758Combined sources
    Turni176 – 1783Combined sources
    Beta strandi180 – 1834Combined sources
    Helixi189 – 1957Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B0CX-ray2.00A1-199[»]
    ProteinModelPortaliP0A8Y3.
    SMRiP0A8Y3. Positions 1-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 83Substrate binding
    Regioni107 – 1082Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EJU. Bacteria.
    COG1011. LUCA.
    HOGENOMiHOG000025211.
    InParanoidiP0A8Y3.
    KOiK07025.
    OMAiTQYPDVQ.
    OrthoDBiEOG618QX2.
    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 AAB03018.1 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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B0CX-ray2.00A1-199[»]
    ProteinModelPortaliP0A8Y3.
    SMRiP0A8Y3. Positions 1-197.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260964. 8 interactions.
    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.
    OrthoDBiEOG618QX2.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Enzyme genomics: application of general enzymatic screens to discover new enzymes."
      Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.
      FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHATASE.
    5. "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family."
      Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.
      J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
    6. "Yihx-encoded haloacid dehalogenase-like phosphatase HAD4 from Escherichia coli is a specific alpha-d-glucose 1-phosphate hydrolase useful for substrate-selective sugar phosphate transformations."
      Pfeiffer M., Wildberger P., Nidetzky B.
      J. Mol. Catal., B Enzym. 110:39-46(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
    7. "The 2.0a crystal structure of the putative phosphatase from Escherichia coli."
      Midwest center for structural genomics (MCSG)
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.

    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: January 20, 2016
    This is version 87 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.