Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A8Y5

- YIDA_ECOLI

UniProt

P0A8Y5 - YIDA_ECOLI

Protein

Sugar phosphatase YidA

Gene

yidA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (21 Jun 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the dephosphorylation of different sugar phosphates including erythrose-4-phosphate (Ery4P), ribose-5-phosphate (Ribu5P), fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), glucose-6-P (Glu6P), and also imidodiphosphate (Imido-di-P) and acetyl phosphate (Acetyl-P). Selectively hydrolyzes alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form.2 Publications

    Catalytic activityi

    Sugar phosphate + H2O = sugar + phosphate.1 Publication

    Cofactori

    Magnesium. Can also use other divalent metal cations as manganese, cobalt and zinc.1 Publication

    Kineticsi

    1. KM=0.019 mM for Ery4P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    2. KM=0.033 mM for Imido-di-P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    3. KM=0.21 mM for Glu1P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    4. KM=0.39 mM for Fru1P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    5. KM=0.44 mM for Fru6P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    6. KM=0.45 mM for Ribu5P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    7. KM=0.54 mM for Man1P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    8. KM=0.81 mM for Glu6P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication
    9. KM=3.8 mM for Acetyl-P (in the presence of magnesium ion as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is between 6 and 7.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei9 – 91Nucleophile1 Publication
    Metal bindingi9 – 91Magnesium
    Binding sitei10 – 101Phosphate; via amide nitrogenBy similarity
    Metal bindingi11 – 111Magnesium; via carbonyl oxygen
    Binding sitei197 – 1971PhosphateBy similarity
    Metal bindingi220 – 2201Magnesium
    Binding sitei223 – 2231PhosphateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: EcoliWiki
    2. phosphatase activity Source: EcoliWiki
    3. sugar-phosphatase activity Source: EcoliWiki

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. small molecule biosynthetic process Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11195-MONOMER.
    ECOL316407:JW3674-MONOMER.
    MetaCyc:EG11195-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sugar phosphatase YidA (EC:3.1.3.23)
    Gene namesi
    Name:yidA
    Ordered Locus Names:b3697, JW3674
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11195. yidA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91D → A: Loss of the phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 270270Sugar phosphatase YidAPRO_0000054423Add
    BLAST

    Proteomic databases

    PaxDbiP0A8Y5.
    PRIDEiP0A8Y5.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A8Y5.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-36033N.
    IntActiP0A8Y5. 10 interactions.
    MINTiMINT-1238706.
    STRINGi511145.b3697.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Helixi10 – 145
    Helixi23 – 3412
    Beta strandi38 – 425
    Helixi47 – 493
    Helixi51 – 566
    Beta strandi65 – 684
    Helixi69 – 713
    Beta strandi73 – 764
    Turni77 – 793
    Beta strandi82 – 854
    Helixi90 – 10314
    Beta strandi106 – 1105
    Beta strandi115 – 1173
    Helixi124 – 1329
    Beta strandi137 – 1393
    Helixi142 – 1443
    Beta strandi153 – 1575
    Helixi160 – 16910
    Helixi172 – 1776
    Beta strandi178 – 1847
    Beta strandi187 – 1926
    Helixi197 – 20812
    Helixi212 – 2143
    Beta strandi215 – 2195
    Helixi222 – 2243
    Helixi225 – 2306
    Beta strandi231 – 2366
    Helixi242 – 2476
    Beta strandi249 – 2513
    Turni255 – 2584
    Helixi259 – 2679

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RKQX-ray1.40A/B2-270[»]
    ProteinModelPortaliP0A8Y5.
    SMRiP0A8Y5. Positions 1-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A8Y5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 442Phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0561.
    HOGENOMiHOG000184780.
    KOiK07024.
    OMAiLGVHFHA.
    OrthoDBiEOG6K13W0.
    PhylomeDBiP0A8Y5.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR000150. Hypothet_cof.
    [Graphical view]
    PfamiPF00702. Hydrolase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR00099. Cof-subfamily. 1 hit.
    TIGR01484. HAD-SF-IIB. 1 hit.
    PROSITEiPS01228. COF_1. 1 hit.
    PS01229. COF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A8Y5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIKLIAIDM DGTLLLPDHT ISPAVKNAIA AARARGVNVV LTTGRPYAGV    50
    HNYLKELHME QPGDYCITYN GALVQKAADG STVAQTALSY DDYRFLEKLS 100
    REVGSHFHAL DRTTLYTANR DISYYTVHES FVATIPLVFC EAEKMDPNTQ 150
    FLKVMMIDEP AILDQAIARI PQEVKEKYTV LKSAPYFLEI LDKRVNKGTG 200
    VKSLADVLGI KPEEIMAIGD QENDIAMIEY AGVGVAMDNA IPSVKEVANF 250
    VTKSNLEDGV AFAIEKYVLN 270
    Length:270
    Mass (Da):29,721
    Last modified:June 21, 2005 - v1
    Checksum:i04E749788D8A9446
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10328 Genomic DNA. Translation: AAA62048.1.
    U00096 Genomic DNA. Translation: AAC76720.1.
    AP009048 Genomic DNA. Translation: BAE77597.1.
    X04341 Genomic DNA. Translation: CAA27873.1.
    PIRiB65172. QQECGB.
    RefSeqiNP_418152.1. NC_000913.3.
    YP_491738.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76720; AAC76720; b3697.
    BAE77597; BAE77597; BAE77597.
    GeneIDi12933583.
    948204.
    KEGGiecj:Y75_p3476.
    eco:b3697.
    PATRICi32122889. VBIEscCol129921_3820.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10328 Genomic DNA. Translation: AAA62048.1 .
    U00096 Genomic DNA. Translation: AAC76720.1 .
    AP009048 Genomic DNA. Translation: BAE77597.1 .
    X04341 Genomic DNA. Translation: CAA27873.1 .
    PIRi B65172. QQECGB.
    RefSeqi NP_418152.1. NC_000913.3.
    YP_491738.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RKQ X-ray 1.40 A/B 2-270 [» ]
    ProteinModelPortali P0A8Y5.
    SMRi P0A8Y5. Positions 1-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36033N.
    IntActi P0A8Y5. 10 interactions.
    MINTi MINT-1238706.
    STRINGi 511145.b3697.

    Proteomic databases

    PaxDbi P0A8Y5.
    PRIDEi P0A8Y5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76720 ; AAC76720 ; b3697 .
    BAE77597 ; BAE77597 ; BAE77597 .
    GeneIDi 12933583.
    948204.
    KEGGi ecj:Y75_p3476.
    eco:b3697.
    PATRICi 32122889. VBIEscCol129921_3820.

    Organism-specific databases

    EchoBASEi EB1181.
    EcoGenei EG11195. yidA.

    Phylogenomic databases

    eggNOGi COG0561.
    HOGENOMi HOG000184780.
    KOi K07024.
    OMAi LGVHFHA.
    OrthoDBi EOG6K13W0.
    PhylomeDBi P0A8Y5.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11195-MONOMER.
    ECOL316407:JW3674-MONOMER.
    MetaCyc:EG11195-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A8Y5.
    PROi P0A8Y5.

    Gene expression databases

    Genevestigatori P0A8Y5.

    Family and domain databases

    Gene3Di 3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR000150. Hypothet_cof.
    [Graphical view ]
    Pfami PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR00099. Cof-subfamily. 1 hit.
    TIGR01484. HAD-SF-IIB. 1 hit.
    PROSITEi PS01228. COF_1. 1 hit.
    PS01229. COF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(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. "DNA sequence of the E. coli gyrB gene: application of a new sequencing strategy."
      Adachi T., Mizuuchi M., Robinson E.A., Appella E., O'Dea M.H., Gellert M., Mizuuchi K.
      Nucleic Acids Res. 15:771-784(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-195.
    5. "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.
    6. "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 AS A PHOSPHATASE, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-9, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.
    7. "Crystal structure of NYSGRC target T1436: a hypothetical protein YidA."
      Ramagopal U.A., Almo S.C.
      Submitted (MAR-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-270 IN COMPLEX WITH MAGNESIUM IONS, SUBUNIT.

    Entry informationi

    Entry nameiYIDA_ECOLI
    AccessioniPrimary (citable) accession number: P0A8Y5
    Secondary accession number(s): P09997, P76737, Q2M809
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 80 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

    External Data

    Dasty 3