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Protein Overview: KGUA_ECOLI

General Information:
Name(s) found: KGUA_ECOLI [Swiss-Prot]
Description(s) found:
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  • gi|75766289|pdb|2ANC|F Chain F, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766288|pdb|2ANC|E Chain E, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766287|pdb|2ANC|D Chain D, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766286|pdb|2ANC|C Chain C, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766285|pdb|2ANC|B Chain B, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766284|pdb|2ANC|A Chain A, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [NCBI NR]
  • gi|75766283|pdb|2ANB|A Chain A, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gmp [NCBI NR]
  • gi|75766282|pdb|2AN9|B Chain B, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gdp [NCBI NR]
  • gi|75766281|pdb|2AN9|A Chain A, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gdp [NCBI NR]
  • gi|48474290|sp|P60546.1|KGUA_ECOLI RecName: Full=Guanylate kinase; AltName: Full=GMP kinase [NCBI NR]
  • gi|290498|gb|AAA62001.1| 5'guanylate kinase [NCBI NR]
  • pir||KIECGU guanylate kinase (EC 2.7.4.8) - Escherichia coli (strain K-12) [NCBI NR]
  • gi|146230|gb|AAB88711.1| GMP kinase [Escherichia coli] [NCBI NR]
  • gi|109157551|pdb|2F3T|F Chain F, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157550|pdb|2F3T|E Chain E, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157549|pdb|2F3T|D Chain D, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157548|pdb|2F3T|C Chain C, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157547|pdb|2F3T|B Chain B, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157546|pdb|2F3T|A Chain A, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [NCBI NR]
  • gi|109157544|pdb|2F3R|B Chain B, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ap5g [NCBI NR]
  • gi|109157543|pdb|2F3R|A Chain A, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ap5g [NCBI NR]
  • Guanylate kinase (EC 2.7.4.8) (GMP kinase) - Escherichia coli [Swiss-Prot]
  • guanylate kinase [Escherichia coli K12]gi|30065076|ref|NP_839247.1| guanylate kinase [Shigella flexneri 2a str. 2457T]gi|30043337|gb|AAP19058.1| guanylate kinase [Shigella flexneri 2a str. 2457T]gi|1790080|gb|AAC76672.1| guanylate kinase [Escherichia c [nrdb_11152004_Chlamydomonas]
  • Guanylate kinase (GMP kinase) [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • 5'guanylate kinase [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • Chain E, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain F, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain D, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain C, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain C, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain F, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gmp [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ganciclovir Monophosphate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ap5g [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of E.Coli Guanylate Kinase In Complex With Ap5g [nr-271106-contam.fasta]
  • GMP kinase [Escherichia coli] [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gdp [nr-271106-contam.fasta]
  • Chain E, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain D, Crystal Structure Of Unliganded Form Of Oligomeric E.Coli Guanylate Kinase [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of Oligomeric E.Coli Guanylate Kinase In Complex With Gdp [nr-271106-contam.fasta]
  • Guanylate kinase OS=Escherichia coli (strain K12) GN=gmk PE=1 SV=1 [uniprot-Ecoli-reviewed-110511.fasta]
    • Organism: Escherichia coli
    Length: 207 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MAQGTLYIVS APSGAGKSSL IQALLKTQPL YDTQVSVSHT TRQPRPGEVH GEHYFFVNHD  60
   61 EFKEMISRDA FLEHAEVFGN YYGTSREAIE QVLATGVDVF LDIDWQGAQQ IRQKMPHARS 120
  121 IFILPPSKIE LDRRLRGRGQ DSEEVIAKRM AQAVAEMSHY AEYDYLIVND DFDTALTDLK 180
  181 TIIRAERLRM SRQKQRHDAL ISKLLAD

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..207] PSI-BLAST 53.30103 The 2.0 A X-ray structure of Guanylate Kinase from E.coli

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • nucleobase, nucleoside, nucleotide kinase activity
    		•  3.66392587433723 bayes_pls_golite062009
  • hydrogen ion transporting ATP synthase activity, rotational mechanism
    		•  3.47528445676761 bayes_pls_golite062009
  • hydrogen ion transmembrane transporter activity
    		•  2.55741461337855 bayes_pls_golite062009
  • substrate-specific transporter activity
    		•  2.54103332067513 bayes_pls_golite062009
  • binding
    		•  2.44689197844883 bayes_pls_golite062009
  • monovalent inorganic cation transmembrane transporter activity
    		•  2.40650518173039 bayes_pls_golite062009
  • nucleotide kinase activity
    		•  2.24094813695083 bayes_pls_golite062009
  • phosphotransferase activity, phosphate group as acceptor
    		•  1.96697952975573 bayes_pls_golite062009
  • substrate-specific transmembrane transporter activity
    		•  1.92480060698169 bayes_pls_golite062009
  • ion transmembrane transporter activity
    		•  1.69194088788064 bayes_pls_golite062009
  • inorganic cation transmembrane transporter activity
    		•  1.60317778681063 bayes_pls_golite062009
  • cation transmembrane transporter activity
    		•  1.48327844851166 bayes_pls_golite062009
  • nucleic acid binding
    		•  1.08697924060619 bayes_pls_golite062009
  • catalytic activity
    		•  1.00104173493322 bayes_pls_golite062009
  • DNA binding
    		•  0.702147676354075 bayes_pls_golite062009
  • adenylate kinase activity
    		•  0.447752711852745 bayes_pls_golite062009
  • transcription regulator activity
    		•  0.287777990975748 bayes_pls_golite062009
  • helicase activity
    		•  0.0775311459068899 bayes_pls_golite062009
  • protein binding
    		•  0.071010918255742 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.79

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle