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UniProtKB - P0A6F3 (GLPK_ECOLI)

Entry version 125 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Glycerol kinase

Gene

glpK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP.UniRule annotation3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity of this regulatory enzyme is affected by several metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) causes alterations in the quaternary structure of the enzyme. FBP inhibition requires that the enzyme exist only in a tetrameric state. Salt such as KCl reduces the affinity of the tetrameric form of the enzyme for FBP. Unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system, also inhibits non-competitively and allostericaly the activity. Unlike FBP, both the dimer and the tetramer appear to be fully sensitive to enzyme EIIA-Glc inhibition. Zn(+2) greatly enhances the inhibitory potency of EIIA-Glc. Both allosteric regulatory agents is strongly pH dependent, with maximal inhibition occurring at pH 6.5.8 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.3 µM for glycerol4 Publications
  2. KM=400 µM for D-glyceraldehyde4 Publications
  3. KM=500 µM for dihydroxyacetone4 Publications
  4. KM=3 mM for L-glyceraldehyde4 Publications
  5. KM=4 mM for ATP4 Publications

    pH dependencei

    Optimum pH is 9.8.4 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycerol degradation via glycerol kinase pathway

    This protein is involved in step 1 of the subpathway that synthesizes sn-glycerol 3-phosphate from glycerol.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Glycerol kinase (glpK), Glycerol kinase (glpK), Glycerol kinase (glpK)
    This subpathway is part of the pathway glycerol degradation via glycerol kinase pathway, which is itself part of Polyol metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes sn-glycerol 3-phosphate from glycerol, the pathway glycerol degradation via glycerol kinase pathway and in Polyol metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei14SubstrateUniRule annotation1 Publication1
    Binding sitei18ATP1
    Binding sitei136SubstrateUniRule annotation1 Publication1
    Binding sitei268ATP1
    Binding sitei311ATP; via carbonyl oxygen1
    Binding sitei315ATP; via amide nitrogen1
    Binding sitei330ATP1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi479Zinc; shared with EIIA-Glc1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi14 – 16ATP3
    Nucleotide bindingi412 – 416ATP5

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAllosteric enzyme, Kinase, Transferase
    Biological processGlycerol metabolism
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:GLYCEROL-KIN-MONOMER
    ECOL316407:JW3897-MONOMER
    MetaCyc:GLYCEROL-KIN-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.1.30 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00618;UER00672

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...    SwissLipidsi    		SLP:000001805

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Glycerol kinaseUniRule annotation (EC:2.7.1.30UniRule annotation)
    Alternative name(s):
    ATP:glycerol 3-phosphotransferaseUniRule annotation
    GlycerokinaseUniRule annotation
    Short name:
    GKUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:glpKUniRule annotation
    Ordered Locus Names:b3926, JW3897
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59S → W: Abolishes inhibition of GK by FBP via disruption of the dimer-tetramer assembly reaction. Inhibition by EIIA-Glc is unchanged compared to wild type. The activity of this mutant is significantly higher than wild-type, and the Michaelis constants are increased slightly compared to wild-type. 1 Publication1
    Mutagenesisi66A → T: Although it completely abolishes FBP regulation and disruptes dimer-tetramer equilibrium, the crystal structure is essentially identical to the symmetric tetramer found in the FBP-bound form of the enzyme. 1 Publication1
    Mutagenesisi231G → D: Displays an increased enzymatic activity and a decreased allosteric regulation by FBP compared to wild-type. It displays a dimer form and is resistant to tetramer formation in the presence of FBP, whereas wild-type dimers are converted into inactive tetramers in the presence of FBP. 1 Publication1
    Mutagenesisi237R → A: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association. 1 Publication1
    Mutagenesisi305G → S in glpK22; abolishes glucose control of glycerol utilization. 1
    Mutagenesisi475I → D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. It increases the affinity for FBP about fivefold. 1 Publication1
    Mutagenesisi480R → D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. Regulation by FBP is not affected by this substitution. No inhibition by EIIA-Glc is observed, which is consistent with a decrease in affinity for EIIA-Glc of about 250-fold. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB04551 beta-D-fructofuranose 1,6-bisphosphate
    DB02937 Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000594512 – 502Glycerol kinaseAdd BLAST501

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei233N6-malonyllysine1 Publication1

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P0A6F3

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A6F3

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P0A6F3

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A6F3

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P0A6F3

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By L-alpha-glycerol 3-phosphate.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc (crr). Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.

    UniRule annotation9 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-548038,EBI-548038

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4263162, 380 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-36011N

    Protein interaction database and analysis system

    More...    IntActi    		P0A6F3, 15 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3926

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1502
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P0A6F3

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P0A6F3

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni84 – 85Substrate binding2
    Regioni234 – 236Allosteric FBP inhibitor binding3
    Regioni246 – 247Substrate binding2

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the FGGY kinase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4107QVN Bacteria
    COG0554 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000222134

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A6F3

    KEGG Orthology (KO)

    More...    KOi    		K00864

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A6F3

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_00186 Glycerol_kin, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR000577 Carb_kinase_FGGY
    IPR018485 Carb_kinase_FGGY_C
    IPR018483 Carb_kinase_FGGY_CS
    IPR018484 Carb_kinase_FGGY_N
    IPR005999 Glycerol_kin

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02782 FGGY_C, 1 hit
    PF00370 FGGY_N, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000538 GlpK, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01311 glycerol_kin, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00933 FGGY_KINASES_1, 1 hit
    PS00445 FGGY_KINASES_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A6F3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTEKKYIVAL DQGTTSSRAV VMDHDANIIS VSQREFEQIY PKPGWVEHDP 
            60         70         80         90        100
    MEIWATQSST LVEVLAKADI SSDQIAAIGI TNQRETTIVW EKETGKPIYN 
           110        120        130        140        150
    AIVWQCRRTA EICEHLKRDG LEDYIRSNTG LVIDPYFSGT KVKWILDHVE 
           160        170        180        190        200
    GSRERARRGE LLFGTVDTWL IWKMTQGRVH VTDYTNASRT MLFNIHTLDW 
           210        220        230        240        250
    DDKMLEVLDI PREMLPEVRR SSEVYGQTNI GGKGGTRIPI SGIAGDQQAA 
           260        270        280        290        300
    LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPTGEVN 
           310        320        330        340        350
    YALEGAVFMA GASIQWLRDE MKLINDAYDS EYFATKVQNT NGVYVVPAFT 
           360        370        380        390        400
    GLGAPYWDPY ARGAIFGLTR GVNANHIIRA TLESIAYQTR DVLEAMQADS 
           410        420        430        440        450
    GIRLHALRVD GGAVANNFLM QFQSDILGTR VERPEVREVT ALGAAYLAGL 
           460        470        480        490        500
    AVGFWQNLDE LQEKAVIERE FRPGIETTER NYRYAGWKKA VKRAMAWEEH 

    DE
    Length:502
    Mass (Da):56,231
    Last modified:January 23, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i854B61EA4648AB80
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		M18393 Genomic DNA Translation: AAA23913.1
    M55990 Genomic DNA Translation: AAA23887.1
    L19201 Genomic DNA Translation: AAB03058.1
    U00096 Genomic DNA Translation: AAC76908.1
    AP009048 Genomic DNA Translation: BAE77384.1
    X15054 Genomic DNA Translation: CAA33154.1
    U41468 Genomic DNA Translation: AAB60196.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A27339 KIECGL

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418361.1, NC_000913.3
    WP_000136788.1, NZ_SSZK01000014.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76908; AAC76908; b3926
    BAE77384; BAE77384; BAE77384

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948423

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW3897
    eco:b3926

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2779

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		M18393 Genomic DNA Translation: AAA23913.1
    M55990 Genomic DNA Translation: AAA23887.1
    L19201 Genomic DNA Translation: AAB03058.1
    U00096 Genomic DNA Translation: AAC76908.1
    AP009048 Genomic DNA Translation: BAE77384.1
    X15054 Genomic DNA Translation: CAA33154.1
    U41468 Genomic DNA Translation: AAB60196.1
    PIRiA27339 KIECGL
    RefSeqiNP_418361.1, NC_000913.3
    WP_000136788.1, NZ_SSZK01000014.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BO5X-ray3.20O/Z2-502[»]
    1BOTX-ray3.05O/Z2-502[»]
    1BU6X-ray2.37O/X/Y/Z2-502[»]
    1BWFX-ray3.00O/Y2-502[»]
    1GLAX-ray2.60G2-502[»]
    1GLBX-ray2.60G2-502[»]
    1GLCX-ray2.65G2-502[»]
    1GLDX-ray2.93G2-502[»]
    1GLEX-ray2.94G2-502[»]
    1GLFX-ray2.62O/X/Y/Z2-502[»]
    1GLJX-ray3.00O/Y2-502[»]
    1GLLX-ray3.00O/Y2-502[»]
    3EZWX-ray2.00A/B/C/D/E/F/G/H2-501[»]
    SMRiP0A6F3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4263162, 380 interactors
    DIPiDIP-36011N
    IntActiP0A6F3, 15 interactors
    STRINGi511145.b3926

    Chemistry databases

    DrugBankiDB04551 beta-D-fructofuranose 1,6-bisphosphate
    DB02937 Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-Diphosphate
    SwissLipidsiSLP:000001805

    2D gel databases

    SWISS-2DPAGEiP0A6F3

    Proteomic databases

    EPDiP0A6F3
    jPOSTiP0A6F3
    PaxDbiP0A6F3
    PRIDEiP0A6F3

    Genome annotation databases

    EnsemblBacteriaiAAC76908; AAC76908; b3926
    BAE77384; BAE77384; BAE77384
    GeneIDi948423
    KEGGiecj:JW3897
    eco:b3926
    PATRICifig|1411691.4.peg.2779

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...    EchoBASEi    		EB0393

    Phylogenomic databases

    eggNOGiENOG4107QVN Bacteria
    COG0554 LUCA
    HOGENOMiHOG000222134
    InParanoidiP0A6F3
    KOiK00864
    PhylomeDBiP0A6F3

    Enzyme and pathway databases

    UniPathwayiUPA00618;UER00672
    BioCyciEcoCyc:GLYCEROL-KIN-MONOMER
    ECOL316407:JW3897-MONOMER
    MetaCyc:GLYCEROL-KIN-MONOMER
    BRENDAi2.7.1.30 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A6F3

    Protein Ontology

    More...    PROi    		PR:P0A6F3

    Family and domain databases

    HAMAPiMF_00186 Glycerol_kin, 1 hit
    InterProiView protein in InterPro
    IPR000577 Carb_kinase_FGGY
    IPR018485 Carb_kinase_FGGY_C
    IPR018483 Carb_kinase_FGGY_CS
    IPR018484 Carb_kinase_FGGY_N
    IPR005999 Glycerol_kin
    PfamiView protein in Pfam
    PF02782 FGGY_C, 1 hit
    PF00370 FGGY_N, 1 hit
    PIRSFiPIRSF000538 GlpK, 1 hit
    TIGRFAMsiTIGR01311 glycerol_kin, 1 hit
    PROSITEiView protein in PROSITE
    PS00933 FGGY_KINASES_1, 1 hit
    PS00445 FGGY_KINASES_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLPK_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A6F3
    Secondary accession number(s): P08859, Q2M8M2, Q59381
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: January 23, 2007
    Last modified: December 11, 2019
    This is version 125 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
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