Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P27249 (GLND_ECOLI)

Entry version 180 (02 Dec 2020)
Sequence version 2 (01 Jun 1994)
Previous versions | rss
Add a publicationFeedback
Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

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

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.5 Publications

Miscellaneous

The transferase reaction proceeds by an ordered bi-bi kinetic mechanism, with PII binding before UTP and pyrophosphate (PPi) released before PII-UMP. The uridylyl-removing reaction proceeds with rapid equilibrium binding of substrate and random release of products (PubMed:9737855).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation1 PublicationNote: Mg2+ appears to be the physiologically relevant metal ion cofactor for both transferase and uridylyl-removing activities.UniRule annotation1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity. Both reactions are activated by ATP and 2-ketoglutarate, via the binding of these effector molecules to the substrates PII and PII-UMP.UniRule annotation4 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

kcat is 137 min(-1) for the UTase reaction. kcat is 2.7 min(-1) for the UR reaction in the absence of glutamine, and 6.5 min(-1) in the presence of 2.5 mM glutamine.
  1. KM=3.0 µM for GlnB protein1 Publication
  2. KM=40 µM for UTP1 Publication
  3. KM=2.3 µM for uridylyl-[protein-PII] (in the absence of glutamine)1 Publication
  4. KM=0.82 µM for uridylyl-[protein-PII] (in the presence of 2.5 mM glutamine)1 Publication

    <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 functionHydrolase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
    LigandMagnesium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:GLND-MONOMER
    MetaCyc:GLND-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.7.7.59, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P27249

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
    Short name:
    UTase/URUniRule annotation
    Alternative name(s):
    Bifunctional [protein-PII] modification enzymeUniRule annotation
    Bifunctional nitrogen sensor proteinUniRule annotation
    Including the following 2 domains:
    [Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
    Short name:
    PII uridylyltransferaseUniRule annotation
    Short name:
    UTaseUniRule annotation
    [Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
    Short name:
    URUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:glnDUniRule annotation
    Ordered Locus Names:b0167, JW0162
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi93G → L or V: Loss of UTase activity, while no significant effect on UR activity. 1 Publication1
    Mutagenesisi94G → D: Loss of UTase activity, while no significant effect on UR activity. 1 Publication1
    Mutagenesisi107D → A, V or Y: Loss of UTase activity, while no significant effect on UR activity. 1 Publication1
    Mutagenesisi514 – 515HD → AA or QN: Loss of UR activity, while no significant effect on UTase activity. 1 Publication2

    <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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001927321 – 890Bifunctional uridylyltransferase/uridylyl-removing enzymeAdd BLAST890

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P27249

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

    More...    PaxDbi    		P27249

    PRoteomics IDEntifications database

    More...    PRIDEi    		P27249

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer. Can also form homooligomers that are much less active.

    1 Publication

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4259747, 20 interactors
    849263, 3 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-9779N

    Protein interaction database and analysis system

    More...    IntActi    		P27249, 24 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0167

    <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

    3D structure databases

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

    More...    SMRi    		P27249

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini468 – 590HDPROSITE-ProRule annotationAdd BLAST123
    Domaini709 – 789ACT 1UniRule annotationAdd BLAST81
    Domaini816 – 890ACT 2UniRule annotationAdd BLAST75

    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>Regioni1 – 349UridylyltransferaseAdd BLAST349
    Regioni350 – 708Uridylyl-removingAdd BLAST359

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing.UniRule annotation1 Publication

    <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 GlnD family.UniRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG2844, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_012833_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P27249

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P27249

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00077, HDc, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00277, PII_uridylyl_transf, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR002912, ACT_dom
    IPR003607, HD/PDEase_dom
    IPR006674, HD_domain
    IPR043519, NT_sf
    IPR013546, PII_UdlTrfase/GS_AdlTrfase
    IPR002934, Polymerase_NTP_transf_dom
    IPR010043, UTase/UR

    The PANTHER Classification System

    More...    PANTHERi    		PTHR47320, PTHR47320, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01842, ACT, 2 hits
    PF08335, GlnD_UR_UTase, 1 hit
    PF01966, HD, 1 hit
    PF01909, NTP_transf_2, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF006288, PII_uridyltransf, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00471, HDc, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF81301, SSF81301, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01693, UTase_glnD, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51671, ACT, 2 hits
    PS51831, HD, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P27249-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNTLPEQYAN TALPTLPGQP QNPCVWPRDE LTVGGIKAHI DTFQRWLGDA 
            60         70         80         90        100
    FDNGISAEQL IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL 
           110        120        130        140        150
    HPLSDVDLLI LSRKKLPDDQ AQKVGELLTL LWDVKLEVGH SVRTLEECML 
           160        170        180        190        200
    EGLSDLTVAT NLIESRLLIG DVALFLELQK HIFSEGFWPS DKFYAAKVEE 
           210        220        230        240        250
    QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 
           260        270        280        290        300
    FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 
           310        320        330        340        350
    YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPI 
           360        370        380        390        400
    DDEFQLRGTL IDLRDETLFM RQPEAILRMF YTMVHNSAIT GIYSTTLRQL 
           410        420        430        440        450
    RHARRHLQQP LCNIPEARKL FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ 
           460        470        480        490        500
    WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFASEETRQR HPLCVDVWPR 
           510        520        530        540        550
    LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG LNSRETQLVA 
           560        570        580        590        600
    WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA 
           610        620        630        640        650
    TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 
           660        670        680        690        700
    RMDNIDEEAL HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS 
           710        720        730        740        750
    PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 
           760        770        780        790        800
    TFIVLEPDGN PLSADRHEVI RFGLEQVLTQ SSWQPPQPRR QPAKLRHFTV 
           810        820        830        840        850
    ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI SLHGARITTI 
           860        870        880        890
    GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG
    Length:890
    Mass (Da):102,390
    Last modified:June 1, 1994 - 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:i6FF0006341A71D34
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti47L → S in AAA23878 (Ref. 1) Curated1
    Sequence conflicti225G → A (PubMed:8202364).Curated1
    Sequence conflicti357 – 358RG → TR in AAA23878 (Ref. 1) Curated2
    Sequence conflicti523D → H in AAA23878 (Ref. 1) Curated1
    Sequence conflicti703A → R in CAA79887 (PubMed:8412694).Curated1

    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
    		M96431 Genomic DNA Translation: AAA23878.1
    Z21842 Genomic DNA Translation: CAA79887.1
    U70214 Genomic DNA Translation: AAB08596.1
    U00096 Genomic DNA Translation: AAC73278.1
    AP009048 Genomic DNA Translation: BAE76045.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		G64740

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414709.1, NC_000913.3
    WP_001094586.1, NZ_SSZK01000004.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73278; AAC73278; b0167
    BAE76045; BAE76045; BAE76045

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		944863

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0162
    eco:b0167

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2114

    <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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		M96431 Genomic DNA Translation: AAA23878.1
    Z21842 Genomic DNA Translation: CAA79887.1
    U70214 Genomic DNA Translation: AAB08596.1
    U00096 Genomic DNA Translation: AAC73278.1
    AP009048 Genomic DNA Translation: BAE76045.1
    PIRiG64740
    RefSeqiNP_414709.1, NC_000913.3
    WP_001094586.1, NZ_SSZK01000004.1

    3D structure databases

    SMRiP27249
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4259747, 20 interactors
    849263, 3 interactors
    DIPiDIP-9779N
    IntActiP27249, 24 interactors
    STRINGi511145.b0167

    Proteomic databases

    jPOSTiP27249
    PaxDbiP27249
    PRIDEiP27249

    Genome annotation databases

    EnsemblBacteriaiAAC73278; AAC73278; b0167
    BAE76045; BAE76045; BAE76045
    GeneIDi944863
    KEGGiecj:JW0162
    eco:b0167
    PATRICifig|1411691.4.peg.2114

    Organism-specific databases

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

    More...    EchoBASEi    		EB1383

    Phylogenomic databases

    eggNOGiCOG2844, Bacteria
    HOGENOMiCLU_012833_0_0_6
    InParanoidiP27249
    PhylomeDBiP27249

    Enzyme and pathway databases

    BioCyciEcoCyc:GLND-MONOMER
    MetaCyc:GLND-MONOMER
    BRENDAi2.7.7.59, 2026
    SABIO-RKiP27249

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P27249

    Family and domain databases

    CDDicd00077, HDc, 1 hit
    HAMAPiMF_00277, PII_uridylyl_transf, 1 hit
    InterProiView protein in InterPro
    IPR002912, ACT_dom
    IPR003607, HD/PDEase_dom
    IPR006674, HD_domain
    IPR043519, NT_sf
    IPR013546, PII_UdlTrfase/GS_AdlTrfase
    IPR002934, Polymerase_NTP_transf_dom
    IPR010043, UTase/UR
    PANTHERiPTHR47320, PTHR47320, 1 hit
    PfamiView protein in Pfam
    PF01842, ACT, 2 hits
    PF08335, GlnD_UR_UTase, 1 hit
    PF01966, HD, 1 hit
    PF01909, NTP_transf_2, 1 hit
    PIRSFiPIRSF006288, PII_uridyltransf, 1 hit
    SMARTiView protein in SMART
    SM00471, HDc, 1 hit
    SUPFAMiSSF81301, SSF81301, 1 hit
    TIGRFAMsiTIGR01693, UTase_glnD, 1 hit
    PROSITEiView protein in PROSITE
    PS51671, ACT, 2 hits
    PS51831, HD, 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 nameiGLND_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: P27249
    Secondary accession number(s): Q2MCG1
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: June 1, 1994
    Last modified: December 2, 2020
    This is version 180 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

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again