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UniProtKB - P0ACC7 (GLMU_ECOLI)

Entry version 134 (02 Dec 2020)
Sequence version 1 (08 Nov 2005)
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Protein

Bifunctional protein GlmU

Gene

glmU

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

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.UniRule annotation5 Publications

<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+1 Publication, Co2+1 PublicationNote: Binds 1 Mg2+ ion per subunit (PubMed:17473010). Can also use Co2+ ion to a lesser extent (PubMed:11329257).2 Publications

<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

Inhibited by its reaction product N-acetylglucosamine-1-phosphate and by UDP-N-acetylmuramic acid, which is one of the first precursors specific for the peptidoglycan pathway.3 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=0.018 mM for N-acetylglucosamine 1-phosphate3 Publications
  2. KM=0.07 mM for alpha-D-glucosamine 1-phosphate1 Publication
  3. KM=0.1 mM for UTP1 Publication
  4. KM=0.15 mM for alpha-D-glucosamine 1-phosphate3 Publications
  5. KM=0.25 mM for alpha-D-glucosamine 1-phosphate3 Publications
  6. KM=0.32 mM for acetyl-CoA3 Publications
  7. KM=0.6 mM for acetyl-CoA3 Publications
  8. KM=0.84 mM for n-propionyl-CoA3 Publications
  9. KM=1.3 mM for UDP-glucosamine3 Publications
  10. KM=2 mM for glucose-1-P3 Publications
  11. KM=3.7 mM for N-acetylgalactosamine-1-P3 Publications
  12. KM=15 mM for galactosamine-1-phosphate3 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Bifunctional protein GlmU (glmU), Bifunctional protein GlmU (glmU)
    This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional protein GlmU (glmU), Bifunctional protein GlmU (glmU)
    This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: LPS lipid A biosynthesis

    This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei25UDP-GlcNAcUniRule annotation1
    Binding sitei76UDP-GlcNAcUniRule annotation3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi105Magnesium or cobalt2 Publications1
    Binding sitei140UDP-GlcNAc; via amide nitrogenUniRule annotation3 Publications1
    Binding sitei154UDP-GlcNAcUniRule annotation3 Publications1
    Binding sitei169UDP-GlcNAcUniRule annotation3 Publications1
    Metal bindingi227Magnesium or cobalt2 Publications1
    Binding sitei227UDP-GlcNAcUniRule annotation1
    Binding sitei333UDP-GlcNAcUniRule annotation2 Publications1
    Binding sitei351UDP-GlcNAcUniRule annotation2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei363Proton acceptorUniRule annotation1
    Binding sitei366UDP-GlcNAcUniRule annotation2 Publications1
    Binding sitei377UDP-GlcNAcUniRule annotation3 Publications1
    Binding sitei380Acetyl-CoA; via amide nitrogenUniRule annotation2 Publications1
    Binding sitei405Acetyl-CoAUniRule annotation3 Publications1
    Binding sitei423Acetyl-CoA; via amide nitrogenUniRule annotation3 Publications1
    Binding sitei440Acetyl-CoAUniRule annotation3 Publications1

    <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 functionAcyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
    Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
    LigandCobalt, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:NAG1P-URIDYLTRANS-MONOMER
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.3.1.157, 2026
    2.7.7.23, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P0ACC7

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

    More...    UniPathwayi    		UPA00113;UER00532
    UPA00113;UER00533
    UPA00973

    <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 protein GlmUUniRule annotation
    Including the following 2 domains:
    UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation3 Publications)
    Alternative name(s):
    N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
    Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation3 Publications)
    <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:glmUUniRule annotation
    Synonyms:yieA
    Ordered Locus Names:b3730, JW3708
    <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 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 ...

    Keywords - Cellular componenti

    Cytoplasm

    <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>Mutagenesisi14G → A: 8-fold decrease in uridyltransferase activity. Creates steric conflict and decreases affinity for UTP. 1 Publication1
    Mutagenesisi18R → A: Dramatically impairs the uridyltransferase activity. 1 Publication1
    Mutagenesisi25K → A: 8-fold decrease in uridyltransferase activity. 1 Publication1
    Mutagenesisi296C → A: No effect. 1 Publication1
    Mutagenesisi307C → A: 1350-fold decrease in acetyltransferase activity. 1 Publication1
    Mutagenesisi324C → A: 8-fold decrease in acetyltransferase activity. 1 Publication1
    Mutagenesisi385C → A: No effect. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3414415

    Drug and drug target database

    More...    DrugBanki    		DB03814, 2-(N-morpholino)ethanesulfonic acid
    DB01992, Coenzyme A
    DB03397, Uridine-Diphosphate-N-Acetylglucosamine

    <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_00000687011 – 456Bifunctional protein GlmUAdd BLAST456

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0ACC7

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

    More...    PaxDbi    		P0ACC7

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0ACC7

    <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

    Homotrimer. In vivo forms a hexameric aggregate.

    5 Publications

    <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

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4262143, 312 interactors
    852548, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-31844N

    Protein interaction database and analysis system

    More...    IntActi    		P0ACC7, 19 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3730

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P0ACC7

    <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

    1456
    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    		P0ACC7

    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    		P0ACC7

    <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>Regioni1 – 229PyrophosphorylaseUniRule annotation2 PublicationsAdd BLAST229
    Regioni11 – 14UDP-GlcNAc bindingUniRule annotation3 Publications4
    Regioni81 – 82UDP-GlcNAc bindingUniRule annotation3 Publications2
    Regioni103 – 105UDP-GlcNAc bindingUniRule annotation3 Publications3
    Regioni230 – 250LinkerUniRule annotation2 PublicationsAdd BLAST21
    Regioni251 – 456N-acetyltransferaseUniRule annotation2 PublicationsAdd BLAST206
    Regioni386 – 387Acetyl-CoA bindingUniRule annotation2

    <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

    In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotationCurated
    In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotationCurated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1207, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_029499_15_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0ACC7

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0ACC7

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd03353, LbH_GlmU_C, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.90.550.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01631, GlmU, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR005882, Bifunctional_GlmU
    IPR038009, GlmU_C_LbH
    IPR001451, Hexapep
    IPR018357, Hexapep_transf_CS
    IPR025877, MobA-like_NTP_Trfase
    IPR029044, Nucleotide-diphossugar_trans
    IPR011004, Trimer_LpxA-like_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00132, Hexapep, 2 hits
    PF14602, Hexapep_2, 1 hit
    PF12804, NTP_transf_3, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51161, SSF51161, 1 hit
    SSF53448, SSF53448, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01173, glmU, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00101, HEXAPEP_TRANSFERASES, 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.

    P0ACC7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH 
            60         70         80         90        100
    VHLVYGHGGD LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL 
           110        120        130        140        150
    MLYGDVPLIS VETLQRLRDA KPQGGIGLLT VKLDDPTGYG RITRENGKVT 
           160        170        180        190        200
    GIVEHKDATD EQRQIQEINT GILIANGADM KRWLAKLTNN NAQGEYYITD 
           210        220        230        240        250
    IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ SEQAEKLLLA 
           260        270        280        290        300
    GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN 
           310        320        330        340        350
    SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM 
           360        370        380        390        400
    KKARLGKGSK AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD 
           410        420        430        440        450
    VFVGSDTQLV APVTVGKGAT IAAGTTVTRN VGENALAISR VPQTQKEGWR 

    RPVKKK
    Length:456
    Mass (Da):49,190
    Last modified:November 8, 2005 - v1
    <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:i2F3C5C84F673C8A3
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA62081 differs from that shown. Reason: Frameshift. Produces two ORFs.Curated
    The sequence AAA62082 differs from that shown. Reason: Frameshift. Produces two ORFs.Curated

    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 conflicti186 – 187KL → NV in CAA25784 (PubMed:6395859).Curated2

    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
    		X01631 Genomic DNA Translation: CAA25784.1
    L10328 Genomic DNA Translation: AAA62082.1 Frameshift.
    L10328 Genomic DNA Translation: AAA62081.1 Frameshift.
    U00096 Genomic DNA Translation: AAC76753.1
    AP009048 Genomic DNA Translation: BAE77558.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		C65176

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418186.1, NC_000913.3
    WP_000933736.1, NZ_STEB01000015.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC76753; AAC76753; b3730
    BAE77558; BAE77558; BAE77558

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948246

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW3708
    eco:b3730

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2970

    <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
    		X01631 Genomic DNA Translation: CAA25784.1
    L10328 Genomic DNA Translation: AAA62082.1 Frameshift.
    L10328 Genomic DNA Translation: AAA62081.1 Frameshift.
    U00096 Genomic DNA Translation: AAC76753.1
    AP009048 Genomic DNA Translation: BAE77558.1
    PIRiC65176
    RefSeqiNP_418186.1, NC_000913.3
    WP_000933736.1, NZ_STEB01000015.1

    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
    1FWYX-ray2.30A/B1-331[»]
    1FXJX-ray2.25A/B1-331[»]
    1HV9X-ray2.10A/B1-456[»]
    2OI5X-ray2.25A/B1-456[»]
    2OI6X-ray2.20A/B1-456[»]
    2OI7X-ray2.54A/B1-456[»]
    3TWDX-ray1.90A/B233-452[»]
    4AA7X-ray2.00A/B227-456[»]
    SMRiP0ACC7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4262143, 312 interactors
    852548, 1 interactor
    DIPiDIP-31844N
    IntActiP0ACC7, 19 interactors
    STRINGi511145.b3730

    Chemistry databases

    BindingDBiP0ACC7
    ChEMBLiCHEMBL3414415
    DrugBankiDB03814, 2-(N-morpholino)ethanesulfonic acid
    DB01992, Coenzyme A
    DB03397, Uridine-Diphosphate-N-Acetylglucosamine

    Proteomic databases

    jPOSTiP0ACC7
    PaxDbiP0ACC7
    PRIDEiP0ACC7

    Genome annotation databases

    EnsemblBacteriaiAAC76753; AAC76753; b3730
    BAE77558; BAE77558; BAE77558
    GeneIDi948246
    KEGGiecj:JW3708
    eco:b3730
    PATRICifig|1411691.4.peg.2970

    Organism-specific databases

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

    More...    EchoBASEi    		EB1184

    Phylogenomic databases

    eggNOGiCOG1207, Bacteria
    HOGENOMiCLU_029499_15_2_6
    InParanoidiP0ACC7
    PhylomeDBiP0ACC7

    Enzyme and pathway databases

    UniPathwayiUPA00113;UER00532
    UPA00113;UER00533
    UPA00973
    BioCyciEcoCyc:NAG1P-URIDYLTRANS-MONOMER
    MetaCyc:NAG1P-URIDYLTRANS-MONOMER
    BRENDAi2.3.1.157, 2026
    2.7.7.23, 2026
    SABIO-RKiP0ACC7

    Miscellaneous databases

    EvolutionaryTraceiP0ACC7

    Protein Ontology

    More...    PROi    		PR:P0ACC7

    Family and domain databases

    CDDicd03353, LbH_GlmU_C, 1 hit
    Gene3Di3.90.550.10, 1 hit
    HAMAPiMF_01631, GlmU, 1 hit
    InterProiView protein in InterPro
    IPR005882, Bifunctional_GlmU
    IPR038009, GlmU_C_LbH
    IPR001451, Hexapep
    IPR018357, Hexapep_transf_CS
    IPR025877, MobA-like_NTP_Trfase
    IPR029044, Nucleotide-diphossugar_trans
    IPR011004, Trimer_LpxA-like_sf
    PfamiView protein in Pfam
    PF00132, Hexapep, 2 hits
    PF14602, Hexapep_2, 1 hit
    PF12804, NTP_transf_3, 1 hit
    SUPFAMiSSF51161, SSF51161, 1 hit
    SSF53448, SSF53448, 1 hit
    TIGRFAMsiTIGR01173, glmU, 1 hit
    PROSITEiView protein in PROSITE
    PS00101, HEXAPEP_TRANSFERASES, 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 nameiGLMU_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: P0ACC7
    Secondary accession number(s): P17114, P76746, Q2M848
    <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: November 8, 2005
    Last sequence update: November 8, 2005
    Last modified: December 2, 2020
    This is version 134 of the entry and version 1 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, 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
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