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P75959

- NAGK_ECOLI

UniProt

P75959 - NAGK_ECOLI

Protein

N-acetyl-D-glucosamine kinase

Gene

nagK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Has also low level glucokinase activity in vitro.1 Publication

    Catalytic activityi

    ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate.1 Publication

    Enzyme regulationi

    Strongly inhibited by ADP.1 Publication

    Kineticsi

    1. KM=342 µM for GlcNAc (at 37 degrees Celsius and pH 7.5)2 Publications
    2. KM=896 µM for ATP (at 37 degrees Celsius and pH 7.5)2 Publications
    3. KM=37 mM for glucose (at 37 degrees Celsius and pH 7.5)2 Publications
    4. KM=3.4 mM for ATP (at 25 degrees Celsius and pH 7.6)2 Publications
    5. KM=3.8 mM for glucose (at 25 degrees Celsius and pH 7.6)2 Publications

    Vmax=118 µmol/min/mg enzyme with GlcNAc as substrate (at 37 degrees Celsius and pH 7.5)2 Publications

    Vmax=24 µmol/min/mg enzyme with glucose as substrate (at 37 degrees Celsius and pH 7.5)2 Publications

    pH dependencei

    Active from pH 6.5 to 10.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi157 – 1571ZincBy similarity
    Metal bindingi177 – 1771ZincBy similarity
    Metal bindingi179 – 1791ZincBy similarity
    Metal bindingi184 – 1841ZincBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 118ATPSequence Analysis
    Nucleotide bindingi133 – 1408ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. N-acetylglucosamine kinase activity Source: EcoCyc
    3. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. N-acetylglucosamine metabolic process Source: UniProtKB-HAMAP
    3. peptidoglycan turnover Source: EcoCyc

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:G6576-MONOMER.
    ECOL316407:JW1105-MONOMER.
    MetaCyc:G6576-MONOMER.
    SABIO-RKP75959.
    UniPathwayiUPA00544.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-acetyl-D-glucosamine kinase (EC:2.7.1.59)
    Alternative name(s):
    GlcNAc kinase
    Gene namesi
    Name:nagK
    Synonyms:ycfX
    Ordered Locus Names:b1119, JW1105
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13442. nagK.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 303303N-acetyl-D-glucosamine kinasePRO_0000095720Add
    BLAST

    Proteomic databases

    PaxDbiP75959.
    PRIDEiP75959.

    Expressioni

    Gene expression databases

    GenevestigatoriP75959.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    zntRP0ACS51EBI-556240,EBI-562184

    Protein-protein interaction databases

    DIPiDIP-11548N.
    IntActiP75959. 10 interactions.
    MINTiMINT-1274945.
    STRINGi511145.b1119.

    Structurei

    3D structure databases

    ProteinModelPortaliP75959.
    SMRiP75959. Positions 1-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ROK (NagC/XylR) family. NagK subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG1940.
    HOGENOMiHOG000150087.
    KOiK00884.
    OMAiRTAKVPP.
    OrthoDBiEOG61P6P0.
    PhylomeDBiP75959.

    Family and domain databases

    HAMAPiMF_01271. GlcNAc_kinase.
    InterProiIPR023505. N-acetyl-D-glucosamine_kinase.
    IPR000600. ROK.
    [Graphical view]
    PfamiPF00480. ROK. 1 hit.
    [Graphical view]
    PROSITEiPS01125. ROK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P75959-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA    50
    DQRFGCKGSV GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV 100
    RLDNDANCFA LSEAWDDEFT QYPLVMGLIL GTGVGGGLIF NGKPITGKSY 150
    ITGEFGHMRL PVDALTMMGL DFPLRRCGCG QHGCIENYLS GRGFAWLYQH 200
    YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI LTIVDPDLVV 250
    IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH 300
    LTD 303
    Length:303
    Mass (Da):33,043
    Last modified:February 1, 1997 - v1
    Checksum:iA857E63925894BBD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74203.1.
    AP009048 Genomic DNA. Translation: BAA35939.1.
    PIRiD64856.
    RefSeqiNP_415637.1. NC_000913.3.
    YP_489387.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74203; AAC74203; b1119.
    BAA35939; BAA35939; BAA35939.
    GeneIDi12931089.
    945664.
    KEGGiecj:Y75_p1089.
    eco:b1119.
    PATRICi32117485. VBIEscCol129921_1165.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC74203.1 .
    AP009048 Genomic DNA. Translation: BAA35939.1 .
    PIRi D64856.
    RefSeqi NP_415637.1. NC_000913.3.
    YP_489387.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P75959.
    SMRi P75959. Positions 1-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11548N.
    IntActi P75959. 10 interactions.
    MINTi MINT-1274945.
    STRINGi 511145.b1119.

    Proteomic databases

    PaxDbi P75959.
    PRIDEi P75959.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74203 ; AAC74203 ; b1119 .
    BAA35939 ; BAA35939 ; BAA35939 .
    GeneIDi 12931089.
    945664.
    KEGGi ecj:Y75_p1089.
    eco:b1119.
    PATRICi 32117485. VBIEscCol129921_1165.

    Organism-specific databases

    EchoBASEi EB3216.
    EcoGenei EG13442. nagK.

    Phylogenomic databases

    eggNOGi COG1940.
    HOGENOMi HOG000150087.
    KOi K00884.
    OMAi RTAKVPP.
    OrthoDBi EOG61P6P0.
    PhylomeDBi P75959.

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    BioCyci EcoCyc:G6576-MONOMER.
    ECOL316407:JW1105-MONOMER.
    MetaCyc:G6576-MONOMER.
    SABIO-RK P75959.

    Miscellaneous databases

    PROi P75959.

    Gene expression databases

    Genevestigatori P75959.

    Family and domain databases

    HAMAPi MF_01271. GlcNAc_kinase.
    InterProi IPR023505. N-acetyl-D-glucosamine_kinase.
    IPR000600. ROK.
    [Graphical view ]
    Pfami PF00480. ROK. 1 hit.
    [Graphical view ]
    PROSITEi PS01125. ROK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling."
      Uehara T., Park J.T.
      J. Bacteriol. 186:7273-7279(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases."
      Miller B.G., Raines R.T.
      Biochemistry 43:6387-6392(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IN VITRO FUNCTION, KINETIC PARAMETERS.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

    Entry informationi

    Entry nameiNAGK_ECOLI
    AccessioniPrimary (citable) accession number: P75959
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3