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Protein

N-acetyl-D-glucosamine kinase

Gene

nagK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Pathway: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

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

  • ATP binding Source: UniProtKB-HAMAP
  • N-acetylglucosamine kinase activity Source: EcoCyc
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: 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.

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.
InParanoidiP75959.
KOiK00884.
OMAiAYEPEVI.
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

        10         20         30         40         50
MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA
60 70 80 90 100
DQRFGCKGSV GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV
110 120 130 140 150
RLDNDANCFA LSEAWDDEFT QYPLVMGLIL GTGVGGGLIF NGKPITGKSY
160 170 180 190 200
ITGEFGHMRL PVDALTMMGL DFPLRRCGCG QHGCIENYLS GRGFAWLYQH
210 220 230 240 250
YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI LTIVDPDLVV
260 270 280 290 300
IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH

LTD
Length:303
Mass (Da):33,043
Last modified:February 1, 1997 - v1
Checksum:iA857E63925894BBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74203.1.
AP009048 Genomic DNA. Translation: BAA35939.1.
PIRiD64856.
RefSeqiNP_415637.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74203; AAC74203; b1119.
BAA35939; BAA35939; BAA35939.
GeneIDi945664.
KEGGiecj:Y75_p1089.
eco:b1119.
PATRICi32117485. VBIEscCol129921_1165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74203.1.
AP009048 Genomic DNA. Translation: BAA35939.1.
PIRiD64856.
RefSeqiNP_415637.1. NC_000913.3.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP75959.
PRIDEiP75959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74203; AAC74203; b1119.
BAA35939; BAA35939; BAA35939.
GeneIDi945664.
KEGGiecj:Y75_p1089.
eco:b1119.
PATRICi32117485. VBIEscCol129921_1165.

Organism-specific databases

EchoBASEiEB3216.
EcoGeneiEG13442. nagK.

Phylogenomic databases

eggNOGiCOG1940.
HOGENOMiHOG000150087.
InParanoidiP75959.
KOiK00884.
OMAiAYEPEVI.
OrthoDBiEOG61P6P0.
PhylomeDBiP75959.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP75959.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.