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P75959 (NAGK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyl-D-glucosamine kinase

EC=2.7.1.59
Alternative name(s):
GlcNAc kinase
Gene names
Name:nagK
Synonyms:ycfX
Ordered Locus Names:b1119, JW1105
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

Catalytic activity

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate. Ref.4

Enzyme regulation

Strongly inhibited by ADP. Ref.4

Pathway

Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_01271

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=342 µM for GlcNAc (at 37 degrees Celsius and pH 7.5) Ref.4 Ref.5

KM=896 µM for ATP (at 37 degrees Celsius and pH 7.5)

KM=37 mM for glucose (at 37 degrees Celsius and pH 7.5)

KM=3.4 mM for ATP (at 25 degrees Celsius and pH 7.6)

KM=3.8 mM for glucose (at 25 degrees Celsius and pH 7.6)

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

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

pH dependence:

Active from pH 6.5 to 10.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

zntRP0ACS51EBI-556240,EBI-562184

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303N-acetyl-D-glucosamine kinase HAMAP-Rule MF_01271
PRO_0000095720

Regions

Nucleotide binding4 – 118ATP Potential
Nucleotide binding133 – 1408ATP Potential

Sites

Metal binding1571Zinc By similarity
Metal binding1771Zinc By similarity
Metal binding1791Zinc By similarity
Metal binding1841Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
P75959 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: A857E63925894BBD

FASTA30333,043
        10         20         30         40         50         60 
MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DQRFGCKGSV 

        70         80         90        100        110        120 
GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT 

       130        140        150        160        170        180 
QYPLVMGLIL GTGVGGGLIF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG 

       190        200        210        220        230        240 
QHGCIENYLS GRGFAWLYQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI 

       250        260        270        280        290        300 
LTIVDPDLVV IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH 


LTD 

« Hide

References

« Hide 'large scale' references
[1]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC74203.1.
AP009048 Genomic DNA. Translation: BAA35939.1.
PIRD64856.
RefSeqNP_415637.1. NC_000913.3.
YP_489387.1. NC_007779.1.

3D structure databases

ProteinModelPortalP75959.
SMRP75959. Positions 1-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11548N.
IntActP75959. 10 interactions.
MINTMINT-1274945.
STRING511145.b1119.

Proteomic databases

PaxDbP75959.
PRIDEP75959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74203; AAC74203; b1119.
BAA35939; BAA35939; BAA35939.
GeneID12931089.
945664.
KEGGecj:Y75_p1089.
eco:b1119.
PATRIC32117485. VBIEscCol129921_1165.

Organism-specific databases

EchoBASEEB3216.
EcoGeneEG13442. nagK.

Phylogenomic databases

eggNOGCOG1940.
HOGENOMHOG000150087.
KOK00884.
OMARTAKVPP.
OrthoDBEOG61P6P0.
PhylomeDBP75959.

Enzyme and pathway databases

BioCycEcoCyc:G6576-MONOMER.
ECOL316407:JW1105-MONOMER.
MetaCyc:G6576-MONOMER.
SABIO-RKP75959.
UniPathwayUPA00544.

Gene expression databases

GenevestigatorP75959.

Family and domain databases

HAMAPMF_01271. GlcNAc_kinase.
InterProIPR023505. N-acetyl-D-glucosamine_kinase.
IPR000600. ROK.
[Graphical view]
PfamPF00480. ROK. 1 hit.
[Graphical view]
PROSITEPS01125. ROK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP75959.

Entry information

Entry nameNAGK_ECOLI
AccessionPrimary (citable) accession number: P75959
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 14, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene