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Q0TIV5 (NAGK_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:ECP_1113
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P By similarity. HAMAP-Rule MF_01271

Catalytic activity

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate. HAMAP-Rule MF_01271

Pathway

Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_01271

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303N-acetyl-D-glucosamine kinase HAMAP-Rule MF_01271
PRO_0000270102

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
Q0TIV5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 0757E639EB22510C

FASTA30333,085
        10         20         30         40         50         60 
MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DRRFGCKGSV 

        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 ITTQLAERLP RHLLPVARVP RIERARHGDA GGMRGAAFLH 


LTD 

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000247 Genomic DNA. Translation: ABG69124.1.
RefSeqYP_669025.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TIV5.
SMRQ0TIV5. Positions 1-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362663.ECP_1113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG69124; ABG69124; ECP_1113.
GeneID4190833.
KEGGecp:ECP_1113.
PATRIC18192949. VBIEscCol77757_1134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1940.
HOGENOMHOG000150087.
KOK00884.
OMAPEIVAQW.
OrthoDBEOG61P6P0.

Enzyme and pathway databases

BioCycECOL362663:GIY5-1120-MONOMER.
UniPathwayUPA00544.

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...

Entry information

Entry nameNAGK_ECOL5
AccessionPrimary (citable) accession number: Q0TIV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 52 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