N-acetyl-D-glucosamine kinase - Escherichia coli (strain K12)

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P75959 (NAGK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=342 µM for GlcNAc (at 37 degrees Celsius and pH 7.5) Ref.4 Ref.5 K_M=896 µM for ATP (at 37 degrees Celsius and pH 7.5) K_M=37 mM for glucose (at 37 degrees Celsius and pH 7.5) K_M=3.4 mM for ATP (at 25 degrees Celsius and pH 7.6) K_M=3.8 mM for glucose (at 25 degrees Celsius and pH 7.6) V_max=118 µmol/min/mg enzyme with GlcNAc as substrate (at 37 degrees Celsius and pH 7.5) V_max=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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: HAMAP peptidoglycan turnover Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from mutant phenotype Ref.4. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP N-acetylglucosamine kinase activity Inferred from direct assay Ref.4. Source: EcoCyc zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
zntR	P0ACS5	1	EBI-556240,EBI-562184

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 303

303

N-acetyl-D-glucosamine kinase HAMAP-Rule MF_01271

PRO_0000095720

Regions

Nucleotide binding

4 – 11

ATP Potential

Nucleotide binding

133 – 140

ATP Potential

Sites

Metal binding

157

Zinc By similarity

Metal binding

177

Zinc By similarity

Metal binding

179

Zinc By similarity

Metal binding

184

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P75959 [UniParc].

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

303

33,043

        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' referencesShow '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. 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 277:1453-1474(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.
PIR	D64856.
RefSeq	NP_415637.1. NC_000913.2. YP_489387.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P75959.
SMR	P75959. Positions 1-303.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-11548N.
IntAct	P75959. 10 interactions.
MINT	MINT-1274945.
STRING	511145.b1119.
Proteomic databases
PaxDb	P75959.
PRIDE	P75959.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74203; AAC74203; b1119. BAA35939; BAA35939; BAA35939.
GeneID	12931089. 945664.
KEGG	ecj:Y75_p1089. eco:b1119.
PATRIC	32117485. VBIEscCol129921_1165.
Organism-specific databases
EchoBASE	EB3216.
EcoGene	EG13442. nagK.
Phylogenomic databases
eggNOG	COG1940.
HOGENOM	HOG000150087.
KO	K00884.
OMA	FGHIRLP.
ProtClustDB	PRK13310.
Enzyme and pathway databases
BioCyc	EcoCyc:G6576-MONOMER. ECOL316407:JW1105-MONOMER. MetaCyc:G6576-MONOMER.
SABIO-RK	P75959.
UniPathway	UPA00544.
Gene expression databases
Genevestigator	P75959.
Family and domain databases
HAMAP	MF_01271. GlcNAc_kinase.
InterPro	IPR023505. N-acetyl-D-glucosamine_kinase. IPR000600. ROK. [Graphical view]
Pfam	PF00480. ROK. 1 hit. [Graphical view]
PROSITE	PS01125. ROK. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAGK_ECOLI

Accession

Primary (citable) accession number: P75959

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents