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P75959

- NAGK_ECOLI

UniProt

P75959 - NAGK_ECOLI

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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

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
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: 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.
InParanoidiP75959.
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 [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:
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.
InParanoidi P75959.
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

« 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: October 29, 2014
This is version 102 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