ID NAGK_ECOLI Reviewed; 303 AA. AC P75959; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 151. DE RecName: Full=N-acetyl-D-glucosamine kinase; DE EC=2.7.1.59; DE AltName: Full=GlcNAc kinase; GN Name=nagK; Synonyms=ycfX; OrderedLocusNames=b1119, JW1105; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15489439; DOI=10.1128/jb.186.21.7273-7279.2004; RA Uehara T., Park J.T.; RT "The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in RT murein recycling."; RL J. Bacteriol. 186:7273-7279(2004). RN [5] RP IN VITRO FUNCTION, AND KINETIC PARAMETERS. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=15157072; DOI=10.1021/bi049424m; RA Miller B.G., Raines R.T.; RT "Identifying latent enzyme activities: substrate ambiguity within modern RT bacterial sugar kinases."; RL Biochemistry 43:6387-6392(2004). CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine CC (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Has CC also low level glucokinase activity in vitro. CC {ECO:0000269|PubMed:15489439}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D- CC glucosamine 6-phosphate; Xref=Rhea:RHEA:17417, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57513, ChEBI:CHEBI:456216, CC ChEBI:CHEBI:506227; EC=2.7.1.59; CC Evidence={ECO:0000269|PubMed:15489439}; CC -!- ACTIVITY REGULATION: Strongly inhibited by ADP. CC {ECO:0000269|PubMed:15489439}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=342 uM for GlcNAc (at 37 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:15489439}; CC KM=896 uM for ATP (at 37 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:15489439}; CC KM=37 mM for glucose (at 37 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:15489439}; CC KM=3.4 mM for ATP (at 25 degrees Celsius and pH 7.6) CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:15489439}; CC KM=3.8 mM for glucose (at 25 degrees Celsius and pH 7.6) CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:15489439}; CC Vmax=118 umol/min/mg enzyme with GlcNAc as substrate (at 37 degrees CC Celsius and pH 7.5) {ECO:0000269|PubMed:15157072, CC ECO:0000269|PubMed:15489439}; CC Vmax=24 umol/min/mg enzyme with glucose as substrate (at 37 degrees CC Celsius and pH 7.5) {ECO:0000269|PubMed:15157072, CC ECO:0000269|PubMed:15489439}; CC pH dependence: CC Active from pH 6.5 to 10. {ECO:0000269|PubMed:15489439}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling. CC -!- INTERACTION: CC P75959; P0ACS5: zntR; NbExp=2; IntAct=EBI-556240, EBI-562184; CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00096; AAC74203.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35939.1; -; Genomic_DNA. DR PIR; D64856; D64856. DR RefSeq; NP_415637.1; NC_000913.3. DR RefSeq; WP_000291270.1; NZ_STEB01000016.1. DR AlphaFoldDB; P75959; -. DR SMR; P75959; -. DR BioGRID; 4260083; 10. DR DIP; DIP-11548N; -. DR IntAct; P75959; 10. DR STRING; 511145.b1119; -. DR jPOST; P75959; -. DR PaxDb; 511145-b1119; -. DR EnsemblBacteria; AAC74203; AAC74203; b1119. DR GeneID; 75171243; -. DR GeneID; 945664; -. DR KEGG; ecj:JW1105; -. DR KEGG; eco:b1119; -. DR PATRIC; fig|1411691.4.peg.1148; -. DR EchoBASE; EB3216; -. DR eggNOG; COG1940; Bacteria. DR HOGENOM; CLU_036604_0_3_6; -. DR InParanoid; P75959; -. DR OMA; VNVPGWR; -. DR OrthoDB; 9810372at2; -. DR PhylomeDB; P75959; -. DR BioCyc; EcoCyc:G6576-MONOMER; -. DR BioCyc; MetaCyc:G6576-MONOMER; -. DR SABIO-RK; P75959; -. DR UniPathway; UPA00544; -. DR PRO; PR:P75959; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:EcoCyc. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_01271; GlcNAc_kinase; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR023505; N-acetyl-D-glucosamine_kinase. DR InterPro; IPR000600; ROK. DR PANTHER; PTHR18964:SF162; N-ACETYL-D-GLUCOSAMINE KINASE; 1. DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1. DR Pfam; PF00480; ROK; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. DR PROSITE; PS01125; ROK; 1. PE 1: Evidence at protein level; KW ATP-binding; Carbohydrate metabolism; Direct protein sequencing; Kinase; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..303 FT /note="N-acetyl-D-glucosamine kinase" FT /id="PRO_0000095720" FT BINDING 4..11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 133..140 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT BINDING 157 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 184 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 303 AA; 33043 MW; A857E63925894BBD CRC64; MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DQRFGCKGSV GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT QYPLVMGLIL GTGVGGGLIF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG QHGCIENYLS GRGFAWLYQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI LTIVDPDLVV IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH LTD //