NAGK_ECOLI
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 03-AUG-2022, entry version 144.
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; Proteobacteria; 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}.
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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; P75959; -.
DR PRIDE; P75959; -.
DR EnsemblBacteria; AAC74203; AAC74203; b1119.
DR EnsemblBacteria; BAA35939; BAA35939; BAA35939.
DR GeneID; 66670615; -.
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 PhylomeDB; P75959; -.
DR BioCyc; EcoCyc:G6576-MON; -.
DR BioCyc; MetaCyc:G6576-MON; -.
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; IBA:GO_Central.
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; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 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
