ID   NAGK_YERPN              Reviewed;         256 AA.
AC   Q1CI48; C4GTW5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=N-acetyl-D-glucosamine kinase;
DE            EC=2.7.1.59;
DE   AltName: Full=GlcNAc kinase;
GN   Name=nagK; OrderedLocusNames=YPN_2003; ORFNames=YP516_2229;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine
CC       (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine + ATP = N-acetyl-D-glucosamine 6-
CC         phosphate + ADP + H(+); 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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- MISCELLANEOUS: Might be inactive, since the sequence is shorter than in
CC       other family members, due to a probable natural frameshift in the C-
CC       terminus.
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; CP000305; ABG18332.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000011; EEO76629.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1CI48; -.
DR   SMR; Q1CI48; -.
DR   KEGG; ypn:YPN_2003; -.
DR   HOGENOM; CLU_036604_0_3_6; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR   CDD; cd24057; ASKHA_NBD_ROK_NAGK; 1.
DR   FunFam; 3.30.420.40:FF:000049; N-acetyl-D-glucosamine kinase; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR049874; ROK_cs.
DR   NCBIfam; NF009835; PRK13310.1; 1.
DR   NCBIfam; NF009836; PRK13311.1; 1.
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   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..256
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_0000270126"
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   256 AA;  27879 MW;  0BCE117500ABD548 CRC64;
     MYYGFDMGGT KIELGVFDEN LQRIWHKRVP TPREDYPQLL QILRDLTEEA DTYCGVQGSV
     GIGIPGLPNA DDGTVFTANV PSAMGQPLQA DLSRLIQREV RIDNDANCFA LSEAWDPEFR
     TYPTVLGLIL GTGVGGGLIV NGSIVSGRNH ITGEFGHFRL PVDALDILGA DIPRVPCGCG
     HRGCIENYIS GRGFEWMYSH FYQHTLPATD IIAHYAAGEP KAVAHVERFM DVLAVCLGNL
     LTMLGSPFGR GGWGVV
//