ID   NAGK_YERPS              Reviewed;         304 AA.
AC   Q669P5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_01271};
DE            EC=2.7.1.59 {ECO:0000255|HAMAP-Rule:MF_01271};
DE   AltName: Full=GlcNAc kinase {ECO:0000255|HAMAP-Rule:MF_01271};
GN   Name=nagK {ECO:0000255|HAMAP-Rule:MF_01271}; OrderedLocusNames=YPTB2439;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine
CC       (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
CC       {ECO:0000255|HAMAP-Rule:MF_01271}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01271};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_01271}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01271}.
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DR   EMBL; BX936398; CAH21677.1; -; Genomic_DNA.
DR   RefSeq; WP_011192586.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q669P5; -.
DR   SMR; Q669P5; -.
DR   EnsemblBacteria; CAH21677; CAH21677; YPTB2439.
DR   GeneID; 66841130; -.
DR   KEGG; ypo:BZ17_11; -.
DR   KEGG; yps:YPTB2439; -.
DR   PATRIC; fig|273123.14.peg.12; -.
DR   OMA; VNVPGWR; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..304
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_0000270127"
FT   BINDING         4..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         133..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
SQ   SEQUENCE   304 AA;  33321 MW;  989779EDC67100BA 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
     LTMLDPHLVV VGGGLSNFEK IYQELPKRLP AHLLRVARLP RIEKARYGDS GGVRGAAFLH
     LAEK