ID   NAGK_PASMU              Reviewed;         304 AA.
AC   Q9CMX5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=PM0675;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02759.1; -; Genomic_DNA.
DR   RefSeq; WP_005726560.1; NC_002663.1.
DR   AlphaFoldDB; Q9CMX5; -.
DR   SMR; Q9CMX5; -.
DR   STRING; 747.DR93_1507; -.
DR   EnsemblBacteria; AAK02759; AAK02759; PM0675.
DR   KEGG; pmu:PM0675; -.
DR   HOGENOM; CLU_036604_0_3_6; -.
DR   OMA; VNVPGWR; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000809; 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; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..304
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_0000270109"
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         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
SQ   SEQUENCE   304 AA;  33039 MW;  9E6A87AF91ABF786 CRC64;
     MRYGFDIGGT KIELAVFNDQ LEKQYSERVE TPKESYEEWL NTIVRLVHKA DEMFQCQGTV
     GLGIPGFVNP ATGIAEIVNI RAADHKPIIQ DLETRLGREV RAENDANCFA LSEAWDEENA
     QYPSVLGLIL GTGFGGGLIF NGKVHSGQTG MAGEVGHTQL NYHALRLLGG DNAPIYDCGC
     GNRACLDTYL SGRGFEMLYR DMQGEALSAQ AIIQRFYAGD QSAVKFVELF IELCAISIGN
     LITVLDPHVI VLGGGLSNFD YLYEALPKAL PARLLRSANV PLIKKAKYGD SGGVRGAAAL
     FLSK