NAGK_SALG2
ID NAGK_SALG2 Reviewed; 303 AA.
AC B5RB82;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=SG1901;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933173; CAR37753.1; -; Genomic_DNA.
DR RefSeq; WP_000291336.1; NC_011274.1.
DR AlphaFoldDB; B5RB82; -.
DR SMR; B5RB82; -.
DR EnsemblBacteria; CAR37753; CAR37753; SG1901.
DR KEGG; seg:SG1901; -.
DR HOGENOM; CLU_036604_0_3_6; -.
DR OMA; VNVPGWR; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000008321; 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..303
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_1000140193"
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 303 AA; 32968 MW; 2632155BA9DE4468 CRC64;
MYYGFDIGGT KIALGVFDST RRLQWEKRVP TPHTSYSAFL DAVCELVAEA DQRLGVKGSV
GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
QYPLVMGLIL GTGVGGGLVL NGKPITGQSY ITGEFGHMRL PVDALTLMGF DFPLRRCGCG
QMGCIENYLS GRGFAWLYQH YYDQSLQAPE IIALWEQGDE QAHAHVERYL DLLAVCLGNI
LTIVDPDLLV IGGGLSNFTA ITTQLAERLP RHLLPVARAP RIERARHGDA GGMRGAAFLH
LTD