NAGK_SHISS
ID NAGK_SHISS Reviewed; 303 AA.
AC Q3Z2Z8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, 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=SSON_1139;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87864.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z2Z8; -.
DR SMR; Q3Z2Z8; -.
DR EnsemblBacteria; AAZ87864; AAZ87864; SSON_1139.
DR KEGG; ssn:SSON_1139; -.
DR HOGENOM; CLU_036604_0_3_6; -.
DR OMA; VNVPGWR; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002529; 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_0000270118"
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; 33032 MW; 02F935E34B3C90DC CRC64;
MYYGFDIGGT KIALGVFDSG RQLQWEKRVP TPRDSYDAFL DAVCELVAEA DQRFGCKGSV
GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
QYPLVMGLIL GTGVGGGLIF NGKPITGKSY ITGEFGHMRL PVDALTMMGL DFPLRRCGCG
QIGCIENYLS GRGFAWLWQH YYHQPLQAPE IIALYDQGDE QARAHVERYL DLLAVCLGNI
LTIVDSDLVV IGGGLSNFPA ITTQLADRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH
LTD
