NAGK_YERPA
ID NAGK_YERPA Reviewed; 256 AA.
AC Q1C6R0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE EC=2.7.1.59;
DE AltName: Full=GlcNAc kinase;
GN Name=nagK; OrderedLocusNames=YPA_1896;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
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).
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=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;
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; CP000308; ABG13862.1; -; Genomic_DNA.
DR RefSeq; WP_002216175.1; NC_008150.1.
DR AlphaFoldDB; Q1C6R0; -.
DR SMR; Q1C6R0; -.
DR EnsemblBacteria; ABG13862; ABG13862; YPA_1896.
DR GeneID; 57976944; -.
DR KEGG; ypa:YPA_1896; -.
DR OMA; VNVPGWR; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001971; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR InterPro; IPR043129; ATPase_NBD.
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..256
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000270124"
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