ID   NAGK_MESAU              Reviewed;          61 AA.
AC   P86200;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   02-SEP-2026, entry version 25.
DE   RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000250|UniProtKB:Q9QZ08};
DE            Short=N-acetylglucosamine kinase {ECO:0000250|UniProtKB:Q9QZ08};
DE            EC=2.7.1.59 {ECO:0000250|UniProtKB:Q9QZ08};
DE   AltName: Full=GlcNAc kinase {ECO:0000250|UniProtKB:Q9QZ08};
DE   AltName: Full=Muramyl dipeptide kinase {ECO:0000305};
DE            EC=2.7.1.- {ECO:0000250|UniProtKB:Q9UJ70};
DE   AltName: Full=N-acetyl-D-mannosamine kinase {ECO:0000305};
DE            EC=2.7.1.60 {ECO:0000250|UniProtKB:Q9QZ08};
DE   Flags: Fragments;
GN   Name=NAGK {ECO:0000250|UniProtKB:Q9QZ08};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20400973; DOI=10.1038/aja.2010.19;
RA   Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT   "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT   (GP96) are unique to hamster caput epididymal spermatozoa.";
RL   Asian J. Androl. 12:344-355(2010).
CC   -!- FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major
CC       component of complex carbohydrates, from lysosomal degradation or
CC       nutritional sources into GlcNAc 6-phosphate (By similarity). Also has
CC       N-acetylmannosamine (ManNAc) kinase activity (By similarity). Involved
CC       in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (By
CC       similarity). Also involved in innate immunity by promoting detection of
CC       bacterial peptidoglycan by NOD2: acts by catalyzing phosphorylation of
CC       muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, to
CC       generate 6-O-phospho-muramyl dipeptide, which acts as a direct ligand
CC       for NOD2 (By similarity). {ECO:0000250|UniProtKB:Q9QZ08,
CC       ECO:0000250|UniProtKB:Q9UJ70}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-glucosamine + ATP = N-acetyl-D-glucosamine 6-
CC         phosphate + ADP + H(+); 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         Evidence={ECO:0000250|UniProtKB:Q9QZ08};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17418;
CC         Evidence={ECO:0000250|UniProtKB:Q9QZ08};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-N-acetyl-D-mannosamine + ATP = aldehydo-N-acetyl-D-
CC         mannosamine 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:25253,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17122, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58557, ChEBI:CHEBI:456216; EC=2.7.1.60;
CC         Evidence={ECO:0000250|UniProtKB:Q9QZ08};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25254;
CC         Evidence={ECO:0000250|UniProtKB:Q9QZ08};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine + ATP = 6-O-
CC         phospho-N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine + ADP + H(+);
CC         Xref=Rhea:RHEA:75935, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:155830, ChEBI:CHEBI:194492, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:Q9UJ70};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75936;
CC         Evidence={ECO:0000250|UniProtKB:Q9UJ70};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC       {ECO:0000250|UniProtKB:Q9QZ08}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9QZ08}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P86200; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000886700; Unplaced.
DR   GO; GO:0160047; F:muramyl dipeptide kinase activity; ISS:UniProtKB.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; ISS:UniProtKB.
DR   GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032495; P:response to muramyl dipeptide; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   ATP-binding; Immunity; Innate immunity; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           <1..>61
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_0000394398"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   MOD_RES         30
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_CONS        31..32
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         61
SQ   SEQUENCE   61 AA;  6868 MW;  F24D4EE847EBDF63 CRC64;
     AGVDPLVPLR QAMFNYFQVP DRLGILTHLY RIAEGAQQGD PLSRSWELLK EGFLLALTQG
     R
//