ID NAGK_BOVIN Reviewed; 344 AA.
AC Q3SZM9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 08-NOV-2023, entry version 104.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE Short=N-acetylglucosamine kinase;
DE EC=2.7.1.59 {ECO:0000250|UniProtKB:Q9QZ08};
DE AltName: Full=GlcNAc kinase;
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};
GN Name=NAGK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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=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 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=ATP + N-acetyl-D-mannosamine = ADP + H(+) + N-acetyl-D-
CC mannosamine 6-phosphate; Xref=Rhea:RHEA:25253, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17122, ChEBI:CHEBI:30616, ChEBI:CHEBI:58557,
CC 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=ATP + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine = 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:0000305}.
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DR EMBL; BC102780; AAI02781.1; -; mRNA.
DR RefSeq; NP_001029486.1; NM_001034314.2.
DR AlphaFoldDB; Q3SZM9; -.
DR SMR; Q3SZM9; -.
DR STRING; 9913.ENSBTAP00000019528; -.
DR PaxDb; 9913-ENSBTAP00000019528; -.
DR GeneID; 508132; -.
DR KEGG; bta:508132; -.
DR CTD; 55577; -.
DR eggNOG; KOG1794; Eukaryota.
DR HOGENOM; CLU_016274_0_0_1; -.
DR InParanoid; Q3SZM9; -.
DR OrthoDB; 3030525at2759; -.
DR TreeFam; TF314158; -.
DR UniPathway; UPA00629; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR039758; NAGK_prok_euk.
DR PANTHER; PTHR12862; BADF TYPE ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12862:SF0; N-ACETYL-D-GLUCOSAMINE KINASE; 1.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Immunity; Innate immunity; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..344
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000253473"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 36
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 107
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 129..130
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 145..147
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 152
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT MOD_RES 205
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ SEQUENCE 344 AA; 37268 MW; 575EC6F41FA4BA08 CRC64;
MVTLYGGVEG GGTRSKVLLL SEDGQILAEA DGLSTNHWLI GTDKCVERIN EMVNRAKRKA
GVDPLVPLRG LGLSLSGGDQ EDAVRMLMEE LRDRFPYLSE SYLITTDAAG SIATATPDGG
VVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGYVKQAMFN YFQVPDRLGI LTHLYRDFDK SRFAGFCRKV AEGAQQGDPL SRCIFRKAGE
MLGRHVVAVL PEIDPVLFQG EMGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNSFS
GFTLLKLRHS SALGAASLGA KHIGHLLPMD YSTSAIAFYS YTFS
//