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   03-AUG-2022, entry version 99.
DE   RecName: Full=N-acetyl-D-glucosamine kinase;
DE            Short=N-acetylglucosamine kinase;
DE            EC=2.7.1.59;
DE   AltName: Full=GlcNAc kinase;
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. Involved in the N-
CC       glycolylneuraminic acid (Neu5Gc) degradation pathway. Also has ManNAc
CC       kinase activity (By similarity). {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: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; Q3SZM9; -.
DR   PRIDE; Q3SZM9; -.
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; 1572762at2759; -.
DR   TreeFam; TF314158; -.
DR   UniPathway; UPA00629; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; ISS:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR039758; NAGK_prok_euk.
DR   PANTHER; PTHR12862; PTHR12862; 1.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   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="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         107
FT                   /ligand="substrate"
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="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         145..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         152
FT                   /ligand="substrate"
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