ID   NAGK_DICDI              Reviewed;         319 AA.
AC   Q54PM7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 72.
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; ORFNames=DDB_G0284433;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Converts N-acetylglucosamine (GlcNAc), a major component of
CC       complex carbohydrates, into GlcNAc 6-phosphate. Also has ManNAc kinase
CC       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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL65265.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000064; EAL65265.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_638627.1; XM_633535.1.
DR   AlphaFoldDB; Q54PM7; -.
DR   SMR; Q54PM7; -.
DR   STRING; 44689.DDB0186012; -.
DR   PaxDb; Q54PM7; -.
DR   PRIDE; Q54PM7; -.
DR   EnsemblProtists; EAL65265; EAL65265; DDB_G0284433.
DR   GeneID; 8624598; -.
DR   KEGG; ddi:DDB_G0284433; -.
DR   dictyBase; DDB_G0284433; -.
DR   eggNOG; KOG1794; Eukaryota.
DR   InParanoid; Q54PM7; -.
DR   PhylomeDB; Q54PM7; -.
DR   PRO; PR:Q54PM7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..319
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_0000331385"
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         153..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ   SEQUENCE   319 AA;  34504 MW;  E5C017C4ED95F26F CRC64;
     MSKEIFIGID GGGTKTSTVA VDSNGQELAR HTSPCSNYHS VGEDLAKAAI NEGIKYVIRK
     VKETITDDDN KEVTVGSICL GMSGVDREKD KLLVKSWVTE LLGESINYSI HNDAIVALSS
     GTQGKLFGVV IICGTGCISL GFNREGVSGR SGGWGPLLGD YGSGYQIGYD ILRHVLKAKD
     QVGPKTSLTQ VLLEKLQLTK EEDLISWAYD PKTQSWQKFA QLSPLAFEQA QLGDEISNLI
     LVDAANALYD LINSVIKKLG LDKEEKFPLV YTGGNIERKG ILSDLLSKKI MENYPNAEIL
     NTTCDPSMGA ALLALNSKK