NAGK_RAT
ID NAGK_RAT Reviewed; 343 AA.
AC P81799; Q32Q91;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 107.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-13; 69-92; 166-178; 198-207; 221-228; 233-235 AND
RP 308-321, ACETYLATION AT ALA-2, ACTIVITY REGULATION, SUBUNIT, AND FUNCTION.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=9523722; DOI=10.1046/j.1432-1327.1998.2520133.x;
RA Hinderlich S., Noehring S., Weise C., Franke P., Staesche R., Reutter W.;
RT "Purification and characterization of N-acetylglucosamine kinase from rat
RT liver. Comparison with UDP-N-acetylglucosamine 2-epimerase/N-
RT acetylmannosamine kinase.";
RL Eur. J. Biochem. 252:133-139(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:9523722}.
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 -!- ACTIVITY REGULATION: Inhibited by the cysteine modifiers iodoacetamide,
CC N-ethylmaleimide and 5,5'-dithiobis(2-nitrobenzoic acid).
CC {ECO:0000269|PubMed:9523722}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9523722}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC family. {ECO:0000305}.
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DR EMBL; BC107647; AAI07648.1; -; mRNA.
DR RefSeq; NP_001032857.1; NM_001037768.1.
DR AlphaFoldDB; P81799; -.
DR SMR; P81799; -.
DR IntAct; P81799; 1.
DR STRING; 10116.ENSRNOP00000039247; -.
DR iPTMnet; P81799; -.
DR PhosphoSitePlus; P81799; -.
DR jPOST; P81799; -.
DR PaxDb; P81799; -.
DR PRIDE; P81799; -.
DR Ensembl; ENSRNOT00000108444; ENSRNOP00000084218; ENSRNOG00000013911.
DR GeneID; 297393; -.
DR KEGG; rno:297393; -.
DR UCSC; RGD:1305057; rat.
DR CTD; 55577; -.
DR RGD; 1305057; Nagk.
DR eggNOG; KOG1794; Eukaryota.
DR GeneTree; ENSGT00510000047418; -.
DR HOGENOM; CLU_016274_0_0_1; -.
DR InParanoid; P81799; -.
DR OMA; DTMGSMF; -.
DR OrthoDB; 1572762at2759; -.
DR PhylomeDB; P81799; -.
DR TreeFam; TF314158; -.
DR Reactome; R-RNO-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; P81799; -.
DR UniPathway; UPA00629; -.
DR PRO; PR:P81799; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013911; Expressed in duodenum and 19 other tissues.
DR Genevisible; P81799; RN.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; ISS:UniProtKB.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; ISO:RGD.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9523722"
FT CHAIN 2..343
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000096698"
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9523722"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT CONFLICT 207
FT /note="D -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="H -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 37196 MW; 43886E3262D08A0F CRC64;
MAALYGGVEG GGTRSKVLLL SEDGQILAEA DGLSTNHWLI GTGTCVERIN EMVDRAKRKA
GVDPLVPLRS LGLSLSGGEQ EDAVRLLMEE LRDRFPYLSE SYFITTDAAG SIATATPDGG
IVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGHVKQAMFN YFQVPDRLGI LTHLYRDFDK SKFAGFCQKI AEGAQQGDPL SRFIFRKAGE
MLGRHVVAVL PEIDPVLFQG ELGLPILCVG SVWKSWELLK EGFLLALTQG REQQAQNSFS
SFTLMKLRHS SALGGASLGA RHIGHHLPMD YSVNAIAFYS YTF
