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P81799 (NAGK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyl-D-glucosamine kinase

Short name=N-acetylglucosamine kinase
EC=2.7.1.59
Alternative name(s):
GlcNAc kinase
Gene names
Name:Nagk
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Also has ManNAc kinase activity. Ref.2

Catalytic activity

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate.

Enzyme regulation

Inhibited by the cysteine modifiers iodoacetamide, N-ethylmaleimide and 5,5'-dithiobis(2-nitrobenzoic acid). Ref.2

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation.

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the eukaryotic-type N-acetylglucosamine kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 343342N-acetyl-D-glucosamine kinase
PRO_0000096698

Regions

Nucleotide binding6 – 138ATP By similarity
Region129 – 1302Substrate binding By similarity
Region145 – 1473Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1071Substrate By similarity
Binding site1521Substrate By similarity
Binding site2711ATP By similarity
Binding site2751ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue761Phosphoserine By similarity
Modified residue2051Phosphotyrosine By similarity

Experimental info

Sequence conflict2071D → T AA sequence Ref.2
Sequence conflict2261Q → E AA sequence Ref.2
Sequence conflict3091H → I AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P81799 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 43886E3262D08A0F

FASTA34337,196
        10         20         30         40         50         60 
MAALYGGVEG GGTRSKVLLL SEDGQILAEA DGLSTNHWLI GTGTCVERIN EMVDRAKRKA 

        70         80         90        100        110        120 
GVDPLVPLRS LGLSLSGGEQ EDAVRLLMEE LRDRFPYLSE SYFITTDAAG SIATATPDGG 

       130        140        150        160        170        180 
IVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD 

       190        200        210        220        230        240 
IGHVKQAMFN YFQVPDRLGI LTHLYRDFDK SKFAGFCQKI AEGAQQGDPL SRFIFRKAGE 

       250        260        270        280        290        300 
MLGRHVVAVL PEIDPVLFQG ELGLPILCVG SVWKSWELLK EGFLLALTQG REQQAQNSFS 

       310        320        330        340 
SFTLMKLRHS SALGGASLGA RHIGHHLPMD YSVNAIAFYS YTF 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[2]"Purification and characterization of N-acetylglucosamine kinase from rat liver. Comparison with UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase."
Hinderlich S., Noehring S., Weise C., Franke P., Staesche R., Reutter W.
Eur. J. Biochem. 252:133-139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13; 69-92; 166-178; 198-207; 221-228; 233-235 AND 308-321, ACETYLATION AT ALA-2, ENZYME REGULATION, SUBUNIT, FUNCTION.
Strain: Wistar.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC107647 mRNA. Translation: AAI07648.1.
RefSeqNP_001032857.1. NM_001037768.1.
UniGeneRn.105985.

3D structure databases

ProteinModelPortalP81799.
SMRP81799. Positions 2-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP81799. 1 interaction.
STRING10116.ENSRNOP00000039247.

PTM databases

PhosphoSiteP81799.

Proteomic databases

PRIDEP81799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000042875; ENSRNOP00000039247; ENSRNOG00000013911.
GeneID297393.
KEGGrno:297393.
UCSCRGD:1305057. rat.

Organism-specific databases

CTD55577.
RGD1305057. Nagk.

Phylogenomic databases

eggNOGCOG2971.
GeneTreeENSGT00510000047418.
HOGENOMHOG000007248.
HOVERGENHBG052570.
KOK00884.
OMAAFYSYTF.
OrthoDBEOG7V1FR7.
PhylomeDBP81799.
TreeFamTF314158.

Enzyme and pathway databases

SABIO-RKP81799.
UniPathwayUPA00629.

Gene expression databases

GenevestigatorP81799.

Family and domain databases

InterProIPR002731. ATPase_BadF.
[Graphical view]
PfamPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio642192.
PROP81799.

Entry information

Entry nameNAGK_RAT
AccessionPrimary (citable) accession number: P81799
Secondary accession number(s): Q32Q91
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 70 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways