Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Uehara T |
Year: |
2004 |
Journal: |
J Bacteriol |
Title: |
The N-acetyl-D-glucosamine kinase of Escherichia coli and its role in murein recycling. |
Volume: |
186 |
Issue: |
21 |
Pages: |
7273-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ramón-Maiques S |
Year: |
2006 |
Journal: |
J Mol Biol |
Title: |
Structural bases of feed-back control of arginine biosynthesis, revealed by the structures of two hexameric N-acetylglutamate kinases, from Thermotoga maritima and Pseudomonas aeruginosa. |
Volume: |
356 |
Issue: |
3 |
Pages: |
695-713 |
|
•
•
•
•
•
|
Publication |
First Author: |
Fernández-Murga ML |
Year: |
2002 |
Journal: |
Acta Crystallogr D Biol Crystallogr |
Title: |
Towards structural understanding of feedback control of arginine biosynthesis: cloning and expression of the gene for the arginine-inhibited N-acetyl-L-glutamate kinase from Pseudomonas aeruginosa, purification and crystallization of the recombinant enzyme and preliminary X-ray studies. |
Volume: |
58 |
Issue: |
Pt 6 Pt 2 |
Pages: |
1045-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Fernández-Murga ML |
Year: |
2004 |
Journal: |
J Bacteriol |
Title: |
Arginine biosynthesis in Thermotoga maritima: characterization of the arginine-sensitive N-acetyl-L-glutamate kinase. |
Volume: |
186 |
Issue: |
18 |
Pages: |
6142-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Burillo S |
Year: |
2004 |
Journal: |
J Bacteriol |
Title: |
Interactions between the nitrogen signal transduction protein PII and N-acetyl glutamate kinase in organisms that perform oxygenic photosynthesis. |
Volume: |
186 |
Issue: |
11 |
Pages: |
3346-54 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sugiyama K |
Year: |
2004 |
Journal: |
Plant Cell Physiol |
Title: |
Interaction of N-acetylglutamate kinase with a PII-like protein in rice. |
Volume: |
45 |
Issue: |
12 |
Pages: |
1768-78 |
|
•
•
•
•
•
|
Publication |
First Author: |
Maheswaran M |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942. |
Volume: |
279 |
Issue: |
53 |
Pages: |
55202-10 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The cyclic N-Acetyl-L-glutamate kinase (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of the arginine biosynthesis pathway. In the cyclic one, typified by Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation [, , , , , , ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents N-acetyl-D-glucosamine kinases which catalyse the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P [, ]. This group of proteins belong to the NagK subfamily of the ROK (nagC/xylR) family. |
|
•
•
•
•
•
|
Publication |
First Author: |
Cunin R |
Year: |
1986 |
Journal: |
Microbiol Rev |
Title: |
Biosynthesis and metabolism of arginine in bacteria. |
Volume: |
50 |
Issue: |
3 |
Pages: |
314-52 |
|
•
•
•
•
•
|
Publication |
First Author: |
Islam MA |
Year: |
2015 |
Journal: |
Mol Cells |
Title: |
N-Acetyl-D-Glucosamine Kinase Promotes the Axonal Growth of Developing Neurons. |
Volume: |
38 |
Issue: |
10 |
Pages: |
876-85 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sharif SR |
Year: |
2016 |
Journal: |
Mol Cells |
Title: |
N-Acetyl-D-Glucosamine Kinase Interacts with Dynein-Lis1-NudE1 Complex and Regulates Cell Division. |
Volume: |
39 |
Issue: |
9 |
Pages: |
669-79 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes N-acetyl-D-glucosamine kinases (NAGKs) from prokaryotes and eukaryotes. NAGK converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate []. It has been shown to play an enzyme activity-independent role in human neurons [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Davis RH |
Year: |
1986 |
Journal: |
Microbiol Rev |
Title: |
Compartmental and regulatory mechanisms in the arginine pathways of Neurospora crassa and Saccharomyces cerevisiae. |
Volume: |
50 |
Issue: |
3 |
Pages: |
280-313 |
|
•
•
•
•
•
|
Publication |
First Author: |
Negredo A |
Year: |
1997 |
Journal: |
Microbiology |
Title: |
Cloning, analysis and one-step disruption of the ARG5,6 gene of Candida albicans. |
Volume: |
143 ( Pt 2) |
|
Pages: |
297-302 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pauwels K |
Year: |
2003 |
Journal: |
Eur J Biochem |
Title: |
The N-acetylglutamate synthase/N-acetylglutamate kinase metabolon of Saccharomyces cerevisiae allows co-ordinated feedback regulation of the first two steps in arginine biosynthesis. |
Volume: |
270 |
Issue: |
5 |
Pages: |
1014-24 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP) is a nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this entry), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This entry also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homologue of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide [,, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Ramón-Maiques S |
Year: |
2002 |
Journal: |
Structure |
Title: |
Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis. |
Volume: |
10 |
Issue: |
3 |
Pages: |
329-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gil-Ortiz F |
Year: |
2003 |
Journal: |
J Mol Biol |
Title: |
The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic. |
Volume: |
331 |
Issue: |
1 |
Pages: |
231-44 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gil F |
Year: |
1999 |
Journal: |
Acta Crystallogr D Biol Crystallogr |
Title: |
N-Acetyl-L-glutamate kinase from Escherichia coli: cloning of the gene, purification and crystallization of the recombinant enzyme and preliminary X-ray analysis of the free and ligand-bound forms. |
Volume: |
55 |
Issue: |
Pt 7 |
Pages: |
1350-2 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gil-Ortiz F |
Year: |
2002 |
Journal: |
Acta Crystallogr D Biol Crystallogr |
Title: |
A crystallographic glimpse of a nucleotide triphosphate (AMPPNP) bound to a protein surface: external and internal AMPPNP molecules in crystalline N-acetyl-L-glutamate kinase. |
Volume: |
58 |
Issue: |
Pt 10 Pt 2 |
Pages: |
1892-5 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The noncyclic N-Acetyl-L-glutamate kinase (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of the arginine biosynthesis pathway. In this one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. The Escherichia coli NAGK is a homodimer [, , , , , ]. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
343
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
337
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
343
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
361
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Miller BG |
Year: |
2004 |
Journal: |
Biochemistry |
Title: |
Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases. |
Volume: |
43 |
Issue: |
21 |
Pages: |
6387-92 |
|
•
•
•
•
•
|
Publication |
First Author: |
Marco-Marín C |
Year: |
2003 |
Journal: |
J Mol Biol |
Title: |
Site-directed mutagenesis of Escherichia coli acetylglutamate kinase and aspartokinase III probes the catalytic and substrate-binding mechanisms of these amino acid kinase family enzymes and allows three-dimensional modelling of aspartokinase. |
Volume: |
334 |
Issue: |
3 |
Pages: |
459-76 |
|
•
•
•
•
•
|