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Information on EC 2.3.1.4 - glucosamine-phosphate N-acetyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LFU9

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Arabidopsis thaliana
UNIPROT: Q9LFU9 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucosamine-6-phosphate n-acetyltransferase, glucosamine-phosphate n-acetyltransferase, glucosamine 6-phosphate n-acetyltransferase, glucosamine-6-phosphate acetyltransferase, glucosamine-6-phosphate n-acetyltransferase 1, osgna1, hsgna1, glcnac-6-phosphate n-acetyltransferase, glucosamine 6-phosphate acetylase, scgna1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyltransferase, glucosamine phosphate
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-
-
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aminodeoxyglucosephosphate acetyltransferase
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-
-
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D-glucosamine-6-P N-acetyltransferase
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-
-
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glucosamine 6-phosphate acetylase
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-
-
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glucosamine 6-phosphate N-acetyltransferase
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glucosamine phosphate acetyltransferase
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-
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glucosamine-6-phosphate acetylase
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-
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N-acetylglucosamine-6-phosphate synthase
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-
-
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phosphoglucosamine acetylase
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-
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phosphoglucosamine N-acetylase
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-
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phosphoglucosamine transacetylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-91-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + D-glucosamine 6-phosphate
CoA + N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
acetyl-CoA
pH 7.5, 30°C
0.231
D-glucosamine 6-phosphate
pH 7.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
acetyl-CoA
pH 7.5, 30°C
0.52
D-glucosamine 6-phosphate
pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
endomembrane system
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the mutant called lignescens, a temperature-sensitive mutant that exhibits ectopic lignin deposition and growth defects under high-temperature conditions, is due to single base transition G68S in glucosamine-6-phosphate N-acetyltransferase. When exposed to the restrictive temperature, the mutant strain contains a significantly smaller amount of UDP-GlcNAc than the wild type. The growth defects and ectopic lignification of the mutant are suppressed by the addition of UDP-GlcNAc. N-glycans are reduced and luminal binding protein 3, a typical UPR gene, is expressed in the mutant strain at the restrictive temperature. Treatment with UPR-inducing reagents phenocopies the mutant
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GNA1_ARATH
149
0
17028
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19200
2 * 19200, calculated, 2 * 20000, SDS-PAGE
20000
2 * 19200, calculated, 2 * 20000, SDS-PAGE
40300
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 19200, calculated, 2 * 20000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.5 A resolution. The centre of the protein is a five-stranded beta-sheet, of which four strands are antiparallel-oriented
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G68S
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the mutant called lignescens, a temperature-sensitive mutant that exhibits ectopic lignin deposition and growth defects under high-temperature conditions, is due to single base transition G68S in glucosamine-6-phosphate N-acetyltransferase. When exposed to the restrictive temperature, the mutant strain contains a significantly smaller amount of UDP-GlcNAc than the wild type. The growth defects and ectopic lignification of the mutant are suppressed by the addition of UDP-GlcNAc. N-glycans are reduced and luminal binding protein 3, a typical UPR gene, is expressed in the mutant strain at the restrictive temperature. Treatment with UPR-inducing reagents phenocopies the mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine by overexpression of glucosamine synthase and glucosamine 6-phosphate N-acetyltransferase and inactivation of catabolic genes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine by overexpression of glucosamine synthase and glucosamine 6-phosphate N-acetyltransferase and inactivation of catabolic genes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deng, M.D.; Severson, D.K.; Grund, A.D.; et al
Metabolic engineering of Escherichia coli for industrial production of glucosamine and N-acetylglucosamine
Metab. Eng.
7
201-214
2005
Arabidopsis thaliana, Candida albicans, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Riegler, H.; Herter, T.; Grishkovskaya, I.; Lude, A.; Ryngajllo, M.; Bolger, M.E.; Essigmann, B.; Usadel, B.
Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana
Biochem. J.
443
427-437
2012
Arabidopsis thaliana (Q9LFU9), Arabidopsis thaliana
Manually annotated by BRENDA team
Nozaki, M.; Sugiyama, M.; Duan, J.; Uematsu, H.; Genda, T.; Sato, Y.
A missense mutation in the glucosamine-6-phosphate N-acetyltransferase-encoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis
Plant Cell
24
3366-3379
2012
Arabidopsis thaliana
Manually annotated by BRENDA team