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Information on EC 5.4.2.3 - phosphoacetylglucosamine mutase and Organism(s) Candida albicans and UniProt Accession Q9P4V2

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EC Tree
IUBMB Comments
The enzyme is activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate.
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This record set is specific for:
Candida albicans
UNIPROT: Q9P4V2
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Word Map
The taxonomic range for the selected organisms is: Candida albicans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phosphoacetylglucosamine mutase, n-acetylglucosamine-phosphate mutase, phospho-n-acetylglucosamine mutase, hsagm1, caagm1, acetylglucosamine phosphomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoacetylglucosamine mutase 1
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2-Acetamido-2-deoxy-D-glucose-1,6-bisphosphate:2-acetamido-2-deoxy-D-glucose 1-phosphate phosphotransferase
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-
-
-
Acetylaminodeoxyglucose phosphomutase
-
-
-
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Acetylglucosamine phosphomutase
-
-
-
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DNA-damage-repair/toleration protein DRT101
-
-
-
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N-acetylglucosamine-phosphate mutase
-
-
-
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PAGM
-
-
-
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PGlcNAc mutase
-
-
-
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Phospho-N-acetylglucosamine mutase
-
-
-
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Phosphomutase, acetylglucosamine
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
the N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180° on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
N-Acetyl-alpha-D-glucosamine 1,6-phosphomutase
The enzyme is activated by N-acetyl-alpha-D-glucosamine 1,6-bisphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-51-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-alpha-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
r
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-alpha-D-glucosamine 6-phosphate
show the reaction diagram
-
-
-
r
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine 6-phosphate
show the reaction diagram
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3aR,5R,6S,7R,7aR)-5-(hydroxymethyl)-2-methyl-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d][1,3]oxazole-6,7-diol
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2,5:4,8-dianhydro-1,3-dideoxy-9-O-phosphono-D-erythro-L-gulo-nonitol
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2-acetamido-1,5-anhydro-2,6,7-trideoxy-7-phosphono-D-gluco-heptitol
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2-acetamido-1,5-anhydro-2,6-dideoxy-6-(sulfoamino)-D-glucitol
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2-acetamido-1,5-anhydro-2,6-dideoxy-6-phosphono-D-glucitol
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2-acetamido-1,5-anhydro-2,6-dideoxy-6-sulfo-D-glucitol
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2-acetamido-1,5-anhydro-2-deoxy-6-O-phosphono-D-glucitol
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2-acetamido-1,5-anhydro-2-deoxy-6-O-sulfo-D-glucitol
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2-acetamido-1,5-anhydro-2-deoxy-D-glucitol
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2-acetamido-2-deoxy-6-O-sulfo-D-glucopyranose
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2-acetamido-2-deoxy-N-phosphono-6-O-phosphono-D-glucopyranosylamine
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[(3aR,5R,6S,7R,7aR)-6,7-dihydroxy-2-methyl-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d][1,3]oxazol-5-yl]methyl phosphate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AGM1_CANAX
544
0
60478
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 60000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both in apo form and in the complex forms with substrate and product. Protein consists of four domains. of which three domains have essentially the same fold. The catalytic cleft is formed by four loops from each domains. The N-acetyl group of the substrate is recognized by V370 and N389 in domain 3, from which the substrate specificity arises. Substrate rotates about 180° on the axis linking C4 and the midpoint of the C5-O5 bond in the reaction
space group P21, crystal diffract to beyond 1.8 A
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant CaAgm1-GST fusion protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression as glutathione S-transferase fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mio, T.; Yamada-Okabe, T.; Arisawa, M.; Yamada-Okabe, H.
Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis
Biochim. Biophys. Acta
1492
369-376
2000
Homo sapiens (O95394), Homo sapiens, Candida albicans (Q9P4V2), Candida albicans
Manually annotated by BRENDA team
Nishitani, Y.; Maruyama, D.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosamine-phosphate mutase from Candida albicans
Acta Crystallogr. Sect. F
62
419-421
2006
Candida albicans
Manually annotated by BRENDA team
Nishitani, Y.; Maruyama, D.; Nonaka, T.; Kita, A.; Fukami, T.A.; Mio, T.; Yamada-Okabe, H.; Yamada-Okabe, T.; Miki, K.
Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes
J. Biol. Chem.
281
19740-19747
2006
Candida albicans (Q9P4V2), Candida albicans
Manually annotated by BRENDA team
Paiotta, A.; D'Orazio, G.; Palorini, R.; Ricciardiello, F.; Zoia, L.; Votta, G.; De Gioia, L.; Chiaradonna, F.; La Ferla, B.
Design, synthesis, and preliminary biological evaluation of GlcNAc-6P analogues for the modulation of phosphoacetylglucosamine mutase 1 (AGM1/PGM3)
Eur. J. Org. Chem.
2018
1946-1952
2018
Candida albicans (Q9P4V2)
-
Manually annotated by BRENDA team