N-acetylglucosamine degradation I

MetaCyc:GLUAMCAT-PWY

N-acetylglucosamine degradation I deacetylates N-acetyl-D-glucosamine 6-phosphate to D-glucosamine 6-phosphate and acetate, then deaminates alpha-D-glucosamine 6-phosphate to beta-D-fructose 6-phosphate and ammonium.

Pathway type
carbohydrate degradation
Organism scope

Read the source YAML

Pathway network

19 nodes · 22 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Pathway network: N-acetylglucosamine degradation I 19 nodes · 22 asserted directed edges. Every arrow links to its evidence table row; nodes link to their component details. Isolated declared components are retained. CHEBI:15377 — consumes → RHEA:22937; Evidence: RHEA:22937consumes CHEBI:57513 — consumes → RHEA:22937; Evidence: RHEA:22937consumes RHEA:22937 — produces → CHEBI:30089; Evidence: RHEA:22937produces RHEA:22937 — produces → CHEBI:58725; Evidence: RHEA:22937produces CHEBI:15377 — consumes → RHEA:12173; Evidence: RHEA:12173consumes CHEBI:75989 — consumes → RHEA:12173; Evidence: RHEA:12173consumes RHEA:12173 — produces → CHEBI:28938; Evidence: RHEA:12173produces RHEA:12173 — produces → CHEBI:57634; Evidence: RHEA:12173produces EC:3.5.1.25 — catalyzes → RHEA:22937; Evidence: RHEA:22936catalyzes EC:3.5.99.6 — catalyzes → RHEA:12173; Evidence: RHEA:12172catalyzes RHEA:22937 — precedes → RHEA:12173; Evidence: MetaCyc:GLUAMCAT-PWYprecedes UniProtKB:P0A759 — enables → RHEA:12173; Evidence: UniProtKB:P0A759enables CHEBI:57513 — activates → UniProtKB:P0A759; Evidence: UniProtKB:P0A759activates UniProtKB:P0AF18 — enables → RHEA:22937; Evidence: UniProtKB:P0AF18enables CHEBI:58725 — inhibits → UniProtKB:P0AF18; Evidence: UniProtKB:P0AF18inhibits CHEBI:30089 — inhibits → UniProtKB:P0AF18; Evidence: UniProtKB:P0AF18inhibits UniProtKB:P0AF18 — has_cofactor → CHEBI:29105; Evidence: UniProtKB:P0AF18has cofactor UniProtKB:P0AF18 — has_cofactor → CHEBI:48828; Evidence: UniProtKB:P0AF18has cofactor UniProtKB:P0AF18 — has_cofactor → CHEBI:29035; Evidence: UniProtKB:P0AF18has cofactor UniProtKB:P0AF18 — has_cofactor → CHEBI:48775; Evidence: UniProtKB:P0AF18has cofactor UniProtKB:P0AF18 — has_cofactor → CHEBI:29033; Evidence: UniProtKB:P0AF18has cofactor UniProtKB:P0AF18 — has_cofactor → CHEBI:49786; Evidence: UniProtKB:P0AF18has cofactor N-acetylglucosamine-6-phosphate deacetylase; EC:3.5.1.25; Declared type: molecular_activity molecular activity N-acetylglucosamine-6- phosphate deacetylase glucosamine-6-phosphate deaminase; EC:3.5.99.6; Declared type: molecular_activity molecular activity glucosamine-6-phosphate deaminase N-acetyl-D-glucosamine 6-phosphate; CHEBI:57513; Declared type: small_molecule small molecule N-acetyl-D-glucosamine 6-phosphate H2O; CHEBI:15377; Declared type: small_molecule small molecule H2O D-glucosamine 6-phosphate; CHEBI:58725; Declared type: small_molecule small molecule D-glucosamine 6-phosphate acetate; CHEBI:30089; Declared type: small_molecule small molecule acetate alpha-D-glucosamine 6-phosphate; CHEBI:75989; Declared type: small_molecule small molecule alpha-D-glucosamine 6-phosphate beta-D-fructose 6-phosphate; CHEBI:57634; Declared type: small_molecule small molecule beta-D-fructose 6-phosphate NH4(+); CHEBI:28938; Declared type: small_molecule small molecule NH4(+) Glucosamine-6-phosphate deaminase; UniProtKB:P0A759; Declared type: protein protein Glucosamine-6-phosphate deaminase N-acetylglucosamine-6-phosphate deacetylase; UniProtKB:P0AF18; Declared type: protein protein N-acetylglucosamine-6- phosphate deacetylase zinc(2+); CHEBI:29105; Declared type: cofactor cofactor zinc(2+) cobalt(2+); CHEBI:48828; Declared type: cofactor cofactor cobalt(2+) manganese(2+); CHEBI:29035; Declared type: cofactor cofactor manganese(2+) cadmium(2+); CHEBI:48775; Declared type: cofactor cofactor cadmium(2+) iron(2+); CHEBI:29033; Declared type: cofactor cofactor iron(2+) nickel(2+); CHEBI:49786; Declared type: cofactor cofactor nickel(2+) N-acetylglucosamine-6-phosphate deacetylase reaction; RHEA:22937; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity N-acetylglucosamine-6- phosphate deacetylase reaction glucosamine-6-phosphate deaminase reaction; RHEA:12173; Declared type: reaction/activity; Source reaction direction: left_to_right reaction / activity glucosamine-6-phosphate deaminase reaction

Components and activities

Declared biological components and source reaction directions
NodeKind or roleSource direction
Escherichia coli
NCBITaxon:562		taxon
N-acetylglucosamine-6-phosphate deacetylase
EC:3.5.1.25		molecular activity
glucosamine-6-phosphate deaminase
EC:3.5.99.6		molecular activity
N-acetyl-D-glucosamine 6-phosphate
CHEBI:57513		small molecule
H2O
CHEBI:15377		small molecule
D-glucosamine 6-phosphate
CHEBI:58725		small molecule
acetate
CHEBI:30089		small molecule
alpha-D-glucosamine 6-phosphate
CHEBI:75989		small molecule
beta-D-fructose 6-phosphate
CHEBI:57634		small molecule
NH4(+)
CHEBI:28938		small molecule
Glucosamine-6-phosphate deaminase
UniProtKB:P0A759		protein
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		protein
zinc(2+)
CHEBI:29105		cofactor
cobalt(2+)
CHEBI:48828		cofactor
manganese(2+)
CHEBI:29035		cofactor
cadmium(2+)
CHEBI:48775		cofactor
iron(2+)
CHEBI:29033		cofactor
nickel(2+)
CHEBI:49786		cofactor
N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937		reactionleft to right
glucosamine-6-phosphate deaminase reaction
RHEA:12173		reactionleft to right

Mechanistic edges

Mechanistic edges and their cited evidence
SubjectPredicate and descriptionObjectEvidence
H2O
CHEBI:15377		consumes

N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937
  • RHEA:22937

    Source assertion: Rhea lists CHEBI:15377 on the substrates side of RHEA:22937 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/22937']/rh:substrates; rh:contains/rh:compound/rh:accession
N-acetyl-D-glucosamine 6-phosphate
CHEBI:57513		consumes

N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937
  • RHEA:22937

    Source assertion: Rhea lists CHEBI:57513 on the substrates side of RHEA:22937 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/22937']/rh:substrates; rh:contains/rh:compound/rh:accession
N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937		produces

acetate
CHEBI:30089
  • RHEA:22937

    Source assertion: Rhea lists CHEBI:30089 on the products side of RHEA:22937 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/22937']/rh:products; rh:contains/rh:compound/rh:accession
N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937		produces

D-glucosamine 6-phosphate
CHEBI:58725
  • RHEA:22937

    Source assertion: Rhea lists CHEBI:58725 on the products side of RHEA:22937 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/22937']/rh:products; rh:contains/rh:compound/rh:accession
H2O
CHEBI:15377		consumes

glucosamine-6-phosphate deaminase reaction
RHEA:12173
  • RHEA:12173

    Source assertion: Rhea lists CHEBI:15377 on the substrates side of RHEA:12173 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/12173']/rh:substrates; rh:contains/rh:compound/rh:accession
alpha-D-glucosamine 6-phosphate
CHEBI:75989		consumes

glucosamine-6-phosphate deaminase reaction
RHEA:12173
  • RHEA:12173

    Source assertion: Rhea lists CHEBI:75989 on the substrates side of RHEA:12173 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/12173']/rh:substrates; rh:contains/rh:compound/rh:accession
glucosamine-6-phosphate deaminase reaction
RHEA:12173		produces

NH4(+)
CHEBI:28938
  • RHEA:12173

    Source assertion: Rhea lists CHEBI:28938 on the products side of RHEA:12173 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/12173']/rh:products; rh:contains/rh:compound/rh:accession
glucosamine-6-phosphate deaminase reaction
RHEA:12173		produces

beta-D-fructose 6-phosphate
CHEBI:57634
  • RHEA:12173

    Source assertion: Rhea lists CHEBI:57634 on the products side of RHEA:12173 in this directed reaction.

    Source locationrdf:Description[@rdf:about='http://rdf.rhea-db.org/12173']/rh:products; rh:contains/rh:compound/rh:accession
N-acetylglucosamine-6-phosphate deacetylase
EC:3.5.1.25		catalyzes

N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937
  • RHEA:22936

    Source assertion: Rhea associates EC:3.5.1.25 with the reaction family containing RHEA:22937.

    Source locationrh:ec
glucosamine-6-phosphate deaminase
EC:3.5.99.6		catalyzes

glucosamine-6-phosphate deaminase reaction
RHEA:12173
  • RHEA:12172

    Source assertion: Rhea associates EC:3.5.99.6 with the reaction family containing RHEA:12173.

    Source locationrh:ec
N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937		precedes

glucosamine-6-phosphate deaminase reaction
RHEA:12173
  • MetaCyc:GLUAMCAT-PWY

    Source assertion: MetaCyc pathway ordering places RHEA:22937 before RHEA:12173 in this pathway. The source ordering may bridge anomer-specific and broader substrate classes.

    Source locationPathway/reaction-ordering and reaction-layout; Rhea-to-MetaCyc cross-references
Glucosamine-6-phosphate deaminase
UniProtKB:P0A759		enables

glucosamine-6-phosphate deaminase reaction
RHEA:12173
  • UniProtKB:P0A759

    Source assertion: UniProt annotates UniProtKB:P0A759 with catalytic activity for the reaction family of RHEA:12173. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
N-acetyl-D-glucosamine 6-phosphate
CHEBI:57513		activates

Glucosamine-6-phosphate deaminase
UniProtKB:P0A759
  • UniProtKB:P0A759

    Source assertion: UniProt activity-regulation annotation: Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-glucitol-6-phosphate (GlcN-ol-6P)

    Source locationcomments[commentType='ACTIVITY REGULATION'].texts
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		enables

N-acetylglucosamine-6-phosphate deacetylase reaction
RHEA:22937
  • UniProtKB:P0AF18

    Source assertion: UniProt annotates UniProtKB:P0AF18 with catalytic activity for the reaction family of RHEA:22937. Annotation evidence: ECO:0000269; organism taxon: NCBITaxon:83333.

    Source locationcomments[commentType='CATALYTIC ACTIVITY'].reaction.reactionCrossReferences
D-glucosamine 6-phosphate
CHEBI:58725		inhibits

N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18
  • UniProtKB:P0AF18

    Source assertion: UniProt activity-regulation annotation: Inhibited by high substrate concentration and by products glucosamine 6-phosphate and acetate. Completely inactivated by the treatment with 5,5'-dithio-bis(2-nitrobenzoate) or 2,2'-dithio-pyridine (2-DPDS). Inhibited by 1,10-phenanthroline and EDTA

    Source locationcomments[commentType='ACTIVITY REGULATION'].texts
acetate
CHEBI:30089		inhibits

N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18
  • UniProtKB:P0AF18

    Source assertion: UniProt activity-regulation annotation: Inhibited by high substrate concentration and by products glucosamine 6-phosphate and acetate. Completely inactivated by the treatment with 5,5'-dithio-bis(2-nitrobenzoate) or 2,2'-dithio-pyridine (2-DPDS). Inhibited by 1,10-phenanthroline and EDTA

    Source locationcomments[commentType='ACTIVITY REGULATION'].texts
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

zinc(2+)
CHEBI:29105
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:29105 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

cobalt(2+)
CHEBI:48828
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:48828 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

manganese(2+)
CHEBI:29035
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:29035 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

cadmium(2+)
CHEBI:48775
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:48775 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

iron(2+)
CHEBI:29033
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:29033 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note
N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0AF18		has_cofactor

nickel(2+)
CHEBI:49786
  • UniProtKB:P0AF18

    Source assertion: UniProt lists CHEBI:49786 as a cofactor of UniProtKB:P0AF18 (evidence: ECO:0000269). Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).

    Source locationcomments[commentType='COFACTOR'].cofactors and note

References

Curation history