superpathway of N-acetylglucosamine, N-acetylmannosamine and N-acetylneuraminate degradation

MetaCyc:GLCMANNANAUT-PWY

Complete META 27.0 two-child, six-core-reaction amino-sugar degradation pathway, scoped here to E. coli K-12 evidence. NanQ ring opening feeds NanA, NanK and NanE, then NagA and NagB produce fructose 6-phosphate; alpha ring opening is a supported alternative. Neu5Ac/NanT, ManNAc/ManXYZ PTS and GlcNAc/NagE or ManXYZ PTS supply the three entry contexts. Native assemblies, alternative metal cofactors and transcriptional control are retained. Ser1-NagB regulatory assays carry explicit construct qualifiers. Generic transport pools and anomer-specific core species remain distinct. BiGG ManNAc identities retain their native model scope: the substrate InChIKey conflicts with ChEBI:17122, so no exact cross-database alias or intervening stereochemical conversion is asserted. The coupled ManNAc PTS and shared PTS phosphorylation reaction are overlapping descriptions, not additive net stoichiometry. The glycolysis link is an opaque downstream interface. PathBank SMP0002044 is a related conflicting definition lacking NanQ, not an exact identifier synonym.

Pathway type

carbohydrate degradation

Organism scope

Escherichia coli K-12 NCBITaxon:83333

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Pathway network

85 nodes · 114 asserted directed edges

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Escherichia coli K-12 `NCBITaxon:83333`	taxon
N-acetylneuraminate lyase `UniProtKB:P0A6L4`	protein
N-acetylmannosamine kinase `UniProtKB:P45425`	protein
N-acetylmannosamine-6-phosphate 2-epimerase `UniProtKB:P0A761`	protein
N-acetylglucosamine-6-phosphate deacetylase `UniProtKB:P0AF18`	protein
Glucosamine-6-phosphate deaminase `UniProtKB:P0A759`	protein
N-acetylneuraminate anomerase NanQ `UniProtKB:P45424`	protein
Sialic acid transporter NanT `UniProtKB:P41036`	protein
HTH-type transcriptional repressor NanR `UniProtKB:P0A8W0`	protein
DNA-binding transcriptional repressor Mlc `UniProtKB:P50456`	protein
PTS system mannose-specific EIIC component `UniProtKB:P69801`	protein
PTS system mannose-specific EIID component `UniProtKB:P69805`	protein
PTS system mannose-specific EIIAB component `UniProtKB:P69797`	protein
PTS system N-acetylglucosamine-specific EIICBA component `UniProtKB:P09323`	protein
Phosphoenolpyruvate-protein phosphotransferase `UniProtKB:P08839`	protein
Nitrogen regulatory protein P-II 1 `UniProtKB:P0A9Z1`	protein
DNA-binding transcriptional dual regulator NagC `UniProtKB:P0AF20`	protein
DNA-binding transcriptional dual regulator CRP `UniProtKB:P0ACJ8`	protein
N-acetyl-alpha-neuraminate `CHEBI:58770`	small molecule
aceneuramate `CHEBI:173083`	small molecule
N-acetyl-beta-neuraminate `CHEBI:58705`	small molecule
aldehydo-N-acetyl-D-mannosamine `CHEBI:17122`	small molecule
pyruvate `CHEBI:15361`	small molecule
ATP `CHEBI:30616`	small molecule
aldehydo-N-acetyl-D-mannosamine 6-phosphate `CHEBI:58557`	small molecule
ADP `CHEBI:456216`	small molecule
H(+) `CHEBI:15378`	small molecule
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
N-acetylneuraminate `CHEBI:35418`	small molecule
N(pros)-phospho-L-histidyl-[protein] `RHEA-COMP:9746`	protein
N-acetyl-D-glucosamine `CHEBI:506227`	small molecule
L-histidyl-[protein] `RHEA-COMP:9745`	protein
phosphoenolpyruvate `CHEBI:58702`	small molecule
N-Acetyl-D-mannosamine `BiGG:acmana`	small molecule
N-Acetyl-D-mannosamine 6-phosphate `BiGG:acmanap`	small molecule
N-acetylneuraminate lyase `MetaCyc:ACNEULY-CPLX`	complex
N-acetylmannosamine kinase `MetaCyc:CPLX0-8588`	complex
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	complex
glucosamine-6-phosphate deaminase `MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX`	complex
PTS enzyme I `MetaCyc:CPLX0-7938`	complex
mannose-specific PTS enzyme IIAB component `MetaCyc:CPLX0-7921`	complex
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	complex
N-acetylglucosamine-specific PTS enzyme II `MetaCyc:CPLX-167`	complex
nitrogen regulatory protein PII-1 `MetaCyc:PIIPROTEIN-CPLX`	complex
phosphocarrier protein HPr `MetaCyc:PTSH-MONOMER`	protein
phosphocarrier HPr-Nπ-phospho-L-histidine `MetaCyc:PTSH-PHOSPHORYLATED`	protein
uridylyl-[protein PII] `MetaCyc:URIDYLYL-PII`	protein
uridylyl-[protein PII-1] `MetaCyc:CPLX0-8568`	complex
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
magnesium(2+) `CHEBI:18420`	cofactor
3',5'-cyclic AMP(1-) `CHEBI:58165`	small molecule
CRP-cyclic-AMP DNA-binding transcriptional dual regulator `EcoCyc:CPLX0-226`	complex
small regulatory RNA SgrS `EcoCyc:RNA0-241`	rna
DNA-binding transcriptional dual regulator CRP `EcoCyc:PC00004`	complex
N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	pathway
N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	pathway
glycolysis I (from glucose 6-phosphate) `MetaCyc:GLYCOLYSIS`	pathway
N-acetyl-alpha-neuraminate => aceneuramate `RHEA:67737`	reaction	left to right
N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	reaction	left to right
aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	reaction	left to right
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	reaction	left to right
aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	reaction	right to left
N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	reaction	left to right
alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	reaction	left to right
N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	reaction	right to left
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	reaction	left to right
L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	reaction	left to right
N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	reaction	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
`MetaCyc:GLCMANNANAUT-PWY`	has_part	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	MetaCyc:GLCMANNANAUT-PWY Source assertion: META 27.0 lists PWY0-1324 as a complete child pathway of this superpathway. Source location `Pathway/reaction-list and Pathway/sub-pathways`
`MetaCyc:GLCMANNANAUT-PWY`	has_part	N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	MetaCyc:GLCMANNANAUT-PWY Source assertion: META 27.0 lists GLUAMCAT-PWY as a complete child pathway of this superpathway. Source location `Pathway/reaction-list and Pathway/sub-pathways`
N-acetyl-alpha-neuraminate `CHEBI:58770`	consumes	N-acetyl-alpha-neuraminate => aceneuramate `RHEA:67737`	RHEA:67737 Source assertion: Rhea release 142 places CHEBI:58770 with coefficient 1 on the substrates side of RHEA:67737. Its directional object is left_to_right relative to master RHEA:67736. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/67737"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-alpha-neuraminate => aceneuramate `RHEA:67737`	produces	aceneuramate `CHEBI:173083`	RHEA:67737 Source assertion: Rhea release 142 places CHEBI:173083 with coefficient 1 on the products side of RHEA:67737. Its directional object is left_to_right relative to master RHEA:67736. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/67737"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-beta-neuraminate `CHEBI:58705`	consumes	N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	RHEA:67741 Source assertion: Rhea release 142 places CHEBI:58705 with coefficient 1 on the substrates side of RHEA:67741. Its directional object is left_to_right relative to master RHEA:67740. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/67741"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	produces	aceneuramate `CHEBI:173083`	RHEA:67741 Source assertion: Rhea release 142 places CHEBI:173083 with coefficient 1 on the products side of RHEA:67741. Its directional object is left_to_right relative to master RHEA:67740. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/67741"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	part_of	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	MetaCyc:PWY0-1324 Source assertion: The native child includes RXN0-7389; reaction layout and corresponding Rhea sides establish this degradation direction. RXN0-7389 uses native right-to-left ring opening; NANE-RXN maps to Rhea right-to-left. Source location `Pathway/reaction-list, reaction-layout and reaction-ordering`
aceneuramate `CHEBI:173083`	consumes	aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	RHEA:23297 Source assertion: Rhea release 142 places CHEBI:173083 with coefficient 1 on the substrates side of RHEA:23297. Its directional object is left_to_right relative to master RHEA:23296. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23297"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	produces	aldehydo-N-acetyl-D-mannosamine `CHEBI:17122`	RHEA:23297 Source assertion: Rhea release 142 places CHEBI:17122 with coefficient 1 on the products side of RHEA:23297. Its directional object is left_to_right relative to master RHEA:23296. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23297"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	produces	pyruvate `CHEBI:15361`	RHEA:23297 Source assertion: Rhea release 142 places CHEBI:15361 with coefficient 1 on the products side of RHEA:23297. Its directional object is left_to_right relative to master RHEA:23296. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23297"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	part_of	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	MetaCyc:PWY0-1324 Source assertion: The native child includes RXN0-7390; reaction layout and corresponding Rhea sides establish this degradation direction. RXN0-7389 uses native right-to-left ring opening; NANE-RXN maps to Rhea right-to-left. Source location `Pathway/reaction-list, reaction-layout and reaction-ordering`
aldehydo-N-acetyl-D-mannosamine `CHEBI:17122`	consumes	aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	RHEA:25254 Source assertion: Rhea release 142 places CHEBI:17122 with coefficient 1 on the substrates side of RHEA:25254. Its directional object is left_to_right relative to master RHEA:25253. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25254"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
ATP `CHEBI:30616`	consumes	aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	RHEA:25254 Source assertion: Rhea release 142 places CHEBI:30616 with coefficient 1 on the substrates side of RHEA:25254. Its directional object is left_to_right relative to master RHEA:25253. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25254"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	produces	aldehydo-N-acetyl-D-mannosamine 6-phosphate `CHEBI:58557`	RHEA:25254 Source assertion: Rhea release 142 places CHEBI:58557 with coefficient 1 on the products side of RHEA:25254. Its directional object is left_to_right relative to master RHEA:25253. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25254"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	produces	ADP `CHEBI:456216`	RHEA:25254 Source assertion: Rhea release 142 places CHEBI:456216 with coefficient 1 on the products side of RHEA:25254. Its directional object is left_to_right relative to master RHEA:25253. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25254"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	produces	H(+) `CHEBI:15378`	RHEA:25254 Source assertion: Rhea release 142 places CHEBI:15378 with coefficient 1 on the products side of RHEA:25254. Its directional object is left_to_right relative to master RHEA:25253. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25254"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	part_of	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	MetaCyc:PWY0-1324 Source assertion: The native child includes NANK-RXN; reaction layout and corresponding Rhea sides establish this degradation direction. RXN0-7389 uses native right-to-left ring opening; NANE-RXN maps to Rhea right-to-left. Source location `Pathway/reaction-list, reaction-layout and reaction-ordering`
aldehydo-N-acetyl-D-mannosamine 6-phosphate `CHEBI:58557`	consumes	aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	RHEA:25259 Source assertion: Rhea release 142 places CHEBI:58557 with coefficient 1 on the substrates side of RHEA:25259. Its directional object is right_to_left relative to master RHEA:25257. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25259"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	produces	N-acetyl-D-glucosamine 6-phosphate `CHEBI:57513`	RHEA:25259 Source assertion: Rhea release 142 places CHEBI:57513 with coefficient 1 on the products side of RHEA:25259. Its directional object is right_to_left relative to master RHEA:25257. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/25259"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	part_of	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	MetaCyc:PWY0-1324 Source assertion: The native child includes NANE-RXN; reaction layout and corresponding Rhea sides establish this degradation direction. RXN0-7389 uses native right-to-left ring opening; NANE-RXN maps to Rhea right-to-left. Source location `Pathway/reaction-list, reaction-layout and reaction-ordering`
N-acetyl-D-glucosamine 6-phosphate `CHEBI:57513`	consumes	N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	RHEA:22937 Source assertion: Rhea release 142 places CHEBI:57513 with coefficient 1 on the substrates side of RHEA:22937. Its directional object is left_to_right relative to master RHEA:22936. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/22937"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
H2O `CHEBI:15377`	consumes	N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	RHEA:22937 Source assertion: Rhea release 142 places CHEBI:15377 with coefficient 1 on the substrates side of RHEA:22937. Its directional object is left_to_right relative to master RHEA:22936. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/22937"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	produces	D-glucosamine 6-phosphate `CHEBI:58725`	RHEA:22937 Source assertion: Rhea release 142 places CHEBI:58725 with coefficient 1 on the products side of RHEA:22937. Its directional object is left_to_right relative to master RHEA:22936. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/22937"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	produces	acetate `CHEBI:30089`	RHEA:22937 Source assertion: Rhea release 142 places CHEBI:30089 with coefficient 1 on the products side of RHEA:22937. Its directional object is left_to_right relative to master RHEA:22936. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/22937"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	part_of	N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	MetaCyc:GLUAMCAT-PWY Source assertion: The child pathway contains sequential NAG6PDEACET-RXN and GLUCOSAMINE-6-P-DEAMIN-RXN in their degradation directions. Source location `Pathway/reaction-list and reaction-layout`
alpha-D-glucosamine 6-phosphate `CHEBI:75989`	consumes	alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	RHEA:12173 Source assertion: Rhea release 142 places CHEBI:75989 with coefficient 1 on the substrates side of RHEA:12173. Its directional object is left_to_right relative to master RHEA:12172. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/12173"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
H2O `CHEBI:15377`	consumes	alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	RHEA:12173 Source assertion: Rhea release 142 places CHEBI:15377 with coefficient 1 on the substrates side of RHEA:12173. Its directional object is left_to_right relative to master RHEA:12172. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/12173"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	produces	beta-D-fructose 6-phosphate `CHEBI:57634`	RHEA:12173 Source assertion: Rhea release 142 places CHEBI:57634 with coefficient 1 on the products side of RHEA:12173. Its directional object is left_to_right relative to master RHEA:12172. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/12173"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	produces	NH4(+) `CHEBI:28938`	RHEA:12173 Source assertion: Rhea release 142 places CHEBI:28938 with coefficient 1 on the products side of RHEA:12173. Its directional object is left_to_right relative to master RHEA:12172. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/12173"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	part_of	N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	MetaCyc:GLUAMCAT-PWY Source assertion: The child pathway contains sequential NAG6PDEACET-RXN and GLUCOSAMINE-6-P-DEAMIN-RXN in their degradation directions. Source location `Pathway/reaction-list and reaction-layout`
N-acetylneuraminate `CHEBI:35418`	consumes	N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	RHEA:28989 Source assertion: Rhea release 142 places CHEBI:35418 with coefficient 1 on the substrates side of RHEA:28989. Its directional object is right_to_left relative to master RHEA:28987. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/28989"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
H(+) `CHEBI:15378`	consumes	N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	RHEA:28989 Source assertion: Rhea release 142 places CHEBI:15378 with coefficient 1 on the substrates side of RHEA:28989. Its directional object is right_to_left relative to master RHEA:28987. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/28989"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	produces	N-acetylneuraminate `CHEBI:35418`	RHEA:28989 Source assertion: Rhea release 142 places CHEBI:35418 with coefficient 1 on the products side of RHEA:28989. Its directional object is right_to_left relative to master RHEA:28987. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/28989"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	produces	H(+) `CHEBI:15378`	RHEA:28989 Source assertion: Rhea release 142 places CHEBI:15378 with coefficient 1 on the products side of RHEA:28989. Its directional object is right_to_left relative to master RHEA:28987. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/28989"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N(pros)-phospho-L-histidyl-[protein] `RHEA-COMP:9746`	consumes	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	RHEA:49241 Source assertion: Rhea release 142 places RHEA-COMP:9746 with coefficient 1 on the substrates side of RHEA:49241. Its directional object is left_to_right relative to master RHEA:49240. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/49241"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-acetyl-D-glucosamine `CHEBI:506227`	consumes	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	RHEA:49241 Source assertion: Rhea release 142 places CHEBI:506227 with coefficient 1 on the substrates side of RHEA:49241. Its directional object is left_to_right relative to master RHEA:49240. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/49241"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	produces	N-acetyl-D-glucosamine 6-phosphate `CHEBI:57513`	RHEA:49241 Source assertion: Rhea release 142 places CHEBI:57513 with coefficient 1 on the products side of RHEA:49241. Its directional object is left_to_right relative to master RHEA:49240. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/49241"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	produces	L-histidyl-[protein] `RHEA-COMP:9745`	RHEA:49241 Source assertion: Rhea release 142 places RHEA-COMP:9745 with coefficient 1 on the products side of RHEA:49241. Its directional object is left_to_right relative to master RHEA:49240. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/49241"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
L-histidyl-[protein] `RHEA-COMP:9745`	consumes	L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	RHEA:23881 Source assertion: Rhea release 142 places RHEA-COMP:9745 with coefficient 1 on the substrates side of RHEA:23881. Its directional object is left_to_right relative to master RHEA:23880. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23881"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
phosphoenolpyruvate `CHEBI:58702`	consumes	L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	RHEA:23881 Source assertion: Rhea release 142 places CHEBI:58702 with coefficient 1 on the substrates side of RHEA:23881. Its directional object is left_to_right relative to master RHEA:23880. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23881"]/rh:substrates; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	produces	N(pros)-phospho-L-histidyl-[protein] `RHEA-COMP:9746`	RHEA:23881 Source assertion: Rhea release 142 places RHEA-COMP:9746 with coefficient 1 on the products side of RHEA:23881. Its directional object is left_to_right relative to master RHEA:23880. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23881"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	produces	pyruvate `CHEBI:15361`	RHEA:23881 Source assertion: Rhea release 142 places CHEBI:15361 with coefficient 1 on the products side of RHEA:23881. Its directional object is left_to_right relative to master RHEA:23880. Source location `rdf:Description[@rdf:about="http://rdf.rhea-db.org/23881"]/rh:products; rh:contains and coefficient predicate rh:contains1; rh:compound/rh:accession`
N-Acetyl-D-mannosamine `BiGG:acmana`	consumes	N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	BiGG:ACMANAptspp Source assertion: iML1515 assigns acmana_p (p compartment) coefficient -1; lower_bound=0 and upper_bound=1000 permit the written uptake direction. This is the coupled PEP-dependent transport reaction, not an elementary phosphoryl transfer. Source location `iML1515/reactions[id=ACMANAptspp]/metabolites/acmana_p; bounds; metabolites[id=acmana_p]` BiGG:acmana Source assertion: The native substrate annotation gives InChIKey MBLBDJOUHNCFQT-XAMCCFCMSA-N and multiple ChEBI cross-references. This model compound is retained without an exact ChEBI alias; the cross-references do not resolve their conflicting structural scope. Source location `Universal metabolite database_links[InChI Key, CHEBI]; iML1515/metabolites[id=acmana_p]/annotation` CHEBI:17122 Source assertion: The issuing ChEBI SQL record gives MBLBDJOUHNCFQT-WCTZXXKLSA-N. Its different stereochemical hash block prevents equating this exact aldehydo species to the BiGG substrate annotation. No conversion between these structures is inferred. Source location `ChEBI release 255 statements[subject=CHEBI:17122,predicate=chemrof:inchi_key_string]`
N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	produces	N-Acetyl-D-mannosamine 6-phosphate `BiGG:acmanap`	BiGG:ACMANAptspp Source assertion: iML1515 assigns acmanap_c (c compartment) coefficient 1; lower_bound=0 and upper_bound=1000 permit the written uptake direction. This is the coupled PEP-dependent transport reaction, not an elementary phosphoryl transfer. Source location `iML1515/reactions[id=ACMANAptspp]/metabolites/acmanap_c; bounds; metabolites[id=acmanap_c]`
phosphoenolpyruvate `CHEBI:58702`	consumes	N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	BiGG:ACMANAptspp Source assertion: iML1515 assigns pep_c (c compartment) coefficient -1; lower_bound=0 and upper_bound=1000 permit the written uptake direction. This is the coupled PEP-dependent transport reaction, not an elementary phosphoryl transfer. Source location `iML1515/reactions[id=ACMANAptspp]/metabolites/pep_c; bounds; metabolites[id=pep_c]`
N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	produces	pyruvate `CHEBI:15361`	BiGG:ACMANAptspp Source assertion: iML1515 assigns pyr_c (c compartment) coefficient 1; lower_bound=0 and upper_bound=1000 permit the written uptake direction. This is the coupled PEP-dependent transport reaction, not an elementary phosphoryl transfer. Source location `iML1515/reactions[id=ACMANAptspp]/metabolites/pyr_c; bounds; metabolites[id=pyr_c]`
N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	PMID:9864311 Source assertion: Extracellular ManNAc enters through ManXYZ-dependent PTS uptake and phosphorylation. Rapid growth in the tested K-12 backgrounds required mlc/nanR derepression; this is an entry route to the complete superpathway. Source location `PMC103530, Results, Transport and phosphorylation of ManNAc; Table 1 and Fig. 1`
N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The superpathway definition explicitly includes transport and convergence of neuraminate, mannosamine and glucosamine acetylated amino sugars at N-acetylglucosamine 6-phosphate. Individual transport chemistry is separately grounded. Source location `Pathway/comment; Plumbridge99`
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The superpathway definition explicitly includes transport and convergence of neuraminate, mannosamine and glucosamine acetylated amino sugars at N-acetylglucosamine 6-phosphate. Individual transport chemistry is separately grounded. Source location `Pathway/comment; Plumbridge99`
N-acetylneuraminate lyase `MetaCyc:ACNEULY-CPLX`	has_part	N-acetylneuraminate lyase `UniProtKB:P0A6L4`	MetaCyc:ACNEULY-CPLX Source assertion: META 27.0 assigns component ACNEULY-MONOMER coefficient 4. Source location `Protein[@frameid="ACNEULY-CPLX"]/component[Protein/@frameid="ACNEULY-MONOMER"]/coefficient` UniProtKB:P0A6L4 Source assertion: The reviewed protein entry cross-references native ACNEULY-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
N-acetylmannosamine kinase `MetaCyc:CPLX0-8588`	has_part	N-acetylmannosamine kinase `UniProtKB:P45425`	MetaCyc:CPLX0-8588 Source assertion: META 27.0 assigns component NANK-MONOMER coefficient 2. Source location `Protein[@frameid="CPLX0-8588"]/component[Protein/@frameid="NANK-MONOMER"]/coefficient` UniProtKB:P45425 Source assertion: The reviewed protein entry cross-references native NANK-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_part	N-acetylglucosamine-6-phosphate deacetylase `UniProtKB:P0AF18`	MetaCyc:NAG6PDEACET-CPLX Source assertion: META 27.0 assigns component NAG6PDEACET-MONOMER coefficient 4. Source location `Protein[@frameid="NAG6PDEACET-CPLX"]/component[Protein/@frameid="NAG6PDEACET-MONOMER"]/coefficient` UniProtKB:P0AF18 Source assertion: The reviewed protein entry cross-references native NAG6PDEACET-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]` PMID:17567047 Source assertion: Purified E. coli NagA behaved as a tetramer in the presence of disulfide reducing agents; the primary experiment does not claim that disulfides are required for the native assembly. Source location `PMC2533526, Results and Discussion S15`
glucosamine-6-phosphate deaminase `MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX`	has_part	Glucosamine-6-phosphate deaminase `UniProtKB:P0A759`	MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX Source assertion: META 27.0 assigns component GLUCOSAMINE-6-P-DEAMIN-MONOMER coefficient 6. Source location `Protein[@frameid="GLUCOSAMINE-6-P-DEAMIN-CPLX"]/component[Protein/@frameid="GLUCOSAMINE-6-P-DEAMIN-MONOMER"]/coefficient` UniProtKB:P0A759 Source assertion: The reviewed protein entry cross-references native GLUCOSAMINE-6-P-DEAMIN-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]` PMID:8240271 Source assertion: The abstract describes a hexamer arranged as a trimer of dimers; Cys-to-Ser variants lacking the interchain disulfide remain stable hexamers. Full scanned article access failed, so no further full-text claim is made. Source location `Primary abstract; PMC1134607 abstract1`
PTS enzyme I `MetaCyc:CPLX0-7938`	has_part	Phosphoenolpyruvate-protein phosphotransferase `UniProtKB:P08839`	MetaCyc:CPLX0-7938 Source assertion: META 27.0 assigns component PTSI-MONOMER coefficient 2. Source location `Protein[@frameid="CPLX0-7938"]/component[Protein/@frameid="PTSI-MONOMER"]/coefficient` UniProtKB:P08839 Source assertion: The reviewed protein entry cross-references native PTSI-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
mannose-specific PTS enzyme IIAB component `MetaCyc:CPLX0-7921`	has_part	PTS system mannose-specific EIIAB component `UniProtKB:P69797`	MetaCyc:CPLX0-7921 Source assertion: META 27.0 assigns component MANX-MONOMER coefficient 2. Source location `Protein[@frameid="CPLX0-7921"]/component[Protein/@frameid="MANX-MONOMER"]/coefficient` UniProtKB:P69797 Source assertion: The reviewed protein entry cross-references native MANX-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	has_part	PTS system mannose-specific EIID component `UniProtKB:P69805`	MetaCyc:CPLX-165 Source assertion: META 27.0 assigns component MANZ-MONOMER coefficient 3. Source location `Protein[@frameid="CPLX-165"]/component[Protein/@frameid="MANZ-MONOMER"]/coefficient` UniProtKB:P69805 Source assertion: The reviewed protein entry cross-references native MANZ-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]` PMID:31209249 Source assertion: Cryo-EM resolves a ManYZ trimer with one ManY and one ManZ per protomer. The isolated structural assembly does not include ManX and does not fix complete ManXYZ stoichiometry. Source location `PMC6796895, main letter paragraphs beginning In this study and The structure of ManYZ; Fig. 1a/b`
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	has_part	PTS system mannose-specific EIIC component `UniProtKB:P69801`	MetaCyc:CPLX-165 Source assertion: META 27.0 assigns component MANY-MONOMER coefficient 3. Source location `Protein[@frameid="CPLX-165"]/component[Protein/@frameid="MANY-MONOMER"]/coefficient` UniProtKB:P69801 Source assertion: The reviewed protein entry cross-references native MANY-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]` PMID:31209249 Source assertion: Cryo-EM resolves a ManYZ trimer with one ManY and one ManZ per protomer. The isolated structural assembly does not include ManX and does not fix complete ManXYZ stoichiometry. Source location `PMC6796895, main letter paragraphs beginning In this study and The structure of ManYZ; Fig. 1a/b`
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	has_part	PTS system mannose-specific EIIAB component `UniProtKB:P69797`	MetaCyc:CPLX-165 Source assertion: META 27.0 assigns component MANX-MONOMER coefficient 1. ManYZ cryo-EM resolves three Y/Z pairs without ManX; native ManX also has a separately annotated dimer. Do not infer a reconciled full-complex stoichiometry. Source location `Protein[@frameid="CPLX-165"]/component[Protein/@frameid="MANX-MONOMER"]/coefficient` UniProtKB:P69797 Source assertion: The reviewed protein entry cross-references native MANX-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
N-acetylglucosamine-specific PTS enzyme II `MetaCyc:CPLX-167`	has_part	PTS system N-acetylglucosamine-specific EIICBA component `UniProtKB:P09323`	MetaCyc:CPLX-167 Source assertion: META 27.0 assigns component NAGE-MONOMER coefficient 2. Source location `Protein[@frameid="CPLX-167"]/component[Protein/@frameid="NAGE-MONOMER"]/coefficient` UniProtKB:P09323 Source assertion: The reviewed protein entry cross-references native NAGE-MONOMER; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
nitrogen regulatory protein PII-1 `MetaCyc:PIIPROTEIN-CPLX`	has_part	Nitrogen regulatory protein P-II 1 `UniProtKB:P0A9Z1`	MetaCyc:PIIPROTEIN-CPLX Source assertion: META 27.0 assigns component PROTEIN-PII coefficient 3. Source location `Protein[@frameid="PIIPROTEIN-CPLX"]/component[Protein/@frameid="PROTEIN-PII"]/coefficient` UniProtKB:P0A9Z1 Source assertion: The reviewed protein entry cross-references native PROTEIN-PII; this identifies the corresponding polypeptide without altering the native assembly coefficient. Source location `uniProtKBCrossReferences[database=BioCyc]`
nitrogen regulatory protein PII-1 `MetaCyc:PIIPROTEIN-CPLX`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	UniProtKB:P0A9Z1 Source assertion: GlnB is a homotrimer. Its uridylylation state controls the separately qualified NagB assays; this native assembly node does not imply an occupancy or assembly for those preparations. Source location `comments[commentType=SUBUNIT]; PMID:29229699 methods sec4-6`
uridylyl-[protein PII-1] `MetaCyc:CPLX0-8568`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	MetaCyc:CPLX0-8568 Source assertion: The native modified PII-1 complex has unmodified-form PIIPROTEIN-CPLX, but this original gives no component coefficients or uridylylation occupancy. It is retained as state context, not equated to an assay preparation. Source location `Protein/unmodified-form; common-name; absence of direct component slots`
N-acetylneuraminate lyase `MetaCyc:ACNEULY-CPLX`	catalyzes	aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	MetaCyc:ACNEULY-CPLX Source assertion: The exact native complex catalyzes an Enzymatic-Reaction with an enzyme back-reference to this frame and reaction RXN0-7390. The represented Rhea direction is the independently resolved degradation direction. Source location `Protein/catalyzes/Enzymatic-Reaction/{enzyme,reaction}`
N-acetylmannosamine kinase `MetaCyc:CPLX0-8588`	catalyzes	aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	MetaCyc:CPLX0-8588 Source assertion: The exact native complex catalyzes an Enzymatic-Reaction with an enzyme back-reference to this frame and reaction NANK-RXN. The represented Rhea direction is the independently resolved degradation direction. Source location `Protein/catalyzes/Enzymatic-Reaction/{enzyme,reaction}`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	catalyzes	N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	MetaCyc:NAG6PDEACET-CPLX Source assertion: The exact native complex catalyzes an Enzymatic-Reaction with an enzyme back-reference to this frame and reaction NAG6PDEACET-RXN. The represented Rhea direction is the independently resolved degradation direction. Source location `Protein/catalyzes/Enzymatic-Reaction/{enzyme,reaction}`
glucosamine-6-phosphate deaminase `MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX`	catalyzes	alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX Source assertion: The exact native complex catalyzes an Enzymatic-Reaction with an enzyme back-reference to this frame and reaction GLUCOSAMINE-6-P-DEAMIN-RXN. The represented Rhea direction is the independently resolved degradation direction. Source location `Protein/catalyzes/Enzymatic-Reaction/{enzyme,reaction}`
N-acetylneuraminate anomerase NanQ `UniProtKB:P45424`	catalyzes	N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	UniProtKB:P45424 Source assertion: NanQ opens both beta- and alpha-Neu5Ac to aceneuramate and favors the beta anomer. The alpha route is a supported alternative beyond the native beta ring-opening step. Source location `comments[commentType=FUNCTION], ECO:0000269 PMID:33895133` PMID:33895133 Source assertion: NanQ accelerates anomer opening to the linear substrate preferred by NanA. Growth defects of the knockout are conditional on assay temperature/pH; they do not establish universal essentiality. Source location `PMC8141875, Results and Discussion, anomerase assays and mutant growth experiments`
N-acetylneuraminate anomerase NanQ `UniProtKB:P45424`	catalyzes	N-acetyl-alpha-neuraminate => aceneuramate `RHEA:67737`	UniProtKB:P45424 Source assertion: NanQ opens both beta- and alpha-Neu5Ac to aceneuramate and favors the beta anomer. The alpha route is a supported alternative beyond the native beta ring-opening step. Source location `comments[commentType=FUNCTION], ECO:0000269 PMID:33895133` PMID:33895133 Source assertion: NanQ accelerates anomer opening to the linear substrate preferred by NanA. Growth defects of the knockout are conditional on assay temperature/pH; they do not establish universal essentiality. Source location `PMC8141875, Results and Discussion, anomerase assays and mutant growth experiments`
N-acetylmannosamine-6-phosphate 2-epimerase `UniProtKB:P0A761`	catalyzes	aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	UniProtKB:P0A761 Source assertion: K-12 NanE is annotated as probable ManNAc6P-to-GlcNAc6P epimerase, ECO:0000305 from PMID:9864311. The homodimer annotation comes from HAMAP MF_01235, ECO:0000255, not purified K-12 assembly measurements. Source location `comments[commentType=FUNCTION or SUBUNIT]`
Sialic acid transporter NanT `UniProtKB:P41036`	catalyzes	N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	UniProtKB:P41036 Source assertion: NanT mediates proton-dependent reversible sialic-acid transport. The imported direction shown serves catabolism; the Rhea formal one-proton equation is not a measured coupling stoichiometry. Source location `comments[commentType=FUNCTION], PMID:22167185` PMID:22167185 Source assertion: E. coli K-12 NanT was reconstituted as a proton-driven transporter capable of counterflow; this differs from the sodium-driven TRAP transporter comparators. Source location `PMC3271013, Results, NanT proton-dependence and counterflow experiments`
N-acetylglucosamine-specific PTS enzyme II `MetaCyc:CPLX-167`	catalyzes	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	MetaCyc:CPLX-167 Source assertion: Native catalyzes links include N-acetyl-D-glucosamine PTS permease activity. Transport phosphorylates incoming GlcNAc through the PTS relay; the Rhea histidyl-protein participants are formal generic states. Source location `Protein/catalyzes/Enzymatic-Reaction` PMID:9864311 Source assertion: GlcNAc uptake/phosphorylation can use NagE or the broad-specificity ManXYZ PTS. These alternatives must not be generalized to ManNAc: nagE and ptsG did not replace ManXYZ for that tested substrate. Source location `PMC103530, Introduction and Results, Table 1`
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	catalyzes	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	MetaCyc:CPLX-165 Source assertion: Native catalyzes links include N-acetyl-D-glucosamine PTS permease activity. Transport phosphorylates incoming GlcNAc through the PTS relay; the Rhea histidyl-protein participants are formal generic states. Source location `Protein/catalyzes/Enzymatic-Reaction` PMID:9864311 Source assertion: GlcNAc uptake/phosphorylation can use NagE or the broad-specificity ManXYZ PTS. These alternatives must not be generalized to ManNAc: nagE and ptsG did not replace ManXYZ for that tested substrate. Source location `PMC103530, Introduction and Results, Table 1`
PTS enzyme I `MetaCyc:CPLX0-7938`	catalyzes	L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	UniProtKB:P08839 Source assertion: Enzyme I transfers a phosphoryl group from PEP to HPr. The Rhea equation uses generic histidyl-protein states; the native enzyme is a homodimer and Mg2+-dependent. Source location `comments[commentType=FUNCTION, SUBUNIT, COFACTOR]`
mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	enables	N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	BiGG:ACMANAptspp Source assertion: The exact MG1655 iML1515 gene rule requires ptsH b2415, ptsI b2416, manX b1817, manY b1818 and manZ b1819 for the coupled ManNAc PTS reaction. Native subunits/assemblies are grounded separately. Source location `reactions[id=ACMANAptspp]/gene_reaction_rule; genes[id=b2415,b2416,b1817,b1818,b1819]`
PTS enzyme I `MetaCyc:CPLX0-7938`	enables	N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	BiGG:ACMANAptspp Source assertion: The exact MG1655 iML1515 gene rule requires ptsH b2415, ptsI b2416, manX b1817, manY b1818 and manZ b1819 for the coupled ManNAc PTS reaction. Native subunits/assemblies are grounded separately. Source location `reactions[id=ACMANAptspp]/gene_reaction_rule; genes[id=b2415,b2416,b1817,b1818,b1819]`
phosphocarrier protein HPr `MetaCyc:PTSH-MONOMER`	enables	N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	BiGG:ACMANAptspp Source assertion: The exact MG1655 iML1515 gene rule requires ptsH b2415, ptsI b2416, manX b1817, manY b1818 and manZ b1819 for the coupled ManNAc PTS reaction. Native subunits/assemblies are grounded separately. Source location `reactions[id=ACMANAptspp]/gene_reaction_rule; genes[id=b2415,b2416,b1817,b1818,b1819]`
phosphocarrier HPr-Nπ-phospho-L-histidine `MetaCyc:PTSH-PHOSPHORYLATED`	enables	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	MetaCyc:PTSH-MONOMER Source assertion: The native PTS relay transfers phosphate from enzyme I through HPr His15 and sugar-specific EII domains to the transported sugar; the phosphorylated HPr state is native PTSH-PHOSPHORYLATED. Source location `Protein/comment; modified-form`
mannose-specific PTS enzyme IIAB component `MetaCyc:CPLX0-7921`	part_of	`MetaCyc:GLCMANNANAUT-PWY`	MetaCyc:CPLX0-7921 Source assertion: ManX IIAB is separately represented as a homodimer; no direct has_part relation to a full ManXYZ assembly is inferred from the inconsistent granularity of the native complex frames. Source location `Protein/component and common-name`
N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	provides_input_for	aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The complete native degradation route orders these reactions; the alternative alpha ring-opening reaction is supported by the NanQ primary assays and converges on the same linear NanA substrate. Source location `Pathway/reaction-ordering; child PWY0-1324 and GLUAMCAT-PWY reaction-ordering` PMID:33895133 Source assertion: The linear product of NanQ is the preferred NanA substrate; the supported alpha and beta inputs converge before downstream sugar catabolism. Source location `PMC8141875, Results and Discussion`
N-acetyl-alpha-neuraminate => aceneuramate `RHEA:67737`	provides_input_for	aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The complete native degradation route orders these reactions; the alternative alpha ring-opening reaction is supported by the NanQ primary assays and converges on the same linear NanA substrate. Source location `Pathway/reaction-ordering; child PWY0-1324 and GLUAMCAT-PWY reaction-ordering` PMID:33895133 Source assertion: The linear product of NanQ is the preferred NanA substrate; the supported alpha and beta inputs converge before downstream sugar catabolism. Source location `PMC8141875, Results and Discussion`
aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate `RHEA:23297`	provides_input_for	aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The complete native degradation route orders these reactions; the alternative alpha ring-opening reaction is supported by the NanQ primary assays and converges on the same linear NanA substrate. Source location `Pathway/reaction-ordering; child reaction-ordering`
aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+) `RHEA:25254`	provides_input_for	aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The complete native degradation route orders these reactions; the alternative alpha ring-opening reaction is supported by the NanQ primary assays and converges on the same linear NanA substrate. Source location `Pathway/reaction-ordering; child reaction-ordering`
aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	provides_input_for	N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The complete native degradation route orders these reactions; the alternative alpha ring-opening reaction is supported by the NanQ primary assays and converges on the same linear NanA substrate. Source location `Pathway/reaction-ordering; child reaction-ordering`
N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	provides_input_for	alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The native reaction ordering and primary convergence route connect these steps. NagA produces anomer-unspecified GlcN6P whereas the directed NagB equation uses alpha-GlcN6P; this ordering does not equate those exact chemical identifiers. Source location `Pathway/reaction-ordering; child reaction-ordering`
N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in) `RHEA:28989`	provides_input_for	N-acetyl-beta-neuraminate => aceneuramate `RHEA:67741`	PMID:33895133 Source assertion: Imported Neu5Ac supplies the cytosolic NanQ/NanA route. The transport equation pools anomers, while the native core specifies beta ring opening; this is pathway context, not an anomer-specific transport claim. Source location `PMC8141875, Introduction, Results and Discussion; PMID:22167185 transport context`
N-acetyl-D-mannosamine transport via PTS (periplasm) `BiGG:ACMANAptspp`	provides_input_for	aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate `RHEA:25259`	PMID:9864311 Source assertion: PTS uptake supplies ManNAc6P to NanE without the NanK ATP step. This physiological ordering does not independently determine the exact transported anomer or validate model structural cross-references. Source location `PMC103530, Results and Discussion, convergence model Fig. 1` BiGG:acmanap Source assertion: The native product has formula C8H14NO9P, charge -2 and InChIKey QDSLHWJDSQGPEE-WCTZXXKLSA-L. It is retained as its native model identity; the substrate annotation conflict is separately stated on the consumed model compound. Source location `Universal metabolite formulae/charges/database_links[InChI Key]; iML1515/metabolites[id=acmanap_c]`
N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	provides_input_for	N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate `RHEA:22937`	PMID:9864311 Source assertion: PTS-mediated GlcNAc uptake directly supplies GlcNAc6P, which NagA deacetylates before NagB deamination. Source location `PMC103530, Fig. 1 and Introduction`
L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate `RHEA:23881`	provides_input_for	N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein] `RHEA:49241`	UniProtKB:P08839 Source assertion: Enzyme I supplies phosphorylated HPr to the sugar-specific PTS relay. This shared energy-transfer context overlaps the net BiGG ManNAc transport equation and is not an additional net stoichiometric input. Source location `comments[commentType=FUNCTION]`
alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+) `RHEA:12173`	provides_input_for	glycolysis I (from glucose 6-phosphate) `MetaCyc:GLYCOLYSIS`	MetaCyc:GLCMANNANAUT-PWY Source assertion: The native parent pathway-link connects FRUCTOSE-6P to GLYCOLYSIS. Only that downstream interface is represented, without importing the connected glycolysis network. Source location `Pathway/pathway-link`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	zinc(2+) `CHEBI:29105`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	cobalt(2+) `CHEBI:48828`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	manganese(2+) `CHEBI:29035`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	cadmium(2+) `CHEBI:48775`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	iron(2+) `CHEBI:29033`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylglucosamine-6-phosphate deacetylase `MetaCyc:NAG6PDEACET-CPLX`	has_cofactor	nickel(2+) `CHEBI:49786`	PMID:17567047 Source assertion: E. coli NagA uses one divalent metal per subunit. Reconstituted Zn, Co, Mn, Cd, Fe and Ni enzymes were active to different degrees; these are alternatives, not six simultaneously required metals. Zn and Co had the highest catalytic efficiencies. Source location `PMC2533526, Results and Discussion S16/S17, Table 1; Methods S9/S10`
N-acetylneuraminate anomerase NanQ `UniProtKB:P45424`	has_cofactor	zinc(2+) `CHEBI:29105`	UniProtKB:P45424 Source assertion: NanQ binds Zn2+; the proposed catalytic role is annotated with ECO:0000305, while Zn association is supported by PMID:33895133. Do not transfer the Zn-dependent interpretation to NanR. Source location `comments[commentType=COFACTOR]`
PTS enzyme I `MetaCyc:CPLX0-7938`	has_cofactor	magnesium(2+) `CHEBI:18420`	UniProtKB:P08839 Source assertion: Reviewed enzyme I cofactor annotation specifies Mg2+, supported by PMID:17053069. Source location `comments[commentType=COFACTOR], ECO:0000269`
HTH-type transcriptional repressor NanR `UniProtKB:P0A8W0`	inhibits	N-acetylneuraminate and N-acetylmannosamine degradation I `MetaCyc:PWY0-1324`	PMID:9864311 Source assertion: NanR represses the nanATEK-yhcH catabolic operon. The pathway-level edge denotes transcriptional control of those components, not direct inhibition of every chemical reaction. Source location `PMC103530, Introduction, Results and Discussion`
DNA-binding transcriptional repressor Mlc `UniProtKB:P50456`	inhibits	mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	PMID:9864311 Source assertion: Mlc represses manXYZ expression; mlc loss increases transport capacity. The edge concerns transporter abundance, not direct catalytic inhibition. Source location `PMC103530, Introduction, Results and Discussion`
DNA-binding transcriptional dual regulator NagC `UniProtKB:P0AF20`	inhibits	N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	PMID:9864311 Source assertion: NagC represses nagE-nagBACD expression; intracellular GlcNAc6P is the inducing signal. The edge concerns expression, not direct inhibition of NagA or NagB. Source location `PMC103530, Introduction, Results and Discussion`
N-acetylneuraminate `CHEBI:35418`	inhibits	HTH-type transcriptional repressor NanR `UniProtKB:P0A8W0`	PMID:33790291 Source assertion: Neu5Ac binding reduced NanR DNA affinity under the reported conditions. NanR remained dimeric with and without ligand; cooperative binding places three dimers on the three-repeat operator, contrary to the older ligand-induced monomerization interpretation. Source location `PMC8012715, Results Sec4/Sec5/Sec6; Methods Sec12/Sec13`
N-acetyl-D-glucosamine 6-phosphate `CHEBI:57513`	inhibits	DNA-binding transcriptional dual regulator NagC `UniProtKB:P0AF20`	PMID:19700525 Source assertion: GlcNAc6P is the NagC inducing signal and increases nagE-nagBACD expression. Growth on GlcN provides only partial NagC induction from peptidoglycan recycling; native NagB can already be allosterically activated under those conditions. Source location `PMC2753035, Abstract; Results and Discussion sec8/sec11`
N-acetyl-D-glucosamine 6-phosphate `CHEBI:57513`	activates	glucosamine-6-phosphate deaminase `MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX`	PMID:19700525 Source assertion: GlcNAc6P allosterically activates wild-type NagB; the reported in vivo growth experiments show substrate supply rather than additional allosteric activation can limit growth. This native mechanism is distinct from the Ser1 construct assays. Source location `PMC2753035, Results and Discussion sec8/sec11`
3',5'-cyclic AMP(1-) `CHEBI:58165`	activates	DNA-binding transcriptional dual regulator CRP `UniProtKB:P0ACJ8`	UniProtKB:P0ACJ8 Source assertion: cAMP allosterically activates DNA binding by CRP homodimers; binding-site annotations explicitly identify CHEBI:58165. This does not imply that every CRP target is transcriptionally activated. Source location `comments[commentType=FUNCTION or SUBUNIT]; features[type=Binding site]/ligand`
CRP-cyclic-AMP DNA-binding transcriptional dual regulator `EcoCyc:CPLX0-226`	regulates	N-acetylglucosamine degradation I `MetaCyc:GLUAMCAT-PWY`	MetaCyc:CPLX-167 Source assertion: The native NagE description names regulation by NagC together with the cAMP-CRP complex. This edge preserves promoter-regulation context without assigning a universal positive sign. Source location `Protein/comment, paragraph beginning Expression of the nagE monocistronic operon` PMID:7791215 Source assertion: The primary abstract reports cAMP/CAP effects on NagC apparent binding to wild-type versus super-operators. Full text was not inspected; no additional promoter-architecture result is inferred. Source location `Issuing Europe PMC primary abstract` EcoCyc:CPLX0-226 Source assertion: The exact cAMP-bound CRP complex is issued in ECOLI 27.0 for K-12 substr. MG1655 (NCBITaxon:511145). Native nagEp regulations have both signs; this contextual Nag edge remains unsigned. Source location `Protein/common-name; metadata/PGDB; regulated promoter nagEp and modes`
DNA-binding transcriptional dual regulator NagC `UniProtKB:P0AF20`	regulates	mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	PMID:7791215 Source assertion: The primary abstract reports NagC binding at two sites upstream of manXYZ. This is promoter-regulatory context without an inferred magnitude or universal direction of expression change. Source location `Issuing Europe PMC primary abstract`
uridylyl-[protein PII] `MetaCyc:URIDYLYL-PII` experimental construct: His-tagged ASKA GlnB, refolded and uridylylated with GlnD. Partial and fully modified preparations were compared; U-PII was not repurified from the uridylylation mixture. Qualification evidence PMID:29229699 Source assertion: The study identifies the recombinant preparation and its construct/purification scope; this qualification restricts the endpoint to that assay material. Source location `PMC5809692, Materials and Methods sec4-3/sec4-6`	activates	Glucosamine-6-phosphate deaminase `UniProtKB:P0A759` experimental construct: Ser1-NagB from E. coli BW25113: first nagB codon omitted in a SUMO fusion; Ulp1 cleavage yields N-terminal Ser instead of native Met. No sequence equivalence elsewhere is asserted. Qualification evidence PMID:29229699 Source assertion: The study identifies the recombinant preparation and its construct/purification scope; this qualification restricts the endpoint to that assay material. Source location `PMC5809692, Materials and Methods sec4-2/sec4-5`	PMID:29229699 Source assertion: Uridylylated PII increased Ser1-NagB activity in the presence of GlcNAc6P; magnitude depended on modification, pH and substrate conditions. GlnD-only mixture controls did not explain activation. No exact modified-trimer occupancy is inferred. Source location `PMC5809692, Results sec2-1/sec2-2; Methods sec4-3/sec4-6`
N-acetylmannosamine-6-phosphate 2-epimerase `UniProtKB:P0A761` experimental construct: His-tagged recombinant ASKA NanE preparation, purified by Ni2+-chelating chromatography. Qualification evidence PMID:29229699 Source assertion: The study identifies the recombinant preparation and its construct/purification scope; this qualification restricts the endpoint to that assay material. Source location `PMC5809692, Materials and Methods sec4-3/sec4-6`	activates	Glucosamine-6-phosphate deaminase `UniProtKB:P0A759` experimental construct: Ser1-NagB from E. coli BW25113: first nagB codon omitted in a SUMO fusion; Ulp1 cleavage yields N-terminal Ser instead of native Met. No sequence equivalence elsewhere is asserted. Qualification evidence PMID:29229699 Source assertion: The study identifies the recombinant preparation and its construct/purification scope; this qualification restricts the endpoint to that assay material. Source location `PMC5809692, Materials and Methods sec4-2/sec4-5`	PMID:29229699 Source assertion: NanE activated Ser1-NagB with or without GlcNAc6P. At 0.7 micromolar NanE, effects depended on pH and substrate conditions. This regulatory assay does not independently establish purified K-12 NanE epimerase chemistry. Source location `PMC5809692, Results sec2-1/sec2-3; Methods sec4-3/sec4-5`
phosphocarrier protein HPr `MetaCyc:PTSH-MONOMER` experimental construct: Recombinant HPr assay preparation in its nonphosphorylated state; the earlier study identifies an ASKA His-tagged preparation. Qualification evidence PMID:28634232 Source assertion: The earlier study purified ASKA HPr with an N-terminal His6 tag. Source location `PMC5572926, Experimental procedures sec9/sec10`	activates	Glucosamine-6-phosphate deaminase `UniProtKB:P0A759` experimental construct: Ser1-NagB from E. coli BW25113: first nagB codon omitted in a SUMO fusion; Ulp1 cleavage yields N-terminal Ser instead of native Met. No sequence equivalence elsewhere is asserted. Qualification evidence PMID:29229699 Source assertion: The study identifies the recombinant preparation and its construct/purification scope; this qualification restricts the endpoint to that assay material. Source location `PMC5809692, Materials and Methods sec4-2/sec4-5`	PMID:29229699 Source assertion: Nonphosphorylated HPr enhanced Ser1-NagB activity in the reported GlcNAc6P-dependent assays. HPr plus U-PII or NanE showed conditional synergy; docking models do not establish a new physical multi-protein complex. Source location `PMC5809692, Results sec2-1/sec2-4 and Fig. 5`
CRP-cyclic-AMP DNA-binding transcriptional dual regulator `EcoCyc:CPLX0-226`	activates	mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	EcoCyc:CPLX0-226 Source assertion: ECOLI 27.0 MG1655 regulations REG0-5729 and REG0-5728 positively regulate manXp with the cAMP-bound CRP complex. This edge concerns ManXYZ expression, not direct stimulation of assembled transporter catalysis. Source location `Protein/regulates/Regulation[@frameid=REG0-5729]; nested regulated-entity/Promoter/regulated-by/Regulation[@frameid=REG0-5728]; mode, regulator and manXp PM00276` PMID:9484892 Source assertion: The primary abstract reports cAMP/CAP-dependent manX transcription and class II promoter activation. Full article methods and experimental strain details were not inspected; no universal amino-sugar growth-condition effect is inferred. Source location `Europe PMC exact MED result, abstractText`
small regulatory RNA SgrS `EcoCyc:RNA0-241`	inhibits	mannose-specific PTS enzyme II `MetaCyc:CPLX-165`	PMID:22988087 Source assertion: SgrS represses ManXYZ synthesis through two manXYZ mRNA binding sites: the manX coding site and the manX-manY intergenic site independently control manX and manYZ translation. manZ is coupled to manY; both sites support efficient message degradation and full 2DG-stress recovery. This is not direct inhibition of assembled transport or an SgrT protein effect. Source location `PMC3479541, Results sec2-sec8, Discussion s2; Figs. 1-7` PMID:22988087 Source assertion: Reporter, binding-site mutant, RNase E mutant, footprinting and stress-growth assays support the mechanism. Main-text methods name CS104/JH derivatives and DJ480; Table S1 was not inspected. These assay backgrounds are not all asserted to be unmodified MG1655 or identical to the native SgrS sequence. Source location `PMC3479541, Materials and Methods s3/sec11-sec16; Figs. 1-6` EcoCyc:RNA0-241 Source assertion: The native ECOLI 27.0 MG1655 record identifies the regulatory RNA SgrS, aliases SgrS/RyaA, distinct from its G0-9941 gene and the SgrT protein. Its first comment paragraph cites Rice12 for independent manX and manYZ translational repression. Source location `RNA/common-name, synonym, gene; metadata/PGDB; RNA/comment paragraph1`
CRP-cyclic-AMP DNA-binding transcriptional dual regulator `EcoCyc:CPLX0-226`	has_part	DNA-binding transcriptional dual regulator CRP `EcoCyc:PC00004`	EcoCyc:CPLX0-226 Source assertion: The ECOLI 27.0 MG1655 cAMP-bound complex explicitly contains protein complex PC00004 and compound CAMP. No component coefficient is supplied here; no bound-complex occupancy or numerical stoichiometry is inferred. Source location `Protein/component/Protein[@frameid=PC00004]; component/Compound[@frameid=CAMP]`
CRP-cyclic-AMP DNA-binding transcriptional dual regulator `EcoCyc:CPLX0-226`	has_part	3',5'-cyclic AMP(1-) `CHEBI:58165`	EcoCyc:CPLX0-226 Source assertion: CAMP is an explicit component of the native cAMP-bound CRP complex; its component coefficient is absent. This records composition without asserting cAMP occupancy. Source location `Protein/component/Compound[@frameid=CAMP]` EcoCyc:CAMP Source assertion: The exact ECOLI CAMP compound has a CHEBI58165 unification link and a charged InChI matching the issuing ChEBI compound. Its identity is distinct from any inferred binding occupancy. Source location `Compound/dblink[dblink-db=CHEBI]; Compound/inchi`
DNA-binding transcriptional dual regulator CRP `EcoCyc:PC00004`	has_part	DNA-binding transcriptional dual regulator CRP `UniProtKB:P0ACJ8`	EcoCyc:PC00004 Source assertion: The ECOLI 27.0 MG1655 CRP protein complex contains component PD00257 with coefficient 2. This establishes the protein homodimer, without inferring a cAMP coefficient for the separately named bound complex. Source location `Protein/component/Protein[@frameid=PD00257]; component/coefficient` EcoCyc:PD00257 Source assertion: The exact ECOLI polypeptide PD00257 has a native UniProt P0ACJ8 unification link. Native MG1655 provenance and the reviewed K-12 UniProt sequence scope remain distinct. Source location `Protein/dblink[dblink-db=UNIPROT][dblink-relationship=unification]`

References

UniProtKB:P0A6L4 N-acetylneuraminate lyase
UniProtKB:P45425 N-acetylmannosamine kinase
UniProtKB:P0A761 N-acetylmannosamine-6-phosphate 2-epimerase
UniProtKB:P0AF18 N-acetylglucosamine-6-phosphate deacetylase
UniProtKB:P0A759 Glucosamine-6-phosphate deaminase
UniProtKB:P45424 N-acetylneuraminate anomerase NanQ
UniProtKB:P41036 Sialic acid transporter NanT
UniProtKB:P0A8W0 HTH-type transcriptional repressor NanR
UniProtKB:P50456 DNA-binding transcriptional repressor Mlc
UniProtKB:P69801 PTS system mannose-specific EIIC component
UniProtKB:P69805 PTS system mannose-specific EIID component
UniProtKB:P69797 PTS system mannose-specific EIIAB component
UniProtKB:P09323 PTS system N-acetylglucosamine-specific EIICBA component
UniProtKB:P08839 Phosphoenolpyruvate-protein phosphotransferase
UniProtKB:P0A9Z1 Nitrogen regulatory protein P-II 1
UniProtKB:P0AF20 DNA-binding transcriptional dual regulator NagC
UniProtKB:P0ACJ8 DNA-binding transcriptional dual regulator CRP
MetaCyc:PWY0-1324 N-acetylneuraminate and N-acetylmannosamine degradation I
MetaCyc:GLCMANNANAUT-PWY MetaCyc:GLCMANNANAUT-PWY
MetaCyc:GLUAMCAT-PWY N-acetylglucosamine degradation I
MetaCyc:GLYCOLYSIS Native downstream glycolysis interface
RHEA:67737 N-acetyl-alpha-neuraminate => aceneuramate
RHEA:67741 N-acetyl-beta-neuraminate => aceneuramate
RHEA:23297 aceneuramate => aldehydo-N-acetyl-D-mannosamine + pyruvate
RHEA:25254 aldehydo-N-acetyl-D-mannosamine + ATP => aldehydo-N-acetyl-D-mannosamine 6-phosphate + ADP + H(+)
RHEA:25259 aldehydo-N-acetyl-D-mannosamine 6-phosphate => N-acetyl-D-glucosamine 6-phosphate
RHEA:22937 N-acetyl-D-glucosamine 6-phosphate + H2O => D-glucosamine 6-phosphate + acetate
RHEA:12173 alpha-D-glucosamine 6-phosphate + H2O => beta-D-fructose 6-phosphate + NH4(+)
RHEA:28989 N-acetylneuraminate(out) + H(+)(out) => N-acetylneuraminate(in) + H(+)(in)
RHEA:49241 N(pros)-phospho-L-histidyl-[protein] + N-acetyl-D-glucosamine(out) => N-acetyl-D-glucosamine 6-phosphate(in) + L-histidyl-[protein]
RHEA:23881 L-histidyl-[protein] + phosphoenolpyruvate => N(pros)-phospho-L-histidyl-[protein] + pyruvate
BiGG:ACMANAptspp N-acetyl-D-mannosamine transport via PTS (periplasm)
BiGG:acmana N-Acetyl-D-mannosamine
BiGG:acmanap N-Acetyl-D-mannosamine 6-phosphate
CHEBI:17122 aldehydo-N-acetyl-D-mannosamine
PMID:9864311 Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli.
MetaCyc:ACNEULY-CPLX N-acetylneuraminate lyase
MetaCyc:CPLX0-8588 N-acetylmannosamine kinase
MetaCyc:NAG6PDEACET-CPLX N-acetylglucosamine-6-phosphate deacetylase
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-CPLX glucosamine-6-phosphate deaminase
MetaCyc:CPLX0-7938 PTS enzyme I
MetaCyc:CPLX0-7921 mannose-specific PTS enzyme IIAB component
MetaCyc:CPLX-165 mannose-specific PTS enzyme II
MetaCyc:CPLX-167 N-acetylglucosamine-specific PTS enzyme II
MetaCyc:PIIPROTEIN-CPLX nitrogen regulatory protein PII-1
MetaCyc:PTSH-MONOMER phosphocarrier protein HPr
MetaCyc:PTSH-PHOSPHORYLATED phosphocarrier HPr-Nπ-phospho-L-histidine
MetaCyc:URIDYLYL-PII uridylyl-[protein PII]
MetaCyc:CPLX0-8568 uridylyl-[protein PII-1]
PMID:33895133 The metalloprotein YhcH is an anomerase providing N-acetylneuraminate aldolase with the open form of its substrate.
PMID:22167185 The membrane proteins SiaQ and SiaM form an essential stoichiometric complex in the sialic acid tripartite ATP-independent periplasmic (TRAP) transporter SiaPQM (VC1777-1779) from Vibrio cholerae.
PMID:17567047 N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion.
PMID:33790291 PMID:33790291
PMID:19700525 PMID:19700525
PMID:7791215 Nag repressor-operator interactions: protein-DNA contacts cover more than two turns of the DNA helix.
PMID:29229699 The Nitrogen Regulatory PII Protein (GlnB) and N-Acetylglucosamine 6-Phosphate Epimerase (NanE) Allosterically Activate Glucosamine 6-Phosphate Deaminase (NagB) in Escherichia coli.
PMID:28634232 PMID:28634232
PMID:8240271 Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.
PMID:31209249 Structure of the mannose transporter of the bacterial phosphotransferase system.
EcoCyc:CPLX0-226 CRP-cyclic-AMP DNA-binding transcriptional dual regulator (ECOLI 27.0; MG1655)
EcoCyc:RNA0-241 small regulatory RNA SgrS (ECOLI 27.0; MG1655)
EcoCyc:PC00004 DNA-binding transcriptional dual regulator CRP (ECOLI 27.0; MG1655)
EcoCyc:CAMP cyclic-AMP native identity and ChEBI unification (ECOLI 27.0; MG1655)
EcoCyc:PD00257 CRP polypeptide native identity and UniProt unification (ECOLI 27.0; MG1655)
PMID:9484892 Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS.
PMID:22988087 Small RNA binding-site multiplicity involved in translational regulation of a polycistronic mRNA.

Curation history

2026-10-11T23:25:22Z codex
- CREATE — Add the evidence-backed amino-sugar catabolism superpathway
  Create MetaCyc:GLCMANNANAUT-PWY with 80 named identities, 114 mechanistic edges and 66 references. Preserve the original 77-ID/109-edge review and its issue425 request for CRP-cAMP and SgrS ManXYZ regulation. The independently accepted successor adds the exact EcoCyc RNA/complex identities, bounded regulatory evidence and assembly edges, retaining construct, state, taxon and source-direction limits. Source replay and external software checks are archived in research/pathway_additions/2026-10-11-next-223; maintained gates, structured review and publication outcomes are recorded separately.
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2026-10-11T23:32:29Z codex
- EDIT — Declare the three native child/interface nodes as pathways
  Adversarial export preservation found that untyped MetaCyc context nodes acquired a false BiochemicalReaction type. Add category: pathway only to PWY0-1324, GLUAMCAT-PWY and GLYCOLYSIS. All identifiers, labels, mechanistic edges, references and evidence values are unchanged from the independently reviewed successor; the exact three-field delta and issue426 disposition are recorded in the final integration dossier.
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