Context
PMID:40171682Review places alginate acetylation in selected Pseudomonas and Azotobacter lineages and distinguishes the proposed MBOAT/SGNH relay from experiments on other polymers.
PMID:40821665Comparative Azotobacter review identifies the AlgI/AlgV/AlgF/AlgX implementation; its categorical donor and enzyme descriptions are qualified by primary evidence.
PMID:10352233A native Azotobacter nonpolar algF mutant produces unacetylated alginate, supporting cross-genus process conservation.
Brown-algal alginate production and other bacterial surface-polymer acylation systems do not establish this module. Current selected native proteins span P. aeruginosa PAO1-derived experiments, P. putida KT2440 and A. vinelandii ATCC 9046.
Alginate O-acetylationBiological Processalginate_o_acetylation
Four complementary roles in alginate acetylation; part ordering is presentational and does not establish a linear sequence of four catalytic reactions.
Context
PMID:40171682Review places alginate acetylation in selected Pseudomonas and Azotobacter lineages and distinguishes the proposed MBOAT/SGNH relay from experiments on other polymers.
PMID:40821665Comparative Azotobacter review identifies the AlgI/AlgV/AlgF/AlgX implementation; its categorical donor and enzyme descriptions are qualified by primary evidence.
PMID:10352233A native Azotobacter nonpolar algF mutant produces unacetylated alginate, supporting cross-genus process conservation.
Brown-algal alginate production and other bacterial surface-polymer acylation systems do not establish this module. Current selected native proteins span P. aeruginosa PAO1-derived experiments, P. putida KT2440 and A. vinelandii ATCC 9046.
Connections
Proposed acetyl delivery from AlgI to the periplasmic AlgJ/AlgV component; native association is demonstrated for Pa, but the chemical intermediate is not.
PMID:37797696Pa AlgI and AlgJ associate in native co-immunoprecipitation experiments.
PMID:40171682The full AlgI-to-AlgJ acyl-shuttle model remains experimentally incomplete.
Proposed acetyl handoff to AlgX; the physiological AlgJ donor/acceptor pair and direct transfer remain unresolved.
PMID:25165982AlgJ and AlgX have distinct biochemical roles; only AlgX directly modifies the tested polymer.
PMID:40171682The review identifies AlgJ-to-AlgX handoff as the major unresolved mechanistic step.
Provides interaction/assembly context, not an asserted acetyl substrate. Pairwise binding supports this model; simultaneous bridging is not established.
PMID:37797696Direct KT2440 pairwise AlgF interactions and Pa AlgF-AlgX association support organization of the acetylation machinery.
Provides interaction/assembly context, not an asserted acetyl substrate. Pairwise binding supports this model; simultaneous bridging is not established.
PMID:37797696Direct KT2440 pairwise AlgF interactions and Pa AlgF-AlgX association support organization of the acetylation machinery.
Part 1: inner-membrane acetyl-donor transfer
AlgI membrane acetyl-transfer componentReactionalgI_membrane_transfer
Annotons
AlgI membrane acyltransferase
algI_acyltransferase_activity
Participant: Family: AlgI family
Family:
AlgI familyInterPro:IPR028362
Function
Processes
Locations
Multipass membrane component required for acetylation. MBOAT ancestry supports an acyltransferase role, but neither the immediate physiological donor nor the complete target-specific covalent relay has been experimentally reconstructed. The proposed C-terminal acyl-shuttle mechanism is informed by Dlt and PatA systems rather than demonstrated AlgI chemistry.
PMID:12003941Nonpolar mutants lose alginate O-acetylation; topology places AlgI across the inner membrane.
PMID:31900562Mutant complementation and stability studies connect AlgI to the acetylation complex; the accessible record supports this at abstract level.
PMID:37797696Native P. aeruginosa co-immunoprecipitation supports AlgI association with AlgJ.
PMID:40171682Review explicitly qualifies the complete proposed alginate acyl-shuttle model.
Part 2: periplasm-facing acetyl relay
AlgJ/AlgV SGNH relay componentReactionalgJ_relay
Annotons
AlgJ/AlgV periplasm-facing acetylation component
algJ_relay_role
Participant: Family: AlgJ/AlgV SGNH acetylation-component family
Family:
AlgJ/AlgV SGNH acetylation-component family The ortholog group is represented by verified proteins. The specific InterPro domain is recorded separately as required_domain, rather than mislabeled as a full-length family identifier. In Azotobacter the acetylation homolog is called AlgV; a separate historical AlgJ designation names the export protein and is excluded.
Required Domain:
Alginate O-acetyltranferase AlgJInterPro:IPR034657
Processes
Locations
Membrane-associated periplasmic SGNH protein required for alginate acetylation. P. putida and P. aeruginosa AlgJ have directly measured acetylesterase activity with artificial substrates; the physiological relay substrate and transfer to AlgX remain unresolved. The module therefore records the proposed contribution without equating in-vitro hydrolysis with the native reaction.
PMID:25165982Both Pseudomonas AlgJ proteins have measured acetylesterase activity. Pa AlgJ has weak or undetectable polymer binding; direct polymer acetyl transfer was demonstrated for AlgX and was not established for AlgJ.
AlgJ exhibits acetylesterase activity in vitro.
PMID:37797696KT2440 AlgF-AlgJ binding is directly measured by ITC; Pa native AlgI-AlgJ association supports complex organization.
PMID:10352233Azotobacter algV is sequenced in the native alginate locus; this is not a purified AlgV assay.
Part 3: periplasmic accessory support
AlgF periplasmic accessory componentBiological ProcessalgF_accessory
Annotons
AlgF accessory protein
algF_accessory_role
Participant: Family: AlgF family
Family:
AlgF familyInterPro:IPR035422
Processes
Locations
Periplasmic noncatalytic component. KT2440 AlgF binds AlgJ and AlgX in separate in-vitro assays and lacks detected acetylesterase activity; P. aeruginosa AlgF has native AlgX association and no detected isolated polymannuronate binding. These support an interaction-mediator model, but simultaneous ternary bridging and exact acetyl-relay geometry remain proposed. Native Azotobacter algF genetics supports participation without establishing its molecular interaction mechanism.
PMID:37797696Target-specific structural, binding and association studies support an interaction role, with the Pseudomonas species and constructs distinguished.
PMID:31900562AlgF deletion affects acetylation and production/stability in the studied P. aeruginosa background.
PMID:10352233The Azotobacter nonpolar algF mutant produces unacetylated alginate.
As expected, AJ34 produced unacetylated alginate.
Part 4: terminal polymer O-acetylation
AlgX alginate O-acetyltransferaseReactionalgX_polymer_transfer
Annotons
AlgX terminal O-acetyltransferase
algX_o_acetyltransferase_activity
Participant: Family: AlgX polymer-modification and export-associated family
Family:
AlgX polymer-modification and export-associated family The ortholog group is represented by verified proteins. The specific InterPro domain is recorded separately as required_domain, rather than mislabeled as a full-length family identifier. Characterized full-length members also contain an AlgX C-terminal carbohydrate-binding module (InterPro:IPR031798); the N-terminal signature alone does not prove polymer binding or the full activity.
Required Domain:
Alginate biosynthesis protein AlgX, N-terminalInterPro:IPR034655
Function
O-acetyltransferase activityGO:0016413
Substrates:
unacetylated mannuronate residues in alginate
Products:
O-acetylated mannuronate residues in alginate
Processes
Locations
Terminal polymer-modifying enzyme. P. aeruginosa AlgX directly transfers acetyl groups from an artificial donor to polymannuronate; its catalytic-site mutants secrete nonacetylated polymer. KT2440 AlgX has directly measured acetylesterase activity, polymer binding and an AlgK-complex structure; polymer acetyl transfer is inferred from the characterized homolog. P. putida binding lacks the increasing-affinity length trend reported for P. aeruginosa. Azotobacter chemistry remains homolog-based. Native AlgX also contributes to polymer protection/export, but this module represents its modification role.
PMID:25165982P. aeruginosa AlgX directly O-acetylates polymannuronate using a surrogate donor.
PMID:23779107Catalytic-site mutations abolish alginate acetylation in vivo; accessible primary abstract supports the mutation conclusion.
PMID:36494359KT2440 AlgKX structure and polymer-binding experiments establish target-specific architecture and affinity behavior; Pa native interface disruption affects secretion/biofilm attachment.
PMID:10352233Azotobacter algX is sequenced in the alginate locus; no direct target polymer-transfer assay is claimed.