GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:PSEPK/algX/algX-uniprot.txt

UniProtKB reviewed entry for algX (Q88ND0)

The record defines the periplasmic SGNH and carbohydrate-binding domains and the two O-acetylation/protection roles.

file:PSEPK/algX/algX-goa.tsv

QuickGO GOA annotations for algX

The fetched GOA table contains the two existing annotations reviewed here.

UniProtKB:Q51372

Reviewed Pseudomonas aeruginosa AlgX exemplar

Q51372 is the characterized ortholog used to transfer the terminal alginate O-acetyltransferase and polysaccharide-binding functions to Q88ND0.

PMID:23779107

Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation.

AlgX catalytic-triad substitutions produce non-acetylated alginate in vivo, while its two-domain structure identifies an SGNH-like catalytic domain and carbohydrate-binding module.

PMID:25165982

P. aeruginosa SGNH hydrolase-like proteins AlgJ and AlgX have similar topology but separate and distinct roles in alginate acetylation.

Q51372 binds polymannuronate length-dependently and catalyzes O-acetylation of polymannuronate using a surrogate donor in vitro.

file:projects/P_PUTIDA/deep-research/PSEPK__alginate-o-acetylation__ppu00543-deep-research-openscientist.md

OpenScientist PSEPK alginate O-acetylation synthesis

The report identifies AlgX as the terminal polymer O-acetyltransferase and distinguishes its chain-protection role.

file:modules/alginate_o_acetylation.yaml

Alginate O-acetylation module

AlgX implements the terminal polymer-acetylation part.