Gene Ontology annotation through association of InterPro records with GO terms.

Gene Ontology annotation based on Enzyme Commission mapping

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

Combined Automated Annotation using Multiple IEA Methods.

Significance of a family-6 carbohydrate-binding module in a modular feruloyl esterase for removing ferulic acid from insoluble wheat arabinoxylan.

Fae1A from R. josui is experimentally characterized as a feruloyl esterase (CE1 family, EC 3.1.1.73), not a cellulase - this contradicts the UniProt automated cellulase EC 3.2.1.4 annotation; Fae1A hydrolyzes ferulate and related hydroxycinnamoyl esters on arabinoxylans and releases diferulate from biomass.
Fae1A is a modular secreted enzyme (~53.1 kDa, 489 aa) comprising an N-terminal signal peptide, CE1 catalytic module, CBM6 carbohydrate-binding module (binds xylan/xylooligosaccharides), and a dockerin module for cellulosome incorporation via cohesin-dockerin interactions on R. josui scaffoldins.
CBM6 deletion reduces activity on insoluble wheat arabinoxylan early in the time course but the CE1-only construct catches up by ~6 h, consistent with CBM6 acting as a polysaccharide-targeting module that concentrates initial turnover near xylan-bound feruloyl groups.

file:RUMJO/fae1A/fae1A-deep-research-falcon.md

Deep research report on fae1A/A0A2Z5TSL2 (Falcon/Edison Scientific Literature)

The UniProt annotation of fae1A as a cellulase (EC 3.2.1.4) appears to be an automated misannotation - direct biochemical characterization (Mamiya 2020, PMID:32601247) shows Fae1A is a feruloyl esterase (EC 3.1.1.73) of the CE1 family with CBM6 targeting of arabinoxylan and dockerin-mediated cellulosome incorporation. The current annotations should be revisited by a curator.