fae1A encodes a bifunctional enzyme with both cellulase (EC 3.2.1.4) and feruloyl esterase activities. This bacterial enzyme from Ruminiclostridium josui catalyzes the endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans, as well as the hydrolysis of feruloyl esters. The protein contains a carbohydrate-binding module (CBM6) and dockerin domain, suggesting it functions as part of a cellulosome complex for efficient plant cell wall degradation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008810 cellulase activity | IEA GO_REF:0000003 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0000272 polysaccharide catabolic process | IEA GO_REF:0000120 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds | IEA GO_REF:0000002 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0016787 hydrolase activity | IEA GO_REF:0000043 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0016798 hydrolase activity, acting on glycosyl bonds | IEA GO_REF:0000043 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0030245 cellulose catabolic process | IEA GO_REF:0000043 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
| GO:0030246 carbohydrate binding | IEA GO_REF:0000002 | ACCEPT | Summary: fae1A has demonstrated cellulase activity (EC 3.2.1.4) as evidenced by its ability to hydrolyze beta-D-glucosidic linkages in cellulose and related polysaccharides. This annotation accurately reflects the primary enzymatic function of the protein. Reason: The cellulase activity is well-documented and represents a core function of fae1A. The EC number 3.2.1.4 is specifically assigned in UniProt, confirming this enzymatic activity. Supporting Evidence: UniProt:A0A2Z5TSL2 RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601}; EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601} |
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Download this section (compressed HTML)Q: How does the modular architecture of Fae1A coordinate feruloyl esterase and xylanase activities for synergistic plant cell wall degradation?
Q: What is the molecular basis for substrate specificity between ferulic acid esters and other phenolic esters in plant biomass?
Q: How does Fae1A integrate into the larger cellulosome complex and interact with other glycoside hydrolases?
Experiment: Single-particle cryo-EM of Fae1A in complex with model plant cell wall substrates to visualize multi-domain organization
Experiment: Activity-based protein profiling to identify all ester bonds cleaved by Fae1A in native lignocellulose
Experiment: FRET-based assays to monitor real-time coordination between esterase and xylanase domains during substrate processing
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