A0A0A7EQR3 · GCE_CERUI
- Protein4-O-methyl-glucuronoyl methylesterase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin (PubMed:25425346, PubMed:26712478).
Catalytic activity
- a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-O-methyl-alpha-D-glucuronate derivative + an alcohol + H+This reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.6 mM | benzyl (methyl 4-O-methyl-alpha-D-glucopyranoside) | |||||
80 mM | benzyl (methyl alpha-D-glucopyranoside) | |||||
55 mM | phenylpropyl (methyl alpha-D-glucopyranoside) | |||||
8.9 mM | phenyl (methyl alpha-D-glucopyranoside) | |||||
4.6 mM | threo-l-[4-(benzyloxy)-3-methoxyphenyl]-3-hydroxy-2- (2-methoxyphenoxy) (methyl 4-O-methyl-alpha-D-glucopyranosid) |
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 286 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 290 | substrate | ||||
Sequence: K | ||||||
Binding site | 332 | substrate | ||||
Sequence: Q | ||||||
Binding site | 340 | substrate | ||||
Sequence: E | ||||||
Binding site | 384 | substrate | ||||
Sequence: W | ||||||
Active site | 420 | Proton donor/acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | cellulose binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | lignin catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name4-O-methyl-glucuronoyl methylesterase
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Cerrenaceae > Cerrena
Accessions
- Primary accessionA0A0A7EQR3
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MFKPSFVALALVSYATA | ||||||
Chain | PRO_5002038279 | 18-474 | 4-O-methyl-glucuronoyl methylesterase | |||
Sequence: QASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCLQGAAPAPARTTAAPPPPPATTAAPPPPTTSAPTGSSPVAGACGAIASTVPNYNNAKLPDPFTFANGTALRTKADWSCRRAEISALIQNYEAGTLPPKPPVVTASFSKSGNTGTLAITAGLSNSQTIKFSPTISYPSGTPPANGWPLIIAYEGGSIPIPAGVATLTYSNSDMAQQNSASSRGQGLFYQLYGSTHSASAMTAWVWGVSRIIDALEMTPTAQINTQRIGVTGCSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHCAWPSSLTPQLNAFINRFLLDQSATTNVFTTNNQFGKVQWNAANWITWTTPTLT | ||||||
Glycosylation | 120 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 285↔421 | |||||
Sequence: CSRDGKGALMAGAFEERIALTIPQESGSGGDACWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGCMTAAHTVWQGLGIADSHGFAQVGGHAHC | ||||||
Disulfide bond | 317↔393 | |||||
Sequence: CWRLSKYEIDNGNQVQDAVEIVGENVWFSTNFNNYVQKLPTVPEDHHLLAAMVAPRAMISFENTDYLWLSPMSSFGC |
Post-translational modification
N-glycosylated (PubMed:25425346).
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-55 | CBM1 | ||||
Sequence: ASAPQWGQCGGIGWTGPTACPSGWACQQLNAYYSQCL | ||||||
Region | 61-91 | Disordered | ||||
Sequence: APARTTAAPPPPPATTAAPPPPTTSAPTGSS | ||||||
Compositional bias | 64-87 | Pro residues | ||||
Sequence: RTTAAPPPPPATTAAPPPPTTSAP | ||||||
Motif | 284-289 | GXSYXG catalytic site motif | ||||
Sequence: GCSRDG |
Sequence similarities
Belongs to the carbohydrate esterase 15 (CE15) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length474
- Mass (Da)49,910
- Last updated2015-03-04 v1
- Checksum7E1F16E59E5E3413
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 64-87 | Pro residues | ||||
Sequence: RTTAAPPPPPATTAAPPPPTTSAP |
Keywords
- Technical term