A7LXT7 · BGH5A_BACO1
- ProteinXyloglucan-specific endo-beta-1,4-glucanase BoGH5A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids502 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides.
Miscellaneous
Gut bacteria supply the human body with energy from dietary polysaccharides through glycosidases that are absent in the human genome. Xyloglucans are a ubiquitous family of highly branched plant cell wall polysaccharides present in the vegetables we consume. Enzymes involved in xyloglucan degradation mediate the conversion of otherwise indigestible plant polysaccharides to short-chain fatty acids (PubMed:24463512).
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.036 mM | XXXG-beta-CNP | |||||
0.145 mM | XLLG-beta-CNP | |||||
3.59 mM | GGGG-beta-CNP |
kcat is 10.5 sec-1 for XXXG-beta-CNP. kcat is 11.1 sec-1 for XLLG-beta-CNP. kcat is 0.12 sec-1 for GGGG-beta-CNP.
pH Dependence
Optimum pH is 6.0-7.0.
Pathway
Glucan metabolism; xyloglucan degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 165 | substrate | ||||
Sequence: N | ||||||
Binding site | 172 | substrate | ||||
Sequence: V | ||||||
Binding site | 251 | substrate | ||||
Sequence: H | ||||||
Binding site | 296 | substrate | ||||
Sequence: N | ||||||
Active site | 297 | Proton donor | ||||
Sequence: E | ||||||
Active site | 430 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 472 | substrate | ||||
Sequence: W |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell outer membrane | |
Molecular Function | xyloglucan-specific endo-beta-1,4-glucanase activity | |
Biological Process | symbiotic process benefiting host | |
Biological Process | xyloglucan catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameXyloglucan-specific endo-beta-1,4-glucanase BoGH5A
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA7LXT7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell outer membrane ; Lipid-anchor
Note: Cell outer membrane localization is predicted by analogy with the archetypal sus locus.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Cells are not able to growth on xyloglucan polysaccharide, This phenotype can be directly rescued by the addition of xyloglucan oligosaccharides.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 33 | Abolishes surface localization and hampers growth on xyloglucans. | ||||
Sequence: C → A | ||||||
Mutagenesis | 430 | Loss of activity. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for signal, lipidation, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MEKQSFSDGLFSPLGIKRVIFMLVLLTTSFIS | ||||||
Lipidation | 33 | N-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 33 | S-diacylglycerol cysteine | ||||
Sequence: C | ||||||
Chain | PRO_0000425894 | 33-502 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A | |||
Sequence: CSNSDEKGGSLEVAQEYRNLEFDARGSRQTIQIDGPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQSLYSVPAYDEYIAPDNTGMRDLTSMQLSALMKAGVNVGNTFEAVIVGNDGSLSGDETCWGNPTPNKVLFEGIKAAGFDVVRIPVAYSHQFEDAATYKIKSAWMDKVEAAVKAALDAGLYVIINIHWEGGWLNHPVDANKEALDERLEAMWKQIALRFRDYDDRLLFAGTNEVNNDDANGAQPTEENYRVQNGFNQVFVNTVRATGGRNHYRHLIVQAYNTDVAKAVAHFTMPLDIVQNRIFLECHYYDPYDFTIMPNDENFKSQWGAAFAGGDVSATGQEGDIEATLSSLNVFINNNVPVIIGEYGPTLRDQLTGEALENHLKSRNDYIEYVVKTCVKNKLVPLYWDAGYTEKLFDRTTGQPHNAASIAAIMKGLN |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 67-127 | BACON | ||||
Sequence: GPAEWHISTSESWCKSSHTIGEGKQYVNITVEANDTQKERTATVTVSASGAPDIIINVKQS |
Domain
The BACON domain was initially thought to act as a carbohydrate-binding domain. However, it does not bind carbohydrates and may rather be required to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide (PubMed:24463512).
Sequence similarities
Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length502
- Mass (Da)55,653
- Last updated2007-10-02 v1
- Checksum59990DE33869CCC2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAXF02000049 EMBL· GenBank· DDBJ | EDO11444.1 EMBL· GenBank· DDBJ | Genomic DNA |