A2QAN3 · BGALA_ASPNC
- ProteinBeta-galactosidase A
- GenelacA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1007 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Miscellaneous
Mutants of this enzyme have improved transgalactosylation activity and can be used for galacto-oligosaccharides (GOS) production in vitro.
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
92.5 mM | lactose |
kcat is 214.9 sec-1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 96 | substrate | ||||
Sequence: Y | ||||||
Binding site | 140-142 | substrate | ||||
Sequence: NAE | ||||||
Binding site | 199 | substrate | ||||
Sequence: N | ||||||
Active site | 200 | Proton donor | ||||
Sequence: E | ||||||
Active site | 298 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 364 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | vacuole | |
Molecular Function | beta-galactosidase activity | |
Molecular Function | oligosaccharide binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | lactose catabolic process | |
Biological Process | polysaccharide catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-galactosidase A
- EC number
- Short namesAn-beta-gal
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA2QAN3
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 298 | Loss of hydrolytic activity. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 304 | Nearly complete loss of hydrolytic activity against lactose compared to wild-type due to decreased substrate affinity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 304 | Over 33% increase of hydrolytic activity against lactose compared to wild-type. No effect on hydrolytic activity compared to wild-type; when associated with H-355 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with H-355, G-357 and F-806. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 355 | No effect on hydrolytic activity compared to wild-type; when associated with F-304 and G-357. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, G-357 and F-806. | ||||
Sequence: Y → H | ||||||
Mutagenesis | 357 | No effect on hydrolytic activity compared to wild-type; when associated with F-304 and H-355. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and F-806. | ||||
Sequence: N → G | ||||||
Mutagenesis | 806 | 43% loss of hydrolytic activity against lactose compared to wild-type. 58% reduction in hydrolytic activity compared to wild-type; when associated with F-304, H-355 and G-357. | ||||
Sequence: W → F | ||||||
Mutagenesis | 806 | 90% loss of hydrolytic activity against lactose compared to wild-type. | ||||
Sequence: W → S |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKLSSACAIALLAAQAAG | ||||||
Chain | PRO_5000219458 | 19-1007 | Beta-galactosidase A | |||
Sequence: ASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLDIFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLRSSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASASGNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLNNEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASPGNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVSGTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDLKILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLFINGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSDYGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNMGLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSPLEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWLAVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAY | ||||||
Glycosylation | 156 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 205↔206 | |||||
Sequence: CC | ||||||
Disulfide bond | 266↔315 | |||||
Sequence: CANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAAC | ||||||
Glycosylation | 402 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 422 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 478 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 522 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 622 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 739 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 760 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 777 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 805 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 914 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,007
- Mass (Da)109,712
- Last updated2007-03-06 v1
- ChecksumCD1E91854D7A8A0A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM269982 EMBL· GenBank· DDBJ | CAK44114.1 EMBL· GenBank· DDBJ | Genomic DNA |