Q3ECS3 · BGL35_ARATH
- ProteinMyrosinase 5
- GeneTGG5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids511 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside.
Miscellaneous
It seems that the absence of a catalytic proton donor in plant myrosinases is not impairing the hydrolysis of glucosinolates.
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
547 μM | sinigrin | 4.5 | ||||
80 mM | p-nitrophenyl beta-D-glucoside | 4.5 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
48.1 μmol/min/mg | 4.5 | with sinigrin as substrate | |||
17 μmol/min/mg | 4.5 | with p-nitrophenyl beta-D-glucoside as substrate |
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 165 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 210-211 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: NQ | ||||||
Binding site | 351 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 418 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 418 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 467 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 474-475 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: EF | ||||||
Binding site | 483 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | beta-glucosidase activity | |
Molecular Function | glucosinolate glucohydrolase activity | |
Molecular Function | scopolin beta-glucosidase activity | |
Molecular Function | thioglucosidase activity | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMyrosinase 5
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ3ECS3
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MAIPKAHYSLAVLVLLFVVVSSS | ||||||
Chain | PRO_0000389597 | 24-511 | Myrosinase 5 | |||
Sequence: QKVCNPECKAKEPFHCDNTHAFNRSGFPKNFTFGAATSAYQIEGAAHRALNGWDYFTHRYPEKVPDRSSADLACDSYDLYKDDVKLLKRMNVQAYRLSIAWSRVLPKGRLTGGVDENGITYYNNLINELKANGIEPYVTIFHWDVPQTLEDEYGGFLSTRIVEDYTNYAELLFQRFGDRVKFWITLNQPLSLALKGYGNGSYPPGRCTGCELGGDSGVEPYTVAHNQLLAHAKTVSLYRKRYQKFQGGKIGTTLIGRWFVPLNEFSELDKAAAKRAFDFFVGWFLDPLVYGKYPTIMREMVGDRLPEFTPEESALVKGSLDFLGLNYYVSQYATDAPPPTQPNAITDARVTLGFYRNGSPIGVVASSFVYYPPGFRQILNYIKDNYKNPLTYITENGVADLDLGNVTLATALADNGRIQNHCSHLSCLKCAMKDGCNVAGYFAWSLMDNYEFGNGYTLRFGMNWVNFTNPADRKEKASGKWFSKFLAK | ||||||
Disulfide bond | 31↔450 | |||||
Sequence: CKAKEPFHCDNTHAFNRSGFPKNFTFGAATSAYQIEGAAHRALNGWDYFTHRYPEKVPDRSSADLACDSYDLYKDDVKLLKRMNVQAYRLSIAWSRVLPKGRLTGGVDENGITYYNNLINELKANGIEPYVTIFHWDVPQTLEDEYGGFLSTRIVEDYTNYAELLFQRFGDRVKFWITLNQPLSLALKGYGNGSYPPGRCTGCELGGDSGVEPYTVAHNQLLAHAKTVSLYRKRYQKFQGGKIGTTLIGRWFVPLNEFSELDKAAAKRAFDFFVGWFLDPLVYGKYPTIMREMVGDRLPEFTPEESALVKGSLDFLGLNYYVSQYATDAPPPTQPNAITDARVTLGFYRNGSPIGVVASSFVYYPPGFRQILNYIKDNYKNPLTYITENGVADLDLGNVTLATALADNGRIQNHCSHLSC | ||||||
Disulfide bond | 39↔445 | |||||
Sequence: CDNTHAFNRSGFPKNFTFGAATSAYQIEGAAHRALNGWDYFTHRYPEKVPDRSSADLACDSYDLYKDDVKLLKRMNVQAYRLSIAWSRVLPKGRLTGGVDENGITYYNNLINELKANGIEPYVTIFHWDVPQTLEDEYGGFLSTRIVEDYTNYAELLFQRFGDRVKFWITLNQPLSLALKGYGNGSYPPGRCTGCELGGDSGVEPYTVAHNQLLAHAKTVSLYRKRYQKFQGGKIGTTLIGRWFVPLNEFSELDKAAAKRAFDFFVGWFLDPLVYGKYPTIMREMVGDRLPEFTPEESALVKGSLDFLGLNYYVSQYATDAPPPTQPNAITDARVTLGFYRNGSPIGVVASSFVYYPPGFRQILNYIKDNYKNPLTYITENGVADLDLGNVTLATALADNGRIQNHC | ||||||
Glycosylation | 46 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 53 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 222 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 230↔233 | |||||
Sequence: CTGC | ||||||
Glycosylation | 428 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 489 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length511
- Mass (Da)57,468
- Last updated2005-11-08 v1
- Checksum0CEA34FA0DFB95B5
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FJ268796 EMBL· GenBank· DDBJ | ACO95140.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC024261 EMBL· GenBank· DDBJ | AAG52628.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE32671.1 EMBL· GenBank· DDBJ | Genomic DNA |