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RHOMR:O52754
Contents
Species (Taxon ID) | Rhodothermus marinus (Rhodothermus obamensis). (29549) | |
Gene Name(s) | lamR (ECO:0000313 with EMBL:AAC69707.1) | |
Protein Name(s) | Laminarinase (ECO:0000313 with EMBL:AAC69707.1) | |
External Links | ||
UniProt | O52754 | |
EMBL | AF047003 | |
PDB | 3ILN | |
PDBsum | 3ILN | |
ProteinModelPortal | O52754 | |
CAZy | GH16 | |
EvolutionaryTrace | O52754 | |
GO | GO:0004553 GO:0046872 GO:0005975 | |
Gene3D | 2.60.120.200 | |
InterPro | IPR013320 IPR000757 IPR008263 | |
Pfam | PF00722 | |
SUPFAM | SSF49899 | |
PROSITE | PS01034 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004553 |
hydrolase activity, hydrolyzing O-glycosyl compounds |
ECO:0000314 |
F |
Figures 5 and 6 confirm the hydrolase function of the LamR enzyme, which is expressed by the lamR gene. Both figures show digests separated by TLC. In figure 5, the intermediate appearance of oligosaccharides detected after a short incubation time prove that the hydrolysis of 1,3-1,4-beta-glucan and laminarin follows the endo type action pattern. In figure 6, LamR displayed a weak and significant activity against cellobiosyl-glucose G1-4G1-3Gr, which suggests that LamR is able to cut specific beta linkages only in low-molecular-mass carbohydrates. |
complete | |||||
enables |
GO:0004553 |
hydrolase activity, hydrolyzing O-glycosyl compounds |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Krah, M et al. (1998) The laminarinase from thermophilic eubacterium Rhodothermus marinus--conformation, stability, and identification of active site carboxylic residues by site-directed mutagenesis. Eur. J. Biochem. 257 101-11 PubMed GONUTS page