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RHOMR:O52754

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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

PMID:9799108[1]

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
CACAO 4481

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000757
InterPro:IPR008263

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000757
InterPro:IPR008263

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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