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Items: 6

1.

glycoside hydrolase family 2 protein

glycoside hydrolase family 2 protein such as beta-galactosidase and beta-mannosidase, which catalyze the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides and beta-D-mannose residues in beta-D-mannosides, respectively

Date:
2024-12-06
Family Accession:
14311996
Method:
Sparcle
2.

DUF4982 domain-containing protein

This domain is found towards the C terminus of Beta-glucuronidase from Formosa agariphila (P17_GH2) and similar proteins mainly from bacteria and fungi. P17_GH2 is involved in the degradation of the polysaccharide ulvan. The function of this domain, which shows an all-beta structure, is unknown [1]. [1]. 31285597. A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan. Reisky L, Prechoux A, Zuhlke MK, Baumgen M, Robb CS, Gerlach N, Roret T, Stanetty C, Larocque R, Michel G, Song T, Markert S, Unfried F, Mihovilovic MD, Trautwein-Schult A, Becher D, Schweder T, Bornscheuer UT, Hehemann JH;. Nat Chem Biol. 2019;15:803-812. (from Pfam)

Date:
2024-10-16
Family Accession:
NF027673.5
Method:
HMM
3.

glycosyl hydrolase 2 galactose-binding domain-containing protein

This domain is found in a number of proteins belonging to glycosyl hydrolase 2 family [1-5]. Paper describing PDB structure 1bhg. [1]. 8599764. Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH;. Nat Struct Biol. 1996;3:375-381. Paper describing PDB structure 1dp0. [2]. 11045615. High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW;. Protein Sci. 2000;9:1685-1699. Paper describing PDB structure 1jyn. [3]. 11732897. A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW;. Biochemistry. 2001;40:14781-14794. Paper describing PDB structure 1px3. [4]. 14621996. Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Juers DH, Hakda S, Matthews BW, Huber RE;. Biochemistry. 2003;42:13505-13511. Paper describing PDB structure 1yq2. [5]. 16171818. Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. Skalova T, Dohnalek J, Spiwok V, Lipovova P, Vondrackova E, Petrokova H, Duskova J, Strnad H, Kralova B, Hasek J;. J Mol Biol. 2005;353:282-294. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046887.1
Method:
HMM
4.

Glycoside hydrolase family 2 C-terminal domain 5

Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme [1]. [1]. 27599737. Structural studies of a cold-adapted dimeric beta-D-galactosidase from Paracoccus sp. 32d. Rutkiewicz-Krotewicz M, Pietrzyk-Brzezinska AJ, Sekula B, Cieslinski H, Wierzbicka-Wos A, Kur J, Bujacz A;. Acta Crystallogr D Struct Biol. 2016;72:1049-1061. (from Pfam)

Date:
2024-10-16
Family Accession:
NF037850.5
Method:
HMM
5.

sugar-binding domain-containing protein

This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Biological Process:
carbohydrate metabolic process (GO:0005975)
Date:
2024-10-16
Family Accession:
NF014851.5
Method:
HMM
6.

Glycosyl hydrolases family 2

This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. [1]. 8008071. Three-dimensional structure of beta-galactosidase from E. coli. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW;. Nature. 1994;369:761-766. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)
Biological Process:
carbohydrate metabolic process (GO:0005975)
Date:
2024-10-16
Family Accession:
NF012906.5
Method:
HMM
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