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Links from Protein

Items: 7

1.

glycoside hydrolase family 95-like protein

This domain is found in Alpha-fucosidase from Bifidobacterium bifidum (AfcA) and in other members of the glycoside hydrolase family 95 from bacteria and plants. AfcA hydrolyses the glycosidic linkage of Fuc1-2Gal via an inverting mechanism. This entry represents the C-terminal beta domain present within the catalytic region of this protein. The domain forms a two- layered jelly roll fold. Its specific function remains unknown [1,2]. Paper describing PDB structure 2eab. [1]. 17459873. Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum. Nagae M, Tsuchiya A, Katayama T, Yamamoto K, Wakatsuki S, Kato R;. J Biol Chem. 2007;282:18497-18509. Paper describing PDB structure 4ufc. [2]. 26112186. Glycan complexity dictates microbial resource allocation in the large intestine. Rogowski A, Briggs JA, Mortimer JC, Tryfona T, Terrapon N, Lowe EC, Basle A, Morland C, Day AM, Zheng H, Rogers TE, Thompson P, Hawkins AR, Yadav MP, Henrissat B, Martens EC, Dupree P, Gilbert HJ, Bolam DN;. Nat Commun. 2015;6:7481. (from Pfam)

Date:
2024-10-16
Family Accession:
NF045341.2
Method:
HMM
2.

glycosyl hydrolase family 95 catalytic domain-containing protein

The founding member of the GH95 family of glycosyl hydrolases is alpha-1,2-fucosidase that catalyses the hydrolysis of an alpha-1,2-linked fucose. A member of this family, FucOB from A. muciniphila was shown to hydrolyse all three types of H antigen structures to obtain the afucosylated Bombay phenotype [6]. Members of this family are multidomain proteins and contain a central catalytic domain with an (alpha/alpha)6 helical barrel topology, represented by this entry. Paper describing PDB structure 1h54. [1]. 11587643. Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases. Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H;. Structure (Camb) 2001;9:689-697. Paper describing PDB structure 2eab. [2]. 17459873. Structural basis of the catalytic reaction mechanism of novel 1,2-alpha-L-fucosidase from Bifidobacterium bifidum. Nagae M, Tsuchiya A, Katayama T, Yamamoto K, Wakatsuki S, Kato R;. J Biol Chem. 2007;282:18497-18509. Paper describing PDB structure 3wiq. [3]. 24255995. Structural and mutational analysis of substrate recognition in kojibiose phosphorylase. Okada S, Yamamoto T, Watanabe H, Nishimoto T, Chaen H, Fukuda S, Wakagi T, Fushinobu S;. FEBS J. 2014;281:778-786. Paper describing PDB structure 4ufc. [4]. 26112186. Glycan complexity dictates microbial resource allocation in the large intestine. Rogowski A, Briggs JA, Mortimer JC, Tryfona T, Terrapon N, Lowe EC, Basle A, Morland C, Day AM, Zheng H, Rogers TE, Thompson P, Hawkins AR, Yadav MP, Henrissat B, Martens EC, Dupree P, Gilbert HJ, Bolam DN;. Nat Commun. 2015;6:7481. Paper describing PDB str. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-10-16
Family Accession:
NF046196.1
Method:
HMM
3.

glycoside hydrolase N-terminal domain-containing protein

This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025851.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

glycoside hydrolase family 95 protein

glycoside hydrolase family 95 protein such as alpha-L-fucosidase, which hydrolyzes alpha-1,2-linked fucose and is involved in the degradation of fucosylated xyloglucans

Date:
2023-09-17
Family Accession:
10628485
Method:
Sparcle
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