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2  structures 1435  species 0  interactions 1977  sequences 29  architectures

Family: Glyco_hydro_65m (PF03632)

Summary: Glycosyl hydrolase family 65 central catalytic domain

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This is the Wikipedia entry entitled "Glycoside hydrolase family 65". More...

Glycoside hydrolase family 65 Edit Wikipedia article

Glycosyl hydrolase family 65, N-terminal domain
PDB 1h54 EBI.jpg
maltose phosphorylase from lactobacillus brevis
Identifiers
Symbol Glyco_hydro_65N
Pfam PF03636
Pfam clan CL0103
InterPro IPR005196
SCOP 1h54
SUPERFAMILY 1h54
CAZy GH65
Glycosyl hydrolase family 65 central catalytic domain
PDB 1h54 EBI.jpg
maltose phosphorylase from lactobacillus brevis
Identifiers
Symbol Glyco_hydro_65m
Pfam PF03632
Pfam clan CL0059
InterPro IPR005195
SCOP 1h54
SUPERFAMILY 1h54
CAZy GH65
Glycosyl hydrolase family 65, C-terminal domain
PDB 1h54 EBI.jpg
maltose phosphorylase from lactobacillus brevis
Identifiers
Symbol Glyco_hydro_65C
Pfam PF03633
InterPro IPR005194
SCOP 1h54
SUPERFAMILY 1h54
CAZy GH65

In molecular biology, glycoside hydrolase family 65 is a family of glycoside hydrolases.

Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]

This family of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase and maltose phosphorylases. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose.

It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown.[6] The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom.[6] The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity[6] although its precise function remains unknown.

References[edit]

  1. ^ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. 
  2. ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779. 
  3. ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ^ a b c van Tilbeurgh H, Egloff MP, Uppenberg J, Haalck L (2001). "Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases". Structure 9 (8): 689–697. doi:10.1016/S0969-2126(01)00626-8. PMID 11587643. 

This article incorporates text from the public domain Pfam and InterPro IPR005194

This article incorporates text from the public domain Pfam and InterPro IPR005195

This article incorporates text from the public domain Pfam and InterPro IPR005196

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Glycosyl hydrolase family 65 central catalytic domain Provide feedback

This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom [1]. The catalytic domain also forms the majority of the dimerisation interface.

Literature references

  1. Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H; , Structure (Camb) 2001;9:689-697.: Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases. PUBMED:11587643 EPMC:11587643


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005195

O-Glycosyl hydrolases (EC) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [PUBMED:7624375, PUBMED:8535779]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

The family of glycosyl hydrolases (CAZY) which contains this domain includes vacuolar acid trehalase and maltose phosphorylase. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucelophilic attack on the anomeric carbon atom [PUBMED:11587643]. The catalytic domain also forms the majority of the dimerisation interface.

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(16)
Full
(1977)
Representative proteomes NCBI
(1594)
Meta
(109)
RP15
(155)
RP35
(305)
RP55
(432)
RP75
(510)
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Format an alignment

  Seed
(16)
Full
(1977)
Representative proteomes NCBI
(1594)
Meta
(109)
RP15
(155)
RP35
(305)
RP55
(432)
RP75
(510)
Alignment:
Format:
Order:
Sequence:
Gaps:
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  Seed
(16)
Full
(1977)
Representative proteomes NCBI
(1594)
Meta
(109)
RP15
(155)
RP35
(305)
RP55
(432)
RP75
(510)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_3470 (release 7.0)
Previous IDs: none
Type: Family
Author: Finn RD
Number in seed: 16
Number in full: 1977
Average length of the domain: 362.80 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 46.01 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.1
Noise cut-off 26.9 26.8
Model length: 370
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Glyco_hydro_65m domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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