Summary
Carbohydrate-binding module 48 (Isoamylase N-terminal domain)
This domain is found in a range of enzymes that act on branched substrates - isoamylase, pullulanase and branching enzyme. This family also contains the beta subunit of 5' AMP activated kinase.
Literature references
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Katsuya Y, Mezaki Y, Kubota M, Matsuura Y; , J Mol Biol 1998;281:885-897.: Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution. PUBMED:9719642
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Wiatrowski HA, Van Denderen BJ, Berkey CD, Kemp BE, Stapleton D, Carlson M; , Mol Cell Biol 2004;24:352-361.: Mutations in the gal83 glycogen-binding domain activate the snf1/gal83 kinase pathway by a glycogen-independent mechanism. PUBMED:14673168
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Polekhina G, Gupta A, Michell BJ, van Denderen B, Murthy S, Feil SC, Jennings IG, Campbell DJ, Witters LA, Parker MW, Kemp BE, Stapleton D; , Curr Biol 2003;13:867-871.: AMPK beta subunit targets metabolic stress sensing to glycogen. PUBMED:12747837
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Hudson ER, Pan DA, James J, Lucocq JM, Hawley SA, Green KA, Baba O, Terashima T, Hardie DG; , Curr Biol 2003;13:861-866.: A novel domain in AMP-activated protein kinase causes glycogen storage bodies similar to those seen in hereditary cardiac arrhythmias. PUBMED:12747836
InterPro entry IPR004193
O-Glycosyl hydrolases 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, PUBMED:. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site PUBMED:. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Enzymes containing this domain belong to family 13 () of the glycosyl hydrolases. This domain is found in a range of enzymes that act on branched substrates ie. isoamylase, pullulanase and branching enzyme. Isoamylase hydrolyses 1,6-alpha-D-glucosidic branch linkages in glycogen, amylopectin and dextrin; 1,4-alpha-glucan branching enzyme functions in the formation of 1,6-glucosidic linkages of glycogen; and pullulanase is a starch-debranching enzyme.Clan
This family is a member of clan GHD (CL0369), which contains the following 7 members:
Alpha-amylase_C CBM_20 CBM_48 Cyc-maltodext_C DUF1939 DUF1966 Glyco_hydro_42CGene Ontology
| Molecular function | hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553) |
| Biological process | carbohydrate metabolic process (GO:0005975) |
Internal database links
| SCOOP: | Meleagrin |
External database links
| CAZY: | CBM_48 |
| PANDIT: | PF02922 |
| SCOP: | 1bf2 |
| SYSTERS: | CBM_48 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
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 HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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
| Seed source: | Structural domain |
| Previous IDs: | isoamylase_N; Isoamylase_N; |
| Type: | Domain |
| Author: | Griffiths-Jones SR |
| Number in seed: | 59 |
| Number in full: | 3185 |
| Average length of the domain: | 85.70 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 11.84 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 84 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
Alpha-amylaseStructures
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 CBM_48 domain has been found.
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