Summary: Alpha amylase, catalytic domain
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This is the Wikipedia entry entitled "Alpha-Amylase". More...
Alpha-Amylase Edit Wikipedia article
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This is the Wikipedia entry entitled "Glycoside hydrolase family 13". More...
Glycoside hydrolase family 13 Edit Wikipedia article
| crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 1 (tvai) mutant d356n/e396q complexed with p2, a pullulan model oligosaccharide | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Alpha-amylase_N | ||||||||
| Pfam | PF02903 | ||||||||
| InterPro | IPR004185 | ||||||||
| SCOP | 1sma | ||||||||
| SUPERFAMILY | 1sma | ||||||||
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| cyclodextrin glucanotransferase (e.c.2.4.1.19) (cgtase) | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Alpha-amylase | ||||||||
| Pfam | PF00128 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR006047 | ||||||||
| SCOP | 1ppi | ||||||||
| SUPERFAMILY | 1ppi | ||||||||
| CAZy | GH13 | ||||||||
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In molecular biology, glycoside hydrolase family 13 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]
Enzymes containing this domain belong to family 13 (CAZY GH_13) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes in this family include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.
[edit] References
- ^ 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): 70907094. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41477.
- ^ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure 3 (9): 853859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
- ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
- ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
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.
Alpha amylase, catalytic domain Provide feedback
Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
Literature references
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Larson SB, Greenwood A, Cascio D, Day J, McPherson A; , J Mol Biol 1994;235:1560-1584.: Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution. PUBMED:8107092 EPMC:8107092
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Strobl S, Maskos K, Betz M, Wiegand G, Huber R, Gomis-Ruth FX, Glockshuber R; , J Mol Biol 1998;278:617-628.: Crystal structure of yellow meal worm alpha-amylase at 1.64 A resolution. PUBMED:9600843 EPMC:9600843
Internal database links
| Similarity to PfamA using HHSearch: | DUF187 hDGE_amylase |
External database links
| CAZY: | GH13 |
| HOMSTRAD: | ghf13 |
| PANDIT: | PF00128 |
| PRINTS: | PR00110 |
| Pseudofam: | PF00128 |
| SCOP: | 1ppi |
| SYSTERS: | Alpha-amylase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006047
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.
Enzymes containing this domain, such as alpha-amylase, belong to family 13 (CAZY) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.
This entry represents the catalytic domain found in several protein members of this family. It has a structure consisting of an 8 stranded alpha/beta barrel that contains the active site, interrupted by a ~70 amino acid calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain [PUBMED:16302977].
More information about this protein can be found at Protein of the Month: alpha-Amylase [PUBMED:].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | cation binding (GO:0043169) |
| catalytic activity (GO:0003824) | |
| Biological process | carbohydrate metabolic process (GO:0005975) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Glyco_hydro_tim (CL0058), which contains the following 50 members:
Alpha-amylase Alpha_L_fucos Cellulase Cellulase-like DUF187 DUF4015 DUF4038 DUF4434 GHL1-3 GHL12 GHL13 GHL15 GHL5 GHL6 Glyco_hydr_30_2 Glyco_hydro_1 Glyco_hydro_10 Glyco_hydro_101 Glyco_hydro_114 Glyco_hydro_14 Glyco_hydro_17 Glyco_hydro_18 Glyco_hydro_20 Glyco_hydro_25 Glyco_hydro_26 Glyco_hydro_2_C Glyco_hydro_3 Glyco_hydro_30 Glyco_hydro_31 Glyco_hydro_35 Glyco_hydro_39 Glyco_hydro_42 Glyco_hydro_44 Glyco_hydro_53 Glyco_hydro_56 Glyco_hydro_59 Glyco_hydro_66 Glyco_hydro_70 Glyco_hydro_72 Glyco_hydro_77 Glyco_hydro_79n Glyco_hydro_97 Glyco_hydro_cc hDGE_amylase Lipid_bd Melibiase NAGidase NAGLU Raffinose_syn XylanaseAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
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 (31) |
Full (28372) |
Representative proteomes | NCBI (23482) |
Meta (3056) |
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| RP15 (2088) |
RP35 (4020) |
RP55 (5641) |
RP75 (6746) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (31) |
Full (28372) |
Representative proteomes | NCBI (23482) |
Meta (3056) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (2088) |
RP35 (4020) |
RP55 (5641) |
RP75 (6746) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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.
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'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.
Note: You can also download the data file for the tree.
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: | Swissprot |
| Previous IDs: | alpha-amylase; |
| Type: | Domain |
| Author: | Sonnhammer ELL, Griffiths-Jones SR |
| Number in seed: | 31 |
| Number in full: | 28372 |
| Average length of the domain: | 261.10 aa |
| Average identity of full alignment: | 18 % |
| Average coverage of the sequence by the domain: | 44.76 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 316 | ||||||||||||
| Family (HMM) version: | 19 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
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Interactions
There are 17 interactions for this family. More...
DUF1939 Kunitz_legume Alpha-amylase CBM_20 DUF1966 CBM_48 Cyc-maltodext_C A_amylase_inhib Alpha-amyl_C2 DUF1964 DUF1921 DUF1923 Alpha-amylase_N TIG Cyc-maltodext_N DUF1945 Alpha-amylase_CStructures
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 Alpha-amylase domain has been found. There are 473 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence