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InterPro: IPR012850 Alpha-amylase, C-terminal beta-sheet
Protein matches
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UniProtKB Matches: 159 proteins |
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Accession
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IPR012850 A-amylase_bs_C |
Type
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Domain |
Signatures
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InterPro Relationships
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Found in
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IPR013775 Alpha-amylase, plant
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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O-Glycosyl 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Alpha-amylase is classified as family 13 of the glycosyl hydrolases and is present in archaea, bacteria, plants and animals. Alpha-amylase is an essential enzyme in alpha-glucan metabolism, acting to catalyse the hydrolysis of alpha-1,4-glucosidic bonds of glycogen, starch and related polysaccharides. Although all alpha-amylases possess the same catalytic function, they can vary with respect to sequence. In general, they are composed of three domains: a TIM barrel containing the active site residues and chloride ion-binding site (domain A), a long loop region inserted between the third beta strand and the alpha-helix of domain A that contains calcium-binding site(s) (domain B), and a C-terminal beta-sheet domain that appears to show some variability in sequence and length between amylases (domain C) [5]. Amylases have at least one conserved calcium-binding site, as calcium is essential for the stability of the enzyme. The chloride-binding functions to activate the enzyme, which acts by a two-step mechanism involving a catalytic nucleophile base (usually an Asp) and a catalytic proton donor (usually a Glu) that are responsible for the formation of the beta-linked glycosyl-enzyme intermediate. This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C terminus. This domain is organised as a five-stranded anti-parallel beta-sheet [6, 7].
More information about this protein can be found at Protein of the Month: alpha-Amylase [8].
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Structural links
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Database links
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Example proteins
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A2YGY2 Alpha-amylase isozyme 2A
P00693 Alpha-amylase type A isozyme
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR013775 |
Alpha-amylase, plant |
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| IPR013781 |
Glycoside hydrolase, subgroup, catalytic core |
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| IPR006046 |
Glycoside hydrolase family 13 |
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| IPR006589 |
Glycosyl hydrolase, family 13, subfamily, catalytic domain |
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| IPR006047 |
Glycosyl hydrolase, family 13, catalytic domain |
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| IPR017853 |
Glycoside hydrolase, catalytic core |
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| IPR012850 |
Alpha-amylase, C-terminal beta-sheet |
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SWISS-MODEL |
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PDB Chain |
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ModBase |
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CATH Domain |
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SCOP Domain |
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Publications
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1.
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Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995
[PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
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2.
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Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995
[PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
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3.
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Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
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4.
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Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
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5.
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Pujadas G, Palau J.
Evolution of alpha-amylases: architectural features and key residues in the stabilization of the (beta/alpha)(8) scaffold.
Mol. Biol. Evol. 18 38-54 2001
[PubMed: 11141191]
http://mbe.oxfordjournals.org/cgi/content/abstract/18/1/38.pdf
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6.
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Kadziola A, Sogaard M, Svensson B, Haser R.
Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis.
J. Mol. Biol. 278 205-17 1998
[PubMed: 9571044]
http://dx.doi.org/10.1006/jmbi.1998.1683
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7.
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Kadziola A, Abe J, Svensson B, Haser R.
Crystal and molecular structure of barley alpha-amylase.
J. Mol. Biol. 239 104-21 1994
[PubMed: 8196040]
http://dx.doi.org/10.1006/jmbi.1994.1354
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8.
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McDowall J.
Protein of the Month ? alpha-Amylase.
2006
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Additional Reading
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Robert X, Haser R, Gottschalk TE, Ratajczak F, Driguez H, Svensson B, Aghajari N.
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs.
Structure 11 2003 973-84
[PubMed: 12906828]
http://dx.doi.org/10.1016/S0969-2126(03)00151-5
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Robert X, Haser R, Mori H, Svensson B, Aghajari N.
Oligosaccharide binding to barley alpha-amylase 1.
J. Biol. Chem. 280 2005 32968-78
[PubMed: 16030022]
http://dx.doi.org/10.1074/jbc.M505515200
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Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhoft B, Willemoes M, Tranier S, Haser R, Svensson B.
The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity.
FEBS J. 274 2007 5055-67
[PubMed: 17803687]
http://dx.doi.org/10.1111/j.1742-4658.2007.06024.x
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Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B.
Multi-site substrate binding and interplay in barley alpha-amylase 1.
FEBS Lett. 582 2008 2567-71
[PubMed: 18588886]
http://dx.doi.org/10.1016/j.febslet.2008.06.027
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InterPro 23.1
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