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InterPro: IPR012850 Alpha-amylase, C-terminal beta-sheet

Protein matchesHelp
UniProtKB
Matches:
159 proteins
AccessionHelp IPR012850 A-amylase_bs_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR013775 Alpha-amylase, plant
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004556 alpha-amylase activity
GO:0005509 calcium ion binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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].

Structural linksHelp
SCOP: b.71.1.1 , c.1.8.1
Database linksHelp
Enzyme: EC:3.2.1.1
PANDIT: PF07821
Blocks: IPB012850

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012850 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR006046 Glycoside hydrolase family 13
IPR006589 Glycosyl hydrolase, family 13, subfamily, catalytic domain
IPR006047 Glycosyl hydrolase, family 13, catalytic domain
IPR017853 Glycoside hydrolase, catalytic core
IPR012850 Alpha-amylase, C-terminal beta-sheet
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp
1. 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
2. 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
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. 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
6. 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
7. 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
8. McDowall J.
Protein of the Month ? alpha-Amylase.
2006

Additional ReadingHelp
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
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
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
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