Summary: Cyclo-malto-dextrinase C-terminal domain
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Cyclo-malto-dextrinase C-terminal domain Provide feedback
This domain is at the very C-terminus of cyclo-malto-dextrinase proteins and consists of 8 beta strands, is largely globular and appears to help stabilise the acitve sites created by upstream domains, Cyc-maltodext_N PF09087 and Alpha-amylase PF00128. Cyclo-malto-dextrinases hydrolyse cyclodextrans to maltose and glucose and catalyse trans-glycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules.
Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B; , Biochim Biophys Acta. 2000;1478:165-185.: Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family. PUBMED:10825529 EPMC:10825529
Internal database links
|Similarity to PfamA using HHSearch:||Alpha-amylase_C Glyco_hydro_42C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019492
This domain is at the very C terminus of cyclo-malto-dextrinase proteins and consists of 8 beta strands, is largely globular and appears to help stabilise the active sites created by upstream domains, INTERPRO, and INTERPRO. Cyclo-malto-dextrinases hydrolyse cyclodextrans to maltose and glucose and catalyse trans-glycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules.
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This domain is C-terminal to the catalytic beta/alpha barrel domain. The superfamily includes the C-terminal domain of a number of sugar-lytic families.
The clan contains the following 8 members:Alpha-amylase_C CBM_20 CBM_48 Cyc-maltodext_C DUF1939 DUF1966 DUF3459 Glyco_hydro_42C
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Gene3D, pdb_1h3g|
|Author:||Finn RD, Coggill PC|
|Number in seed:||32|
|Number in full:||208|
|Average length of the domain:||79.20 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||13.36 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Cyc-maltodext_C domain has been found. There are 12 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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