Your basket is currently empty.
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
P80072 - MALT_BACTQ
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P80072|MALT_BACTQ Maltase (Fragment) OS=Bacillus thermoamyloliquefaciens PE=1 SV=1 MKKAWWKEGVVYQIY
- Add to basket
- Help video
Select a section on the left to see content.
<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityiHydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
- maltose alpha-glucosidase activity Source: UniProtKB-EC
Protein family/group databases
Carbohydrate-Active enZymes<br/><a href='/database/136'>More..</a>CAZyi GH13. Glycoside Hydrolase Family 13.Recommended name:Maltase (EC:184.108.40.206)Alternative name(s):Alpha-glucosidase I Bacillus thermoamyloliquefaciens 1425 [NCBI] cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus
Feature key Position(s) Length Description Graphical view Feature identifier Actions 1 – ›15 ›15 Maltase PRO_0000054326 Add
BLASTBelongs to the glycosyl hydrolase 13 family.Curated
<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei
<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusi: Fragment.Length:15Mass (Da):1,929Last modified:August 1, 1992 - v1<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i62B4CE501F2D3042
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.</p><p><a href='../manual/non_ter' target='_top'>More...</a></p>Non-terminal residuei 15 – 15 1
Protein sequence database of the Protein Information Resource<br/><a href='/database/78'>More..</a>PIRi S21240.
Protein sequence database of the Protein Information Resource<br/><a href='/database/78'>More..</a> PIRi S21240.
3D structure databases
Database of comparative protein structure models<br/><a href='/database/63'>More..</a> ModBasei Search... Search...
Protein family/group databases
Carbohydrate-Active enZymes<br/><a href='/database/136'>More..</a> CAZyi GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
Structural Biology Knowledgebase Search...
Family and domain databases
- "Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition."
Suzuki Y., Yonezawa K., Hattori M., Takii Y.
Eur. J. Biochem. 205:249-256(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE.Strain: KP1071 / FERM P8477.
MALT_BACTQ P80072Primary (citable) accession number: P80072 Integrated into UniProtKB/Swiss-Prot: August 1, 1992 Last sequence update: August 1, 1992 Last modified: October 1, 2014 This is version 39 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
- Glycosyl hydrolasesClassification of glycosyl hydrolase families and list of entries
- SIMILARITY commentsIndex of protein domains and families
External DataDasty 3