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P37356 - AMAA_GEOTM
N-acyl-L-amino acid amidohydrolase
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P37356|AMAA_GEOTM N-acyl-L-amino acid amidohydrolase (Fragment) OS=Geobacillus thermoglucosidasius PE=1 SV=1 MTNEEIKRLVDEVKEGVIAXRRHL
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<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 activityiAn N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.
<p>Provides information relevant to cofactors. A cofactor is any non-protein substance required for an enzyme to be catalytically active. Some cofactors are inorganic, such as metal ions in various oxidation states. Others, such as most vitamins, are organic molecules.</p><p><a href='../manual/cofactor' target='_top'>More...</a></p>CofactoriCobalt.By similarity
- aminoacylase activity Source: UniProtKB-EC
<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - LigandiCobaltRecommended name:N-acyl-L-amino acid amidohydrolase (EC:220.127.116.11)Short name:L-aminoacylase
Geobacillus thermoglucosidasius (Bacillus thermoglucosidasius) 1426 [NCBI] cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus
<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini 1 – ›24 ›24 N-acyl-L-amino acid amidohydrolase PRO_0000061950 Add
<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureiHomotetramer.Belongs to the peptidase M20 family.Curated
<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:24Mass (Da):2,848Last modified:October 1, 1994 - 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:iBC954E4D2B0EC64A
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 24 – 24 1
3D structure databases
Database of comparative protein structure models<br/><a href='/database/63'>More..</a> ModBasei Search... Search...
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Family and domain databases
Search... AMAA_GEOTM P37356Primary (citable) accession number: P37356 Integrated into UniProtKB/Swiss-Prot: October 1, 1994 Last sequence update: October 1, 1994 Last modified: October 1, 2014 This is version 48 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
- Peptidase familiesClassification of peptidase families and list of entries
- SIMILARITY commentsIndex of protein domains and families
External DataDasty 3