Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR000587 is a Creatinase, N-terminal.
<p>Creatinase or creatine amidinohydrolase ([ec:3.5.3.3]) catalyses the conversion of creatine and water to sarcosine and urea. The enzyme works as a homodimer, and is induced by choline chloride. Each monomer of creatinase has two clearly defined domains, a small N-terminal domain, and a large C-terminal domain.</p> <p>The structure of the C-terminal region represents the "pita-bread" fold [[cite:PUB00103861], [cite:PUB00103862]]. The fold contains both α-helices and an anti-parallel β-sheet within two structurally similar domains that are thought to be derived from an ancient gene duplication. The active site, where conserved, is located between the two domains. The fold is common to methionine aminopeptidase ([ec:3.4.11.18]), aminopeptidase P ([ec:3.4.11.9]), prolidase ([ec:3.4.13.9]), agropine synthase and creatinase ([ec:3.5.3.3]). Though many of these peptidases require a divalent cation, creatinase is not a metal-dependent enzyme [[cite:PUB00044073], [cite:PUB00026792], [cite:PUB00000379]].</p> <p>This entry represents the N-terminal domain of creatinase, aminopeptidase P, prolidases and similar proteins.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: probable Xaa-Pro aminopeptidase P-like [Glycine max] gi|356573012|ref|XP_003554659.1| | 18 | ||
| – | Xaa-pro aminopeptidase, putative; TAIR: AT3G05350.1 Metallopeptidase M24 family protein; Swiss-Prot: sp|D1ZKF3|AMPP1_SORMK Probable Xaa-Pro aminopeptidase P; TrEMBL-Plants: tr|A0A0R0F3E9|A0A0R0F3E9_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0773100 | 18 | ||
| – | Xaa-pro aminopeptidase, putative; TAIR: AT4G36760.1 aminopeptidase P1; Swiss-Prot: sp|D1ZKF3|AMPP1_SORMK Probable Xaa-Pro aminopeptidase P; TrEMBL-Plants: tr|G7KC66|G7KC66_MEDTR Xaa-pro aminopeptidase P; Found in the gene: LotjaGi2g1v0393500 | 18 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01085 | CDD | 1 | 33.33 |