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2uxy
From Proteopedia
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==Aliphatic amidase== | ==Aliphatic amidase== | ||
| - | <StructureSection load='2uxy' size='340' side='right' caption='[[2uxy]], [[Resolution|resolution]] 1.25Å' scene=''> | + | <StructureSection load='2uxy' size='340' side='right'caption='[[2uxy]], [[Resolution|resolution]] 1.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2uxy]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2uxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UXY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C3Y:S-[(1S)-1-HYDROXY-1-(HYDROXYAMINO)ETHYL]-L-CYSTEINE'>C3Y</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=C3Y:S-[(1S)-1-HYDROXY-1-(HYDROXYAMINO)ETHYL]-L-CYSTEINE'>C3Y</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k17|1k17]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1k17|1k17]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Amidase Amidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.4 3.5.1.4] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2uxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uxy OCA], [https://pdbe.org/2uxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uxy RCSB], [https://www.ebi.ac.uk/pdbsum/2uxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uxy ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/AMIE_PSEAE AMIE_PSEAE]] Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. Enables the organism to use acetamide as both carbon and nitrogen source.[HAMAP-Rule:MF_01242] Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates (By similarity).[HAMAP-Rule:MF_01242] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Amidase]] | [[Category: Amidase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Andrade, J]] | [[Category: Andrade, J]] | ||
Current revision
Aliphatic amidase
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