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2hji
From Proteopedia
(Difference between revisions)
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<StructureSection load='2hji' size='340' side='right'caption='[[2hji]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | <StructureSection load='2hji' size='340' side='right'caption='[[2hji]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2hji]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2hji]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_oxytocus_perniciosus"_flugge_1886 "bacillus oxytocus perniciosus" flugge 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zrr|1zrr]], [[1vr3|1vr3]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zrr|1zrr]], [[1vr3|1vr3]]</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/Acireductone_dioxygenase_(Fe(2+)-requiring) Acireductone dioxygenase (Fe(2+)-requiring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.54 1.13.11.54] </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=2hji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hji OCA], [https://pdbe.org/2hji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hji RCSB], [https://www.ebi.ac.uk/pdbsum/2hji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hji ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MTND_KLEOX MTND_KLEOX]] Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.<ref>PMID:8407993</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 11:09, 5 January 2022
Structural model for the Fe-containing isoform of acireductone dioxygenase
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