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| | <StructureSection load='1t4c' size='340' side='right'caption='[[1t4c]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='1t4c' size='340' side='right'caption='[[1t4c]], [[Resolution|resolution]] 2.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t4c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35274 Atcc 35274]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t4c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=OXD:OXALIC+ACID'>OXD</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OXX:OXALYL-ASPARTYL+ANHYDRIDE'>OXX</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4c OCA], [https://pdbe.org/1t4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4c RCSB], [https://www.ebi.ac.uk/pdbsum/1t4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4c ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p5h|1p5h]], [[1p5r|1p5r]], [[1vgq|1vgq]], [[1vgr|1vgr]], [[1t3z|1t3z]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FRC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=847 ATCC 35274])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyl-CoA_transferase Formyl-CoA transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.16 2.8.3.16] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4c OCA], [http://pdbe.org/1t4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t4c RCSB], [http://www.ebi.ac.uk/pdbsum/1t4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FCTA_OXAFO FCTA_OXAFO]] Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy.[HAMAP-Rule:MF_00742] | + | [https://www.uniprot.org/uniprot/FCTA_OXAFO FCTA_OXAFO] Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy.[HAMAP-Rule:MF_00742] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35274]] | |
| - | [[Category: Formyl-CoA transferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jonsson, S]] | + | [[Category: Oxalobacter formigenes]] |
| - | [[Category: Lindqvist, Y]] | + | [[Category: Jonsson S]] |
| - | [[Category: Ricagno, S]]
| + | [[Category: Lindqvist Y]] |
| - | [[Category: Richards, N G]] | + | [[Category: Ricagno S]] |
| - | [[Category: Anhydride]] | + | [[Category: Richards NG]] |
| - | [[Category: Caib-baif family]] | + | |
| - | [[Category: Coa transferase]]
| + | |
| - | [[Category: Intertwined]]
| + | |
| - | [[Category: Knotted fold]]
| + | |
| - | [[Category: Oxalate]]
| + | |
| - | [[Category: Oxalate degradation]]
| + | |
| - | [[Category: Oxalyl-coa]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
FCTA_OXAFO Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy.[HAMAP-Rule:MF_00742]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Oxalobacter formigenes is an obligate anaerobe that colonizes the human gastrointestinal tract and employs oxalate breakdown to generate ATP in a novel process involving the interplay of two coupled enzymes and a membrane-bound oxalate:formate antiporter. Formyl-CoA transferase is a critical enzyme in oxalate-dependent ATP synthesis and is the first Class III CoA-transferase for which a high resolution, three-dimensional structure has been determined (Ricagno, S., Jonsson, S., Richards, N., and Lindqvist, Y. (2003) EMBO J. 22, 3210-3219). We now report the first detailed kinetic characterizations of recombinant, wild type formyl-CoA transferase and a number of site-specific mutants, which suggest that catalysis proceeds via a series of anhydride intermediates. Further evidence for this mechanistic proposal is provided by the x-ray crystallographic observation of an acylenzyme intermediate that is formed when formyl-CoA transferase is incubated with oxalyl-CoA. The catalytic mechanism of formyl-CoA transferase is therefore established and is almost certainly employed by all other members of the Class III CoA-transferase family.
Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes.,Jonsson S, Ricagno S, Lindqvist Y, Richards NG J Biol Chem. 2004 Aug 20;279(34):36003-12. Epub 2004 Jun 21. PMID:15213226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jonsson S, Ricagno S, Lindqvist Y, Richards NG. Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes. J Biol Chem. 2004 Aug 20;279(34):36003-12. Epub 2004 Jun 21. PMID:15213226 doi:http://dx.doi.org/10.1074/jbc.M404873200
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