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5zqi

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Current revision (09:03, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5zqi' size='340' side='right'caption='[[5zqi]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='5zqi' size='340' side='right'caption='[[5zqi]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zqi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZQI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Defluviitalea Defluviitalea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZQI FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqi OCA], [http://pdbe.org/5zqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zqi RCSB], [http://www.ebi.ac.uk/pdbsum/5zqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqi ProSAT]</span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zqi OCA], [https://pdbe.org/5zqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zqi RCSB], [https://www.ebi.ac.uk/pdbsum/5zqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zqi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A4V8GZK9_9FIRM A0A4V8GZK9_9FIRM]
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Brown algae are one of the largest groups of oceanic primary producers for CO2 removal and carbon sinks for coastal regions. However, the mechanism for brown alga assimilation remains largely unknown in thermophilic microorganisms. In this work, a thermophilic alginolytic community was enriched from coastal sediment, from which an obligate anaerobic and thermophilic bacterial strain, designated Alg1, was isolated. Alg1 shared a 16S rRNA gene identity of 94.6% with Defluviitalea saccharophila LIND6LT2(T). Phenotypic, chemotaxonomic, and phylogenetic studies suggested strain Alg1 represented a novel species of the genus Defluviitalea, for which the name Defluviitalea phaphyphila sp. nov. is proposed. Alg1 exhibited an intriguing ability to convert carbohydrates of brown algae, including alginate, laminarin, and mannitol, to ethanol and acetic acid. Three gene clusters participating in this process were predicted to be in the genome, and candidate enzymes were successfully expressed, purified, and characterized. Six alginate lyases were demonstrated to synergistically deconstruct alginate into unsaturated monosaccharide, followed by one uronic acid reductase and two 2-keto-3-deoxy-d-gluconate (KDG) kinases to produce pyruvate. A nonclassical mannitol 1-phosphate dehydrogenase, catalyzing D-mannitol 1-phosphate to fructose 1-phosphate in the presence of NAD(+), and one laminarase also were disclosed. This work revealed that a thermophilic brown alga-decomposing system containing numerous novel thermophilic alginate lyases and a unique mannitol 1-phosphate dehydrogenase was adopted by the natural ethanologenic strain Alg1 during the process of evolution in hostile habitats.
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Defluviitalea phaphyphila sp. nov., a Novel Thermophilic Bacterium That Degrades Brown Algae.,Ji SQ, Wang B, Lu M, Li FL Appl Environ Microbiol. 2015 Nov 20;82(3):868-77. doi: 10.1128/AEM.03297-15., Print 2016 Feb 1. PMID:26590273<ref>PMID:26590273</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5zqi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Defluviitalea]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dong, S]]
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[[Category: Dong S]]
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[[Category: Feng, Y G]]
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[[Category: Feng YG]]
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[[Category: Ji, S Q]]
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[[Category: Ji SQ]]
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[[Category: Li, F L]]
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[[Category: Li FL]]
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[[Category: Lu, M]]
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[[Category: Lu M]]
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[[Category: Su, H]]
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[[Category: Su H]]
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[[Category: Alginate lyase]]
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[[Category: B-sandwich fold]]
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[[Category: Lyase]]
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[[Category: Pl7]]
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Current revision

Alginate lyase AlgAT5 from Polysaccharide Lyase family 7

PDB ID 5zqi

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