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3lq1
From Proteopedia
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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=3lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lq1 RCSB], [http://www.ebi.ac.uk/pdbsum/3lq1 PDBsum]</span></td></tr> | <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=3lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lq1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lq1 RCSB], [http://www.ebi.ac.uk/pdbsum/3lq1 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MEND_LISMF MEND_LISMF]] Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 03:50, 25 December 2014
Crystal structure of 2-succinyl-6-hydroxy-2,4-cyclohexadiene 1-carboxylic acid synthase/2-oxoglutarate decarboxylase FROM Listeria monocytogenes str. 4b F2365
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Categories: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase | Listeria monocytogenes | Almo, S C | Burley, S K | Freeman, J | Hu, S | Structural genomic | NYSGXRC, New York SGX Research Center for Structural Genomics | Patskovsky, Y | Sauder, J M | Toro, R | Magnesium | Manganese | Menaquinone biosynthesis | Metal-binding | Nysgrc | PSI, Protein structure initiative | Sephchc synthase | Thiamine pyrophosphate | Transferase
