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| | <StructureSection load='1dk4' size='340' side='right'caption='[[1dk4]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1dk4' size='340' side='right'caption='[[1dk4]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dk4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dk4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DK4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1awb|1awb]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </span></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=1dk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk4 OCA], [https://pdbe.org/1dk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk4 ProSAT]</span></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=1dk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dk4 OCA], [https://pdbe.org/1dk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dk4 RCSB], [https://www.ebi.ac.uk/pdbsum/1dk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dk4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BSUHB_METJA BSUHB_METJA]] Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.<ref>PMID:11062561</ref> <ref>PMID:9647837</ref>
| + | [https://www.uniprot.org/uniprot/BSUHB_METJA BSUHB_METJA] Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.<ref>PMID:11062561</ref> <ref>PMID:9647837</ref> |
| | == 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 43067]] | |
| - | [[Category: Inositol-phosphate phosphatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, L]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Johnson, K A]] | + | [[Category: Chen L]] |
| - | [[Category: Roberts, M F]] | + | [[Category: Johnson KA]] |
| - | [[Category: Stec, B]] | + | [[Category: Roberts MF]] |
| - | [[Category: Yang, H]] | + | [[Category: Stec B]] |
| - | [[Category: Complexed with zn and pi]]
| + | [[Category: Yang H]] |
| - | [[Category: Homodimer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
BSUHB_METJA Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.[1] [2]
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
In sequenced genomes, protein coding regions with unassigned function constitute between 10 and 50% of all open reading frames. Often key enzymes cannot be identified using sequence homology searches. For example, despite the fact that methanogens have an apparently functional gluconeogenesis pathway, standard tools have been unable to identify a fructose-1,6-bisphosphatase (FBPase) gene in the sequenced Methanoccocus jannaschii genome. Using a combination of functional and structural tools, we have shown that the protein product of the M. jannaschii gene MJ0109, which had been tentatively annotated as an inositol monophosphatase (IMPase), has both IMPase and FBPase activities. Moreover, several gene products annotated as IMPases from different thermophilic organisms also possess FBPase activity. Thus, we have found the FBPase that was 'missing' in thermophiles and shown that it also functions as an IMPase.
MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase.,Stec B, Yang H, Johnson KA, Chen L, Roberts MF Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
- ↑ Chen L, Roberts MF. Cloning and expression of the inositol monophosphatase gene from Methanococcus jannaschii and characterization of the enzyme. Appl Environ Microbiol. 1998 Jul;64(7):2609-15. PMID:9647837
- ↑ Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
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