Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (7,8-dihydropterin-6-yl)methyl diphosphate Identifier CHEBI:72950 Charge -3 Formula C7H8N5O8P2 InChIKeyhelp_outline FCQGJGLSOWZZON-UHFFFAOYSA-K SMILEShelp_outline Nc1nc2NCC(COP([O-])(=O)OP([O-])([O-])=O)=Nc2c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-(β-D-ribofuranosyl)aminobenzene 5'-phosphate Identifier CHEBI:72778 Charge -2 Formula C11H14NO7P InChIKeyhelp_outline UKBUHWIOGWAJEO-DBIOUOCHSA-L SMILEShelp_outline Nc1ccc(cc1)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,085 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-[(7,8-dihydropterin-6-yl)methyl]-4-(β-D-ribofuranosyl)aniline 5'-phosphate Identifier CHEBI:72951 Charge -2 Formula C18H21N6O8P InChIKeyhelp_outline VNLUYZYZRAWLHI-NGFQHRJXSA-L SMILEShelp_outline Nc1nc2NCC(CNc3ccc(cc3)[C@@H]3O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]3O)=Nc2c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:35951 | RHEA:35952 | RHEA:35953 | RHEA:35954 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Identifying two ancient enzymes in Archaea using predicted secondary structure alignment.
Xu H., Aurora R., Rose G.D., White R.H.
It is now possible to compare life forms at high levels of detail and completeness due to the increasing availability of whole genomes from all three domains. However, exploration of interesting hypotheses requires the ability to recognize a correspondence between proteins that may since have dive ... >> More
It is now possible to compare life forms at high levels of detail and completeness due to the increasing availability of whole genomes from all three domains. However, exploration of interesting hypotheses requires the ability to recognize a correspondence between proteins that may since have diverged beyond the threshold of detection by sequence-based methods. Since protein structure is far better conserved than protein sequence, structural information can enhance detection sensitivity, and this is the basis for the field of structural genomics. Demonstrating the effectiveness of this approach, we identify two important but previously elusive Archaeal enzymes: a homolog of dihydropteroate synthase and a thymidylate synthase. The former is especially noteworthy in that no Archaeal homolog of a bacterial folate biosynthetic enzyme has been found to date. Experimental confirmation of the deduced activity of both enzymes is described. Identification of two different proteins was attempted deliberately to help allay concern that predictive success is merely a lucky accident. << Less