Enzymes
| UniProtKB help_outline | 18,312 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
[protein-PII]-uridylyl-L-tyrosine
Identifier
RHEA-COMP:12148
Reactive part
help_outline
- Name help_outline uridylyl-L-tyrosine residue Identifier CHEBI:90602 Charge -1 Formula C18H19N3O10P SMILEShelp_outline C1=CC(NC(N1[C@@H]2O[C@H](COP(OC3=CC=C(C=C3)C[C@H](N*)C(=O)*)(=O)[O-])[C@H]([C@H]2O)O)=O)=O 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 H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,337 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[protein-PII]-L-tyrosine
Identifier
RHEA-COMP:12147
Reactive part
help_outline
- Name help_outline L-tyrosine residue Identifier CHEBI:46858 Charge 0 Formula C9H9NO2 SMILEShelp_outline O=C(*)[C@@H](N*)CC=1C=CC(=CC1)O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline UMP Identifier CHEBI:57865 (Beilstein: 3570858) help_outline Charge -2 Formula C9H11N2O9P InChIKeyhelp_outline DJJCXFVJDGTHFX-XVFCMESISA-L SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])([O-])=O)O[C@H]([C@@H]1O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 54 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:48600 | RHEA:48601 | RHEA:48602 | RHEA:48603 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| EcoCyc help_outline |
Publications
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Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein.
Araujo L.M., Huergo L.F., Invitti A.L., Gimenes C.I., Bonatto A.C., Monteiro R.A., Souza E.M., Pedrosa F.O., Chubatsu L.S.
Azospirillum brasilense is a diazotroph found in association with important agricultural crops. In this organism, the regulation of nitrogen fixation by ammonium ions involves several proteins including the uridylyltransferase/uridylyl-removing enzyme, GlnD, which reversibly uridylylates the two P ... >> More
Azospirillum brasilense is a diazotroph found in association with important agricultural crops. In this organism, the regulation of nitrogen fixation by ammonium ions involves several proteins including the uridylyltransferase/uridylyl-removing enzyme, GlnD, which reversibly uridylylates the two PII proteins, GlnB and GlnZ, in response to the concentration of ammonium ions. In the present study, the uridylylation/deuridylylation cycle of A. brasilense GlnB and GlnZ proteins by GlnD was reconstituted in vitro using the purified proteins. The uridylylation assay was analyzed using non-denaturing polyacrylamide gel electrophoresis and fluorescent protein detection. Our results show that the purified A. brasilense GlnB and GlnZ proteins were uridylylated by the purified A. brasilense GlnD protein in a process dependent on ATP and 2-oxoglutarate. The dependence on ATP for uridylylation was similar for both proteins. On the other hand, at micromolar concentration of 2-oxoglutarate (up to 100 microM), GlnB uridylylation was almost twice that of GlnZ, an effect that was not observed at higher concentrations of 2-oxoglutarate (up to 10 mM). Glutamine inhibited uridylylation and stimulated deuridylylation of both GlnB and GlnZ. However, glutamine seemed to inhibit GlnZ uridylylation more efficiently. Our results suggest that the differences in the uridylylation pattern of GlnB and GlnZ might be important for fine-tuning of the signaling pathway of cellular nitrogen status in A. brasilense. << Less
Braz. J. Med. Biol. Res. 41:289-294(2008) [PubMed] [EuropePMC]