Primary Information |
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| BoMiProt ID | Bomi6080 |
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| Protein Name | GMP reductase 2/GMPR 2/Guanosine 5'-monophosphate oxidoreductase 2/Guanosine monophosphate reductase 2 |
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| Organism | Bos taurus |
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| Uniprot ID | Q32L93 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001033208.1 |
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| Aminoacid Length | 348 |
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| Molecular Weight | 38033 |
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| FASTA Sequence |
Download |
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| Gene Name | GMPR2 |
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| Gene ID | 515837 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Guanosine monophosphate (GMP) reductase catalyzes the reductive deamination of GMP to inosine monophosphate (IMP). GMP reductase plays an important role in the conversion of nucleoside and nucleotide derivatives of guanine to adenine nucleotides. |
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| Biochemical Properties | As a member of the purine salvage pathway, it participates in the reutilization of free intracellular bases. The protein forms a tetramer composed of subunits adopting the ubiquitous (alpha/beta)8 barrel fold. Interestingly, the substrate GMP is bound to hGMPR2 through interactions with Met269, Ser270, Arg286, Ser288, and Gly290; this makes the conformation of the adjacent flexible binding region (residues 268-289) fixed, much like a door on a hinge. |
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| PTMs | N6-Acetylation at Lys |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | Cys186 is the potential active site, and that the conformation of the loop (residues 129-133) suggests a preference for the coenzyme NADPH over NADH. |
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| Bibliography | 1.Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y. Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP. J Mol Biol. 2006 Feb 3;355(5):980-8. doi: 10.1016/j.jmb.2005.11.047. Epub 2005 Dec 1. PMID: 16359702. 2.Martinelli LK, Ducati RG, Rosado LA, Breda A, Selbach BP, Santos DS, Basso LA. Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation. Mol Biosyst. 2011 Apr;7(4):1289-305. doi: 10.1039/c0mb00245c. Epub 2011 Feb 7. PMID: 21298178. |
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