Search by BoMiProt ID - Bomi6080


Primary Information

BoMiProt ID Bomi6080
Protein Name GMP reductase 2/GMPR 2/Guanosine 5'-monophosphate oxidoreductase 2/Guanosine monophosphate reductase 2
Organism Bos taurus
Uniprot IdQ32L93
Milk FractionWhey
Ref Sequence Id NP_001033208.1
Aminoacid Length 348
Molecular Weight 38033
Fasta Sequence https://www.uniprot.org/uniprot/Q32L93.fasta
Gene Name GMPR2
Gene Id 515837
Protein Existence Status reviewed

Secondary Information

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.
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.
PTMs N6-Acetylation at Lys
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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. 
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.