Record Information
Version2.0
Creation Date2012-05-31 13:47:33 -0600
Update Date2015-06-03 15:53:50 -0600
Secondary Accession Numbers
  • ECMDB01201
Identification
Name:Guanosine diphosphate
DescriptionGuanosine 5'-(trihydrogen diphosphate). A guanine nucleotide containing two phosphate groups esterified to the sugar moiety. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g. the G-proteins that are involved in signal transduction.
Structure
Thumb
Synonyms:
  • 5'-GDP
  • GDP
  • Guanosine 5'-(trihydrogen pyrophosphate)
  • Guanosine 5'-(trihydrogen pyrophosphoric acid)
  • Guanosine 5'-diphosphate
  • Guanosine 5'-diphosphoric acid
  • Guanosine 5'-pyrophosphate
  • Guanosine 5'-pyrophosphoric acid
  • Guanosine diphosphoric acid
  • Guanosine mono(trihydrogen diphosphate)
  • Guanosine mono(trihydrogen diphosphoric acid)
  • Guanosine pyrophosphate
  • Guanosine pyrophosphoric acid
  • Guanosine-5'-diphosphate
  • Guanosine-5'-diphosphoric acid
  • Guanosine-diphosphate
  • Guanosine-diphosphoric acid
  • PpG
Chemical Formula:C10H15N5O11P2
Weight:Average: 443.2005
Monoisotopic: 443.024329371
InChI Key:QGWNDRXFNXRZMB-UUOKFMHZSA-N
InChI:InChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
CAS number:146-91-8
IUPAC Name:[({[(2R,3S,4R,5R)-5-(2-amino-6-oxo-6,9-dihydro-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]phosphonic acid
Traditional IUPAC Name:{[(2R,3S,4R,5R)-5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy(hydroxy)phosphoryl}oxyphosphonic acid
SMILES:NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1
Chemical Taxonomy
Description belongs to the class of organic compounds known as purine ribonucleoside diphosphates. These are purine ribobucleotides with diphosphate group linked to the ribose moiety.
KingdomOrganic compounds
Super ClassNucleosides, nucleotides, and analogues
ClassPurine nucleotides
Sub ClassPurine ribonucleotides
Direct ParentPurine ribonucleoside diphosphates
Alternative Parents
Substituents
  • Purine ribonucleoside diphosphate
  • Purine ribonucleoside monophosphate
  • Pentose phosphate
  • Pentose-5-phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • 6-oxopurine
  • Hypoxanthine
  • Monosaccharide phosphate
  • Organic pyrophosphate
  • Pentose monosaccharide
  • Imidazopyrimidine
  • Purine
  • Aminopyrimidine
  • Monoalkyl phosphate
  • Pyrimidone
  • Monosaccharide
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Alkyl phosphate
  • Phosphoric acid ester
  • Pyrimidine
  • Vinylogous amide
  • Tetrahydrofuran
  • Azole
  • Imidazole
  • Heteroaromatic compound
  • Secondary alcohol
  • 1,2-diol
  • Organoheterocyclic compound
  • Azacycle
  • Oxacycle
  • Organooxygen compound
  • Organic nitrogen compound
  • Hydrocarbon derivative
  • Organic oxide
  • Organopnictogen compound
  • Alcohol
  • Amine
  • Organic oxygen compound
  • Primary amine
  • Organonitrogen compound
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State:Solid
Charge:-3
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility4.44 g/LALOGPS
logP-1.5ALOGPS
logP-3.7ChemAxon
logS-2ALOGPS
pKa (Strongest Acidic)1.71ChemAxon
pKa (Strongest Basic)2.55ChemAxon
Physiological Charge-3ChemAxon
Hydrogen Acceptor Count13ChemAxon
Hydrogen Donor Count7ChemAxon
Polar Surface Area248.28 ŲChemAxon
Rotatable Bond Count6ChemAxon
Refractivity85.93 m³·mol⁻¹ChemAxon
Polarizability34.74 ųChemAxon
Number of Rings3ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
Guanosine diphosphate + Reduced Thioredoxin > dGDP + Water + Oxidized Thioredoxin
Guanosine diphosphate + glutaredoxin > dGDP + glutaredoxin + Water
Adenosine triphosphate + Guanosine diphosphate <> ADP + Guanosine triphosphate
Adenosine triphosphate + Guanosine triphosphate + Water + Sulfate > Adenosine phosphosulfate + Guanosine diphosphate + Phosphate + Pyrophosphate
Adenosine triphosphate + Guanosine diphosphate > Adenosine monophosphate + Hydrogen ion + Guanosine 3',5'-bis(diphosphate)
P1,P4-Bis(5'-guanosyl) tetraphosphate + Water >2 Guanosine diphosphate +2 Hydrogen ion
Adenosine monophosphate + Guanosine triphosphate <> ADP + Guanosine diphosphate
Guanosine triphosphate + Water > Guanosine diphosphate + Hydrogen ion + Phosphate
Guanosine diphosphate + Hydrogen ion + D-Mannose 1-phosphate > Guanosine diphosphate mannose + Phosphate
Guanosine diphosphate mannose + Water > Guanosine diphosphate + Hydrogen ion + D-Mannose
Cytidine + Guanosine triphosphate > Cytidine monophosphate + Guanosine diphosphate + Hydrogen ion
Guanosine triphosphate + Uridine > Guanosine diphosphate + Hydrogen ion + Uridine 5'-monophosphate
Adenosine triphosphate + Guanosine monophosphate <> ADP + Guanosine diphosphate
Water + Guanosine 3',5'-bis(diphosphate) <> Guanosine diphosphate + Pyrophosphate
L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate
Guanosine triphosphate + Pyruvic acid <> Guanosine diphosphate + Phosphoenolpyruvic acid
RNA + Phosphate <> RNA + Guanosine diphosphate
Guanosine triphosphate + Cytidine <> Guanosine diphosphate + Cytidine monophosphate
Guanosine triphosphate + Uridine <> Guanosine diphosphate + Uridine 5'-monophosphate
Guanosine triphosphate + Inosinic acid + L-Aspartic acid <> Guanosine diphosphate + Phosphate + Adenylsuccinic acid
dGDP + Thioredoxin disulfide + Water <> Guanosine diphosphate + Thioredoxin
Adenosyl cobinamide + Guanosine triphosphate <> Adenosyl cobinamide phosphate + Guanosine diphosphate
L-Aspartic acid + Inosinic acid + Guanosine triphosphate > Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphate
GDP-&alpha;-D-glucose + Water > Hydrogen ion + b-D-Glucose + Guanosine diphosphate
Guanosine diphosphate + Adenosine triphosphate > Guanosine triphosphate + ADP
Adenosine triphosphate + Guanosine diphosphate > Adenosine monophosphate + Guanosine 3',5'-bis(diphosphate)
Guanosine diphosphate + Water > Hydrogen ion + Guanosine monophosphate + Phosphate
Guanosine 3',5'-bis(diphosphate) + Water > Hydrogen ion + Pyrophosphate + Guanosine diphosphate
Guanosine diphosphate mannose + Water > Guanosine diphosphate + D-Mannose
Adenosine triphosphate + Guanosine monophosphate > ADP + Guanosine diphosphate
Guanosine triphosphate + Water > Guanosine diphosphate + Inorganic phosphate
Guanosine triphosphate + Inosinic acid + L-Aspartic acid > Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMP
Guanosine 3',5'-bis(diphosphate) + Water > Guanosine diphosphate + Pyrophosphate
Adenosine triphosphate + Guanosine triphosphate + Adenosyl cobinamide <> Adenosyl cobinamide phosphate + ADP + Guanosine diphosphate
Succinyl-CoA + Phosphate + Guanosine diphosphate + Succinyl-CoA <> Succinic acid + Coenzyme A + Guanosine triphosphate
Guanosine triphosphate + Inosinic acid + L-Aspartic acid + L-Aspartic acid > Guanosine diphosphate + Phosphate + N(6)-(1,2-dicarboxyethyl)AMP
Inosinic acid + L-Aspartic acid + Guanosine triphosphate + L-Aspartic acid > Guanosine diphosphate + Phosphate +2 Hydrogen ion + N(6)-(1,2-dicarboxyethyl)AMP + Adenylsuccinic acid
Guanosine monophosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine diphosphate + ADP
Guanosine diphosphate + Adenosine triphosphate > Adenosine diphosphate + Guanosine triphosphate + ADP
Guanosine diphosphate + reduced thioredoxin > oxidized thioredoxin + Water + dGDP + dGDP
Guanosine diphosphate + a reduced NrdH glutaredoxin-like protein > Water + an oxidized NrdH glutaredoxin-like protein + dGDP + dGDP
L-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + Phosphate
More...

SMPDB Pathways:
Aspartate metabolismPW000787 ThumbThumb?image type=greyscaleThumb?image type=simple
purine nucleotides de novo biosynthesisPW000910 ThumbThumb?image type=greyscaleThumb?image type=simple
purine nucleotides de novo biosynthesis 1435709748PW000960 ThumbThumb?image type=greyscaleThumb?image type=simple
purine nucleotides de novo biosynthesis 2PW002033 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways:
EcoCyc Pathways:
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
30± 2 uMK120.2 g/L NH4Cl, 2.0 g/L (NH4)2SO4, 3.25 g/L KH2PO4, 2.5 g/L K2HPO4, 1.5 g/L NaH2PO4, 0.5 g/L MgSO4; trace substances: 10 mg/L CaCl2, 0.5 mg/L ZnSO4, 0.25 mg/L CuCl2, 0.25 mg/L MnSO4, 0.175 mg/L CoCl2, 0.125 mg/L H3BO3, 2.5 mg/L AlCl3, 0.5 mg/L Na2MoO4, 10Stationary Phase, glucose limitedBioreactor, pH controlled, aerated, dilution rate=0.125 L/h37 oCPMID: 11488613
676± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
23± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
18± 0 uMK12 NCM3722Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateMid-Log PhaseShake flask and filter culture37 oCPMID: 19561621
180± 0 uMBW2511348 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoStationary Phase, glucose limitedBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h37 oCPMID: 17379776
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-004i-5930200000-bdc0893316c12636a495View in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (2 TMS) - 70eV, Positivesplash10-0229-6393250000-a57b7f18975223fa888cView in MoNA
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, PositiveNot AvailableView in JSpectraViewer
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-0udl-0900600000-5c7173a5771dfefadc5eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-0udi-0900000000-d38af29994fa5108c331View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-0udi-0900000000-3072d857dcc8a1b2cbaaView in MoNA
LC-MS/MSLC-MS/MS Spectrum - , negativesplash10-0kdi-5901100000-24a5c807e53370f01d0cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - , positivesplash10-0udi-0900000000-6399eaf97235815c4cb7View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 35V, Positivesplash10-0udi-0900000000-80f8e0b42526cc03fef4View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 30V, Negativesplash10-0pdl-2902100000-027fb059218f84756c35View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 30V, Negativesplash10-0pdl-2902200000-876f01fe6b2be177ac75View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 30V, Negativesplash10-0pdl-3902100000-054557b6d17ed830f7e5View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 40V, Negativesplash10-004i-9600000000-2f85040f9b280383ec8aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - 20V, Negativesplash10-054o-5904800000-e39f64dcf91afa144498View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 10V, Negativesplash10-0006-0001900000-cdce5e7d8986462632b2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - 35V, Negativesplash10-0kdi-5901100000-ba4bded631640c110a56View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0udi-0911300000-fcd49d8a5e9d3dc3f933View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udi-0900000000-ded96f0f499982ac1ab0View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0udi-0900000000-ac93e95f54842f42e273View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0f6x-0900800000-1ed1199fdace4d1b4d80View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0zir-3900000000-b9aeef613c34fe99a48cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9200000000-f630c9237e72a76d3d63View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0udi-0900200000-fa2d42f6050d9ab60119View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0udi-0900000000-ed3d09503a04c850d595View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0udi-0900000000-19a5699334c495daa4e5View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0006-0001900000-7b9b9276c5e39c703f8cView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-004i-9202300000-fa0fbdc8c265ee49a371View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-004i-9100000000-278ab542160fff840256View in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,1H] 2D NMR SpectrumNot AvailableView in JSpectraViewer
2D NMR[1H,13C] 2D NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. Pubmed: 19561621
  • Buchholz, A., Takors, R., Wandrey, C. (2001). "Quantification of intracellular metabolites in Escherichia coli K12 using liquid chromatographic-electrospray ionization tandem mass spectrometric techniques." Anal Biochem 295:129-137. Pubmed: 11488613
  • Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. Pubmed: 8595732
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference:Edlin, Gordon; Donini, P. Synthesis of guanosine 5'-diphosphate, 2'-(or 3'-) diphosphate, and related nucleotides in a variety of physiological conditions. Journal of Biological Chemistry (1971), 246(13), 4371-3.
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID17552
HMDB IDHMDB01201
Pubchem Compound ID8977
Kegg IDC00035
ChemSpider ID8630
WikipediaGDP
BioCyc IDGDP
EcoCyc IDGDP
Ligand ExpoGDP

Enzymes

General function:
Involved in oxidation-reduction process
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox- active cysteines
Gene Name:
nrdA
Uniprot ID:
P00452
Molecular weight:
85774
Reactions
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
General function:
Involved in RNA binding
Specific function:
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction
Gene Name:
pnp
Uniprot ID:
P05055
Molecular weight:
77100
Reactions
RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.
General function:
Involved in bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity
Specific function:
Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP
Gene Name:
apaH
Uniprot ID:
P05637
Molecular weight:
31296
Reactions
P(1),P(4)-bis(5'-adenosyl) tetraphosphate + H(2)O = 2 ADP.
General function:
Involved in acid phosphatase activity
Specific function:
A phosphate monoester + H(2)O = an alcohol + phosphate
Gene Name:
appA
Uniprot ID:
P07102
Molecular weight:
47056
Reactions
A phosphate monoester + H(2)O = an alcohol + phosphate.
Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.
General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Gene Name:
ndk
Uniprot ID:
P0A763
Molecular weight:
15463
Reactions
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
General function:
Involved in adenylosuccinate synthase activity
Specific function:
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Gene Name:
purA
Uniprot ID:
P0A7D4
Molecular weight:
47345
Reactions
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.
General function:
Involved in ATP binding
Specific function:
ATP + uridine = ADP + UMP
Gene Name:
udk
Uniprot ID:
P0A8F4
Molecular weight:
24353
Reactions
ATP + uridine = ADP + UMP.
ATP + cytidine = ADP + CMP.
General function:
Involved in magnesium ion binding
Specific function:
ATP + pyruvate = ADP + phosphoenolpyruvate
Gene Name:
pykF
Uniprot ID:
P0AD61
Molecular weight:
50729
Reactions
ATP + pyruvate = ADP + phosphoenolpyruvate.
General function:
Involved in nucleotide binding
Specific function:
ATP-dependent phosphorylation of adenosylcobinamide and adds GMP to adenosylcobinamide phosphate
Gene Name:
cobU
Uniprot ID:
P0AE76
Molecular weight:
20164
Reactions
ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or GDP.
GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP.
General function:
Involved in hydrolase activity
Specific function:
Catalyzes the hydrolysis of 4-amino-2-methyl-5- hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2- methyl-5-hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate
Gene Name:
nudJ
Uniprot ID:
P0AEI6
Molecular weight:
17433
General function:
Involved in amino acid binding
Specific function:
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp
Gene Name:
relA
Uniprot ID:
P0AG20
Molecular weight:
83875
Reactions
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
General function:
Involved in catalytic activity
Specific function:
In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the synthesis and degradation of ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c- di-GMP induces it
Gene Name:
spoT
Uniprot ID:
P0AG24
Molecular weight:
79342
Reactions
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate.
Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate.
General function:
Involved in electron carrier activity
Specific function:
Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin
Gene Name:
trxC
Uniprot ID:
P0AGG4
Molecular weight:
15555
Reactions
Protein dithiol + NAD(P)(+) = protein disulfide + NAD(P)H.
General function:
Involved in catalytic activity
Specific function:
ATP + sulfate = diphosphate + adenylyl sulfate
Gene Name:
cysD
Uniprot ID:
P21156
Molecular weight:
35188
Reactions
ATP + sulfate = diphosphate + adenylyl sulfate.
General function:
Involved in magnesium ion binding
Specific function:
ATP + pyruvate = ADP + phosphoenolpyruvate
Gene Name:
pykA
Uniprot ID:
P21599
Molecular weight:
51357
Reactions
ATP + pyruvate = ADP + phosphoenolpyruvate.
General function:
Involved in GTPase activity
Specific function:
May be the GTPase, regulating ATP sulfurylase activity
Gene Name:
cysN
Uniprot ID:
P23845
Molecular weight:
52558
Reactions
ATP + sulfate = diphosphate + adenylyl sulfate.
General function:
Involved in nucleotidyltransferase activity
Specific function:
Involved in the biosynthesis of the capsular polysaccharide colanic acid
Gene Name:
manC
Uniprot ID:
P24174
Molecular weight:
53016
Reactions
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
General function:
Involved in catalytic activity
Specific function:
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin
Gene Name:
nrdD
Uniprot ID:
P28903
Molecular weight:
80022
Reactions
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin.
General function:
Involved in hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Specific function:
Could participate in the regulation of cell wall biosynthesis by influencing the concentration of GDP-mannose or GDP-glucose in the cell. May be involved in the degradation of GDP-mannose and GDP-glucose, diverting the GDP to the synthesis of GDP-fucose as required. Might also be involved in the biosynthesis of the slime polysaccharide colanic acid
Gene Name:
nudD
Uniprot ID:
P32056
Molecular weight:
18273
Reactions
GDP-D-mannose + H(2)O = GDP + D-mannose.
General function:
Involved in oxidoreductase activity
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis
Gene Name:
nrdF
Uniprot ID:
P37146
Molecular weight:
36443
Reactions
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
General function:
Involved in GTPase activity
Specific function:
May play a role in 30S ribosomal subunit biogenesis. Unusual circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover. Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96 fold increase in kcat) ribosomes (PubMed:14973029). The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870). This inhibition is not due to competition for binding sites on the 30S or 70S ribosome (PubMed:15828870)
Gene Name:
rsgA
Uniprot ID:
P39286
Molecular weight:
39193
General function:
Involved in oxidation-reduction process
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide
Gene Name:
nrdE
Uniprot ID:
P39452
Molecular weight:
80478
Reactions
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
General function:
Involved in protein binding
Specific function:
Essential for recycling GMP and indirectly, cGMP
Gene Name:
gmk
Uniprot ID:
P60546
Molecular weight:
23593
Reactions
ATP + GMP = ADP + GDP.
General function:
Involved in ATP binding
Specific function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth
Gene Name:
adk
Uniprot ID:
P69441
Molecular weight:
23586
Reactions
ATP + AMP = 2 ADP.
General function:
Involved in oxidoreductase activity
Specific function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis
Gene Name:
nrdB
Uniprot ID:
P69924
Molecular weight:
43517
Reactions
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
General function:
Involved in electron carrier activity
Specific function:
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (Probable)
Gene Name:
grxD
Uniprot ID:
P0AC69
Molecular weight:
12879
General function:
Involved in electron carrier activity
Specific function:
The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase
Gene Name:
grxC
Uniprot ID:
P0AC62
Molecular weight:
9137
General function:
Involved in protein binding
Specific function:
Involved in reducing some disulfides in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase
Gene Name:
grxB
Uniprot ID:
P0AC59
Molecular weight:
24350
General function:
Involved in electron carrier activity
Specific function:
The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase
Gene Name:
grxA
Uniprot ID:
P68688
Molecular weight:
9685
General function:
Involved in electron carrier activity
Specific function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions
Gene Name:
trxA
Uniprot ID:
P0AA25
Molecular weight:
11807

Transporters

General function:
Involved in nucleoside diphosphate kinase activity
Specific function:
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Gene Name:
ndk
Uniprot ID:
P0A763
Molecular weight:
15463
Reactions
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
General function:
Involved in transporter activity
Specific function:
Non-specific porin
Gene Name:
ompN
Uniprot ID:
P77747
Molecular weight:
41220
General function:
Involved in transporter activity
Specific function:
Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
Gene Name:
phoE
Uniprot ID:
P02932
Molecular weight:
38922
General function:
Involved in transporter activity
Specific function:
OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
Gene Name:
ompF
Uniprot ID:
P02931
Molecular weight:
39333
General function:
Involved in transporter activity
Specific function:
Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
Gene Name:
ompC
Uniprot ID:
P06996
Molecular weight:
40368