Record Information
Version2.0
Creation Date2012-05-31 09:57:04 -0600
Update Date2015-09-13 12:56:06 -0600
Secondary Accession Numbers
  • ECMDB00089
Identification
Name:Cytidine
Description:Cytidine is a nucleoside that is composed of the base cytosine linked to the five-carbon sugar D-ribose. Cytidine is a pyrimidine that besides being incorporated into nucleic acids, can serve as substrate for the salvage pathway of pyrimidine nucleotide synthesis; as precursor of the cytidine triphosphate (CTP) needed in the phosphatidylcholine (PC) and phosphatidylethanolamine (PE) biosynthetic pathway. These variations probably reflect the species differences in cytidine deaminase. The biosynthesis of PC via the Kennedy pathway requires phosphocholine and cytidine triphosphate (CTP), a cytidine nucleotide, which is involved in the rate-limiting step. (PMID: 16769123, 15780864, 16720547)
Structure
Thumb
Synonyms:
  • 1-(b-D-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(b-delta-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(b-δ-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(beta-D-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(beta-delta-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(β-D-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-(β-δ-Ribofuranosyl)-2-oxo-4-amino-1,2-dihydro-1,3-diazine
  • 1-b-D-Ribofuranosyl-cytosine
  • 1-b-D-Ribofuranosylcytosine
  • 1-b-D-ribosyl-Cytosine
  • 1-b-delta-Ribofuranosyl-cytosine
  • 1-b-delta-Ribofuranosylcytosine
  • 1-b-delta-Ribosyl-cytosine
  • 1-b-δ-Ribofuranosyl-cytosine
  • 1-b-δ-Ribofuranosylcytosine
  • 1-b-δ-Ribosyl-cytosine
  • 1-beta-D-Ribofuranosyl-Cytosine
  • 1-beta-D-Ribofuranosylcytosine
  • 1-beta-D-Ribosyl-Cytosine
  • 1-beta-delta-Ribofuranosyl-Cytosine
  • 1-beta-delta-Ribofuranosylcytosine
  • 1-beta-delta-Ribosyl-Cytosine
  • 1-β-D-Ribofuranosyl-cytosine
  • 1-β-D-Ribofuranosylcytosine
  • 1-β-D-Ribosyl-cytosine
  • 1-β-δ-Ribofuranosyl-cytosine
  • 1-β-δ-Ribofuranosylcytosine
  • 1-β-δ-Ribosyl-cytosine
  • 1b-D-Ribofuranosylcytosine
  • 1b-delta-Ribofuranosylcytosine
  • 1b-Ribofuranosylcytosine
  • 1b-δ-Ribofuranosylcytosine
  • 1beta-D-Ribofuranosylcytosine
  • 1beta-delta-Ribofuranosylcytosine
  • 1beta-Ribofuranosylcytosine
  • 1β-D-Ribofuranosylcytosine
  • 1β-Ribofuranosylcytosine
  • 1β-δ-Ribofuranosylcytosine
  • 4-Amino-1-b-D-ribofuranosyl-2(1H)-pyrimidinone
  • 4-amino-1-b-delta-Ribofuranosyl-2(1H)-pyrimidinone
  • 4-amino-1-b-δ-Ribofuranosyl-2(1H)-pyrimidinone
  • 4-Amino-1-beta-delta-ribofuranosyl-2(1H)-pyrimidinone
  • 4-amino-1-β-δ-Ribofuranosyl-2(1H)-pyrimidinone
  • Cytidine
  • Cytosine riboside
  • Cytosine-1b-D-Ribofuranoside
  • Cytosine-1b-delta-Ribofuranoside
  • Cytosine-1b-δ-ribofuranoside
  • Cytosine-1beta-D-Ribofuranoside
  • Cytosine-1beta-delta-Ribofuranoside
  • Cytosine-1β-D-ribofuranoside
  • Cytosine-1β-δ-ribofuranoside
Chemical Formula:C9H13N3O5
Weight:Average: 243.2166
Monoisotopic: 243.085520541
InChI Key:UHDGCWIWMRVCDJ-XVFCMESISA-N
InChI:InChI=1S/C9H13N3O5/c10-5-1-2-12(9(16)11-5)8-7(15)6(14)4(3-13)17-8/h1-2,4,6-8,13-15H,3H2,(H2,10,11,16)/t4-,6-,7-,8-/m1/s1
CAS number:65-46-3
IUPAC Name:4-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]-1,2-dihydropyrimidin-2-one
Traditional IUPAC Name:cytidine
SMILES:NC1=NC(=O)N(C=C1)[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O
Chemical Taxonomy
ClassificationNot classified
Physical Properties
State:Solid
Charge:0
Melting point:230.5 °C
Experimental Properties:
PropertyValueSource
LogP:-2.51 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility43.8 mg/mLALOGPS
logP-2.2ALOGPS
logP-2.8ChemAxon
logS-0.74ALOGPS
pKa (Strongest Acidic)12.55ChemAxon
pKa (Strongest Basic)-0.55ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count7ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area128.61 Å2ChemAxon
Rotatable Bond Count2ChemAxon
Refractivity54.54 m3·mol-1ChemAxon
Polarizability22.39 Å3ChemAxon
Number of Rings2ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:
Pyrimidine metabolismPW000942 Pw000942Pw000942 greyscalePw000942 simple
Pyrimidine ribonucleosides degradtionPW002024 Pw002024Pw002024 greyscalePw002024 simple
pyrimidine ribonucleosides degradationPW002104 Pw002104Pw002104 greyscalePw002104 simple
KEGG Pathways:
EcoCyc Pathways:
  • pyrimidine ribonucleosides degradation I PWY0-1295
  • salvage pathways of pyrimidine ribonucleotides PWY0-163
Concentrations
ConcentrationStrainMediaGrowth StatusGrowth SystemTemperatureDetails
3± 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
Find out more about how we convert literature concentrations.
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-MS (5 TMS)splash10-0zfr-2951000000-7baf0e1ea8b1a34362e2View in MoNA
GC-MSGC-MS Spectrum - GC-MS (4 TMS)splash10-0g4j-2980000000-9337623aef7fec22dd97View in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-05dl-9420000000-f2b3f5707444409e125dView in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-0zfr-2951000000-7baf0e1ea8b1a34362e2View in MoNA
GC-MSGC-MS Spectrum - GC-MSsplash10-0g4j-2980000000-9337623aef7fec22dd97View in MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-0083-6964300000-64e7e138ddd30a0aec2cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-03di-0900000000-177050786fcbfaf2d270View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-03di-0900000000-1251248af66dca3401e2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-03di-6900000000-c6b010a1d3e65a0942eeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-0590100000-94eb2baae24aa405b1baView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-9000000000-8155621584c25975ffa1View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-03di-0900000000-5065bc83a32bee37d07cView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-0590200000-4d5dc5376c40d083efbeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-001i-0900000000-6ea86f62a48910b456a0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-03di-0900000000-5c93b66b8899a4d3ce06View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Positivesplash10-0006-0090000000-f0e6ac0bacdbef1206b0View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-000f-0090010000-1cf915fa4dfb86b5861bView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0900000000-6bb7990f165932decea7View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0006-0090000000-0b7dc368d61ee31afb78View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-000l-0090020000-fa04fb11f98259c403b6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0006-0190172001-0671df3c315b8af9e13fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0a4i-0900000000-8aa3fec051a7d9807888View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-0006-0090000000-0563823e8f3a9def519aView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , Negativesplash10-004i-0028900000-f4b6c319a7e9fb17df2eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Positivesplash10-01ox-0590000000-d5d20f84ab30e96c30f6View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) 30V, Positivesplash10-03di-0930000000-c4d3377790616b8b7869View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QTOF (UPLC Q-Tof Premier, Waters) , Negativesplash10-0a4i-1930000000-faec28788ea577988b82View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-0910000000-9575881412c4c94a7eaeView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-03di-5900000000-2cb5f7e3dbd7baa35b56View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-03dj-9600000000-7d281b2b2d57c8786e11View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-01ox-0960000000-db9207082a1fabf42daeView in MoNA
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Barbour JD, Grant RM: The role of viral fitness in HIV pathogenesis. Curr HIV/AIDS Rep. 2005 Feb;2(1):29-34. Pubmed: 16091246
  • 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
  • Cansev, M. (2006). "Uridine and cytidine in the brain: their transport and utilization." Brain Res Rev 52:389-397. Pubmed: 16769123
  • Eells JT, Spector R: Purine and pyrimidine base and nucleoside concentrations in human cerebrospinal fluid and plasma. Neurochem Res. 1983 Nov;8(11):1451-7. Pubmed: 6656991
  • Huthoff H, Malim MH: Cytidine deamination and resistance to retroviral infection: towards a structural understanding of the APOBEC proteins. Virology. 2005 Apr 10;334(2):147-53. Pubmed: 15780864
  • 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
  • Lee SH, Jung BH, Kim SY, Chung BC: A rapid and sensitive method for quantitation of nucleosides in human urine using liquid chromatography/mass spectrometry with direct urine injection. Rapid Commun Mass Spectrom. 2004;18(9):973-7. Pubmed: 15116424
  • Mahieux R, Suspene R, Delebecque F, Henry M, Schwartz O, Wain-Hobson S, Vartanian JP: Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases. J Gen Virol. 2005 Sep;86(Pt 9):2489-94. Pubmed: 16099907
  • Min IM, Selsing E: Antibody class switch recombination: roles for switch sequences and mismatch repair proteins. Adv Immunol. 2005;87:297-328. Pubmed: 16102577
  • Navaratnam N, Sarwar R: An overview of cytidine deaminases. Int J Hematol. 2006 Apr;83(3):195-200. Pubmed: 16720547
  • Schrofelbauer B, Yu Q, Zeitlin SG, Landau NR: Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J Virol. 2005 Sep;79(17):10978-87. Pubmed: 16103149
  • Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
  • 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
  • Zhong SQ, Sun LJ, Yan YZ, Sun YQ, Zhong YY: Effect of Xuesaitong soft capsule on hemorrheology and in auxiliarily treating patients with acute cerebral infarction. Chin J Integr Med. 2005 Jun;11(2):128-31. Pubmed: 16150200
Synthesis Reference:Qu, Guirong; Yang, Xining; Shen, Yanhong; Dong, Chunhong; Guo, Haiming; Wang, Xiuqiang; Wang, Dongchao. Synthesis of cytidine. Faming Zhuanli Shenqing Gongkai Shuomingshu (2007), 11pp.
Material Safety Data Sheet (MSDS)Download (PDF)
External Links:
ResourceLink
CHEBI ID17562
HMDB IDHMDB00089
Pubchem Compound ID6175
Kegg IDC00475
ChemSpider ID5940
WikipediaCytidine
BioCyc IDCYTIDINE
EcoCyc IDCYTIDINE
Ligand ExpoCTN

Enzymes

General function:
Involved in hydrolase activity
Specific function:
Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell
Gene Name:
ushA
Uniprot ID:
P07024
Molecular weight:
60824
Reactions
UDP-sugar + H(2)O = UMP + alpha-D-aldose 1-phosphate.
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
General function:
Involved in hydrolase activity
Specific function:
This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2',3'- cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to the corresponding nucleoside and phosphate
Gene Name:
cpdB
Uniprot ID:
P08331
Molecular weight:
70832
Reactions
Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 3'-phosphate.
A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
General function:
Involved in hydrolase activity
Specific function:
Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'- monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain- length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase
Gene Name:
surE
Uniprot ID:
P0A840
Molecular weight:
26900
Reactions
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
A 3'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
(Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
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 catalytic activity
Specific function:
Nucleotidase that shows high phosphatase activity toward three nucleoside 5'-monophosphates, UMP, dUMP, and dTMP, and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6- phosphogluconate. Is strictly specific to substrates with 5'- phosphates and shows no activity against nucleoside 2'- or 3'- monophosphates. Might be involved in the pyrimidine nucleotide substrate cycles
Gene Name:
yjjG
Uniprot ID:
P0A8Y1
Molecular weight:
25300
Reactions
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
General function:
Involved in zinc ion binding
Specific function:
This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis
Gene Name:
cdd
Uniprot ID:
P0ABF6
Molecular weight:
31539
Reactions
Cytidine + H(2)O = uridine + NH(3).
General function:
Involved in acid phosphatase activity
Specific function:
Dephosphorylates several organic phosphomonoesters and catalyzes the transfer of low-energy phosphate groups from phosphomonoesters to hydroxyl groups of various organic compounds. Preferentially acts on aryl phosphoesters. Might function as a broad-spectrum dephosphorylating enzyme able to scavenge both 3'- and 5'-nucleotides and also additional organic phosphomonoesters
Gene Name:
aphA
Uniprot ID:
P0AE22
Molecular weight:
26103
Reactions
A phosphate monoester + H(2)O = an alcohol + phosphate.
General function:
Involved in hydrolase activity, hydrolyzing N-glycosyl compounds
Specific function:
Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity with decreasing activity in the order uridine, xanthosine, inosine, adenosine, cytidine, guanosine
Gene Name:
rihC
Uniprot ID:
P22564
Molecular weight:
32560
General function:
Involved in hydrolase activity, hydrolyzing N-glycosyl compounds
Specific function:
Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. Has a low but significant activity for the purine nucleoside xanthosine
Gene Name:
rihB
Uniprot ID:
P33022
Molecular weight:
33748
Reactions
A pyrimidine nucleoside + H(2)O = D-ribose + a pyrimidine base.
General function:
Involved in catalytic activity
Specific function:
Nucleotidase that shows strict specificity toward deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. Might be involved in the regulation of all dNTP pools in E.coli
Gene Name:
yfbR
Uniprot ID:
P76491
Molecular weight:
22708
Reactions
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
General function:
Involved in hydrolase activity, hydrolyzing N-glycosyl compounds
Specific function:
Hydrolyzes with equal efficiency cytidine or uridine to ribose and cytosine or uracil, respectively
Gene Name:
rihA
Uniprot ID:
P41409
Molecular weight:
33823

Transporters

General function:
Involved in nucleoside transmembrane transporter activity
Specific function:
Nucleoside transport
Gene Name:
xapB
Uniprot ID:
P45562
Molecular weight:
46139
General function:
Involved in nucleoside:sodium symporter activity
Specific function:
Transports nucleosides with a high affinity except guanosine and deoxyguanosine. Driven by a proton motive force
Gene Name:
nupC
Uniprot ID:
P0AFF2
Molecular weight:
43475
General function:
Involved in nucleoside transmembrane transporter activity
Specific function:
Transports nucleosides with a high affinity. Driven by a proton motive force
Gene Name:
nupG
Uniprot ID:
P0AFF4
Molecular weight:
46389
General function:
Involved in nucleoside:sodium symporter activity
Specific function:
Nucleoside transporter
Gene Name:
nupX
Uniprot ID:
P33021
Molecular weight:
43409
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