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Conserved domains on  [gi|1779108731|ref|WP_155162060|]
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uridine phosphorylase [Sansalvadorimonas verongulae]

Protein Classification

uridine phosphorylase( domain architecture ID 10013750)

uridine phosphorylase (UP), a key enzyme in the pyrimidine salvage pathway, catalyzes the reversible phosphorolysis of uridine or 2'-deoxyuridine to uracil and ribose 1-phosphate or 2'-deoxyribose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 1-251 0e+00

uridine phosphorylase; Provisional


:

Pssm-ID: 183018  Cd Length: 251  Bit Score: 510.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   1 MSDVFHLGLVKADLQGAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA 80
Cdd:PRK11178    1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  81 QLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTF 160
Cdd:PRK11178   81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 161 YPGQERYDTLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAV 240
Cdd:PRK11178  161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                         250
                  ....*....|.
gi 1779108731 241 NIVVDAARILL 251
Cdd:PRK11178  241 KIVVEAARRLL 251
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 1-251 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 510.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   1 MSDVFHLGLVKADLQGAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA 80
Cdd:PRK11178    1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  81 QLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTF 160
Cdd:PRK11178   81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 161 YPGQERYDTLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAV 240
Cdd:PRK11178  161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                         250
                  ....*....|.
gi 1779108731 241 NIVVDAARILL 251
Cdd:PRK11178  241 KIVVEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 5-248 3.58e-116

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 332.10  E-value: 3.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   5 FHLGLVKADLqgAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLGI 84
Cdd:cd17767     1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  85 RTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQ 164
Cdd:cd17767    79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 165 ERYDTlrgYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAVNIVV 244
Cdd:cd17767   159 GRPGP---GLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                  ....
gi 1779108731 245 DAAR 248
Cdd:cd17767   236 EALK 239
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 4-251 9.02e-113

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 323.77  E-value: 9.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   4 VFHLGLVKADLQgaELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLG 83
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  84 IRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPG 163
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 164 QERyDTLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAVNIV 243
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 1779108731 244 VDAARILL 251
Cdd:TIGR01718 238 VEAVKRLL 245
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-252 1.06e-105

Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 442068  Cd Length: 251  Bit Score: 305.94  E-value: 1.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   1 MSDVFHLGLVKADLqgAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA 80
Cdd:COG2820     8 DGSQYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  81 QLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTF 160
Cdd:COG2820    86 ALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 161 YPGQERYDtlrgYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAqlMARTESHAV 240
Cdd:COG2820   166 YAEQGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKD--PEEAVERAI 239

                         250
                  ....*....|..
gi 1779108731 241 NIVVDAARILLN 252
Cdd:COG2820   240 KVALEALKKLIE 251
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 18-251 5.46e-35

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 125.15  E-value: 5.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  18 ELAIVPGDPERVKKIAE-LMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRVGTTG 94
Cdd:pfam01048   1 KIAIIGGSPEELALLAElLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  95 AIQEDIDVGSVIVTTGSVRLDGASQ-------HFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQERY 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 168 dtlrgyvirkyqgsMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAgVIVNRTQQEIPDAQLMARTESHAVNIVVDAA 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIR-VVSDLAAGGADGELTHEEVEEFAERAAERAA 225


                  ....
gi 1779108731 248 RILL 251
Cdd:pfam01048 226 ALLL 229
 
Name Accession Description Interval E-value
PRK11178 PRK11178
uridine phosphorylase; Provisional
 1-251 0e+00

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 510.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   1 MSDVFHLGLVKADLQGAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA 80
Cdd:PRK11178    1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  81 QLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTF 160
Cdd:PRK11178   81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 161 YPGQERYDTLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAV 240
Cdd:PRK11178  161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                         250
                  ....*....|.
gi 1779108731 241 NIVVDAARILL 251
Cdd:PRK11178  241 KIVVEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 5-248 3.58e-116

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 332.10  E-value: 3.58e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   5 FHLGLVKADLqgAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLGI 84
Cdd:cd17767     1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  85 RTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQ 164
Cdd:cd17767    79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 165 ERYDTlrgYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAVNIVV 244
Cdd:cd17767   159 GRPGP---GLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                  ....
gi 1779108731 245 DAAR 248
Cdd:cd17767   236 EALK 239
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 4-251 9.02e-113

uridine phosphorylase; This model represents a family of bacterial and archaeal uridine phosphorylases unrelated to the mammalian enzymes of the same name. The E. coli, Salmonella and Klebsiella genes have been characterized. Sequences from Clostridium, Streptomyces, Treponema, Halobacterium and Pyrobaculum were included above trusted on the basis of sequence homology and a PAM-based neighbor-joining tree. A clade including second sequences from Halobacterium and Vibrio was somewhat more distantly related and may represent a slightly different substrate specificity - these were placed below the noise cutoff. More distantly related is a clade of archaeal sequences which as related to the DeoD family of inosine phosphorylases (TIGR00107) as they are to these uridine phosphorylases. This clade includes a characterized protein from Sulfolobus solfataricus which has been mis-named as a methylthioadenosine phosphorylase, but which acts on inosine and guanosine - it is unclear whether uridine has been evaluated as a substrate. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130779  Cd Length: 245  Bit Score: 323.77  E-value: 9.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   4 VFHLGLVKADLQgaELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLG 83
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  84 IRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPG 163
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 164 QERyDTLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAQLMARTESHAVNIV 243
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 1779108731 244 VDAARILL 251
Cdd:TIGR01718 238 VEAVKRLL 245
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-252 1.06e-105

Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 442068  Cd Length: 251  Bit Score: 305.94  E-value: 1.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   1 MSDVFHLGLVKADLqgAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA 80
Cdd:COG2820     8 DGSQYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  81 QLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTF 160
Cdd:COG2820    86 ALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 161 YPGQERYDtlrgYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEIPDAqlMARTESHAV 240
Cdd:COG2820   166 YAEQGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKD--PEEAVERAI 239

                         250
                  ....*....|..
gi 1779108731 241 NIVVDAARILLN 252
Cdd:COG2820   240 KVALEALKKLIE 251
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 19-246 9.92e-59

nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of this family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350156  Cd Length: 216  Bit Score: 185.57  E-value: 9.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  19 LAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRVGTTGAIQE 98
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  99 DIDVGSVIVTTGSVRLDGASQHF-APLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQerydtlrgyvirk 177
Cdd:cd09005    81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRET------------- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 178 yQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGVIVNRTQQEI-PDAQLMARTESHAVNIVVDA 246
Cdd:cd09005   148 -REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIgFVDEFLSEAEKKAIEIALDA 216
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 18-253 5.76e-45

5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. Sulfolobus solfataricus MTAPI will utilize inosine, guanosine, and adenosine as substrates, in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAPII belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-I family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350164  Cd Length: 220  Bit Score: 150.45  E-value: 5.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  18 ELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRVGTTGAIQ 97
Cdd:cd17764     1 ERVIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  98 EDIDVGSVIVTTGSVRLDGA--SQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQERYdtlrgyvi 175
Cdd:cd17764    81 PELRVGDIVVATGASYYPGGglGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEF-------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 176 rkyqgsMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAgVIVN---RTQQEIPDAQLMARTeshavniVVDAARILLN 252
Cdd:cd17764   153 ------AERWSSLGFIAVEMECATLFTLGWLRGVKAGAVL-VVSDnlvKGGKLMLTKEELEEK-------VMKAAKAVLE 218


                  .
gi 1779108731 253 S 253
Cdd:cd17764   219 A 219
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 17-236 1.53e-43

purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine nucleosides. Thermus thermophiles PNP catalyzes the phosphorolysis of guanosine but not adenosine. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350165  Cd Length: 234  Bit Score: 147.07  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  17 AELAIVPGDPERVKKIAE-LMDRAEHLCSHRE---YTiwRAYIGDnAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRVGT 92
Cdd:cd17765    13 AEAVLLPGDPGRATYIAEtFFDGPRLYNDHRGllgYT--GTYKGK-PVSVQTTGMGCPSAAIVVEELAQLGVKRLIRVGT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  93 TGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLE-YPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQErydtlr 171
Cdd:cd17765    90 CGGLSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPTP------ 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1779108731 172 gyvirkyqGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAGV--IVNRTQQEIPDAQLMARTE 236
Cdd:cd17765   164 --------DGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdLIGDPERRIDDEELRAGVD 222
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 6-214 1.08e-35

Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440575  Cd Length: 236  Bit Score: 126.77  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   6 HLGLVKADLqgAELAIVPGDPERVKKIAE-LMDRAEHLCSHRE---YTiwrAYIGDNAVIVCSTGIGGPSTSIAVEELAQ 81
Cdd:COG0813     5 HIGAKKGDI--AETVLLPGDPLRAKYIAEtFLEDAVLVNEVRGmlgYT---GTYKGKRVSVMGSGMGIPSISIYAYELIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  82 -LGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDG-ASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDT 159
Cdd:COG0813    80 eYGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNvNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1779108731 160 FY-PGQERYDTlrgyvirkyqgsmneWQNLGVLNYEMESATLLTMCAALGLRAGCV 214
Cdd:COG0813   160 FYrEDPDLLEK---------------LAKYGVLAVEMEAAALYTLAAKYGKRALAI 200
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 18-251 5.46e-35

Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase (PNP) Uridine phosphorylase (UdRPase) 5'-methylthioadenosine phosphorylase (MTA phosphorylase)


Pssm-ID: 426013  Cd Length: 233  Bit Score: 125.15  E-value: 5.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  18 ELAIVPGDPERVKKIAE-LMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEE--LAQLGIRTFLRVGTTG 94
Cdd:pfam01048   1 KIAIIGGSPEELALLAElLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  95 AIQEDIDVGSVIVTTGSVRLDGASQ-------HFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYPGQERY 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 168 dtlrgyvirkyqgsMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVAgVIVNRTQQEIPDAQLMARTESHAVNIVVDAA 247
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIR-VVSDLAAGGADGELTHEEVEEFAERAAERAA 225


                  ....
gi 1779108731 248 RILL 251
Cdd:pfam01048 226 ALLL 229
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 4-225 5.33e-34

uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350155  Cd Length: 282  Bit Score: 123.74  E-value: 5.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   4 VFHLGLVKADLqgAELAIVPGDPERVKKIAELMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEEL---- 79
Cdd:cd00436    10 IYHLHLKPEDL--ADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  80 ----------AQLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDG--------ASQHFAPLEYPAVADFECANAM--- 138
Cdd:cd00436    88 nidfktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNllnfydhpNTDEEAELENAFIAHTSWFKGKprp 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 139 --VMASRD-----RGVTYRTGITASSDTFYPGQERYdtLRG-----YVIRKYQGSmnEWQNLGVLNYEMESATLLTMCAA 206
Cdd:cd00436   168 yvVKASPElldalTGVGYVVGITATAPGFYGPQGRQ--LRLpladpDLLDKLSSF--SYGGLRITNFEMETSAIYGLSRL 243

                         250
                  ....*....|....*....
gi 1779108731 207 LGLRAGCVAGVIVNRTQQE 225
Cdd:cd00436   244 LGHRALSICAIIANRATGE 262
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 17-217 2.07e-29

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP; Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350157  Cd Length: 228  Bit Score: 110.18  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  17 AELAIVPGDPERVKKIAE-LMDRAEHLCSHRE---YTIWraYIGdNAVIVCSTGIGGPSTSIAVEELAQL-GIRTFLRVG 91
Cdd:cd09006    10 AKTVLMPGDPLRAKYIAEtFLEDAKLVNSVRNmlgYTGT--YKG-KRVSVMGSGMGMPSIGIYAYELFKFyGVKNIIRIG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  92 TTGAIQEDIDVGSVIVTTGSVRLDG-ASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFY-PGQERYDT 169
Cdd:cd09006    87 TCGAYQPDLKLRDVVLAMGASTDSNyNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYdDDPELWKK 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1779108731 170 lrgyvirkyqgsmneWQNLGVLNYEMESATLLTMCAALGLRAGCVAGV 217
Cdd:cd09006   167 ---------------LKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
6-214 1.91e-27

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 105.32  E-value: 1.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   6 HLGLVKADLqgAELAIVPGDPERVKKIAE-LMDRAEHLCSHRE---YTiwRAYIGdNAVIVCSTGIGGPSTSIAVEELAQ 81
Cdd:PRK05819    4 HINAKKGDI--ADTVLMPGDPLRAKYIAEtFLEDVVCVNEVRGmlgFT--GTYKG-KRVSVMGTGMGIPSISIYANELIT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  82 -LGIRTFLRVGTTGAIQEDIDVGSVIVTTGS------VRLDgasqhFAPLEYPAVADFECANAMVMASRDRGVTYRTGIT 154
Cdd:PRK05819   79 dYGVKKLIRVGSCGALQEDVKVRDVVIAMGAstdsnvNRIR-----FKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNV 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1779108731 155 ASSDTFYpgQERYDtlrgyvirkyqgsMNE-WQNLGVLNYEMESATLLTMCAALGLRAGCV 214
Cdd:PRK05819  154 FSADLFY--NPDPE-------------MFDvLEKYGVLGVEMEAAALYGLAAKYGVKALTI 199
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
17-211 3.65e-23

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 94.01  E-value: 3.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  17 AELAIVPGDPERVKKIAE-LMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRVGTTG 94
Cdd:PRK13374   14 AETVLMPGDPLRAKYIAEtYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELiATFGVKNIIRVGSCG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  95 AIQEDIDVGSVIVTTG-SVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFY-PGQERYDtlrg 172
Cdd:PRK13374   94 ATQDDVKLMDVIIAQGaSTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYdPDEDAIE---- 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1779108731 173 yvirkyqgsmnEWQNLGVLNYEMESATLLTMCAALGLRA 211
Cdd:PRK13374  170 -----------AMERFGILGVDMEVAGLYGLAAYLGAEA 197
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 18-215 1.99e-22

uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 91.78  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  18 ELAIVPGDPERVKKIAE--LMDRAEHLCSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRVGTTGA 95
Cdd:cd09007     3 EKCVLVFSGDLLEYLLEeyGAEKIGELSSAGHTPLYRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  96 IQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDRGVTYRTGITASSDTFYpgqerydtlrgyvi 175
Cdd:cd09007    83 LDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEPDPELLDALEEALEKAGIPYVRGKTWTTDAPY-------------- 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1779108731 176 RKYQGSMNEWQNLGVLNYEMESATLLTMCAALGLRAGCVA 215
Cdd:cd09007   149 RETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVELAQLL 188
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 2-221 2.08e-22

uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Human UPP1 has a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350163  Cd Length: 276  Bit Score: 92.98  E-value: 2.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   2 SDV-FHLGLVKADLQGAEL------AIVPGDPERVKKIAELMdrAEHL--------------CSHREYTIWRAyigdNAV 60
Cdd:cd17763     1 VDFlYHLGLDTSSHDLKKMfgdvkfVCMGGSPGRMENFAEYL--AKELgiklpagaalvnlsKTTDRYSMYKV----GPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  61 IVCSTGIGGPSTSIAVEELAQL----GIR--TFLRVGTTGAIqeDIDVGSVIVTTGSVrlDGASQHFAPL-------EYP 127
Cdd:cd17763    75 LSVSHGMGIPSLSILLHELIKLlhyaGCKdvTFIRIGTSGGI--GVEPGTVVITTEAV--DGELEPFYEQvilgkvvKRP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 128 AVADFECANAMV-MASRDRGVTYRTGITASSDTFYPGQERYD-TLRGYVIRKYQGSMNEWQNLGVLNYEMESATLLTMCA 205
Cdd:cd17763   151 AVLDAQLAEELLeCAKELDDFPTVIGKTMCANDFYEGQGRLDgAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCH 230

                         250
                  ....*....|....*.
gi 1779108731 206 ALGLRAGCVAGVIVNR 221
Cdd:cd17763   231 RAGIKAAVVCVTLLNR 246
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 5-231 5.63e-14

uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130780 [Multi-domain]  Cd Length: 287  Bit Score: 69.79  E-value: 5.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731   5 FHLGL------VKADLQGAELAIVPGDPERVKKIAE-LMDRAEHLCSHREYTIWRAyiGDNAVI-----VC--STGIGGP 70
Cdd:TIGR01719  13 YHFGIntsthdFPAVFGDVKFVCMGGTPSRMKAFARyVGAELGLSCGRDYPNISER--GDRFAMykvgpVLcvSHGMGIP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  71 STSIAVEEL------AQLGIRTFLRVGTTGAIqeDIDVGSVIVTTGSV-----------RLDGASQHFAPLEyPAVADFE 133
Cdd:TIGR01719  91 SISIMLHELikllyyARCKNPTFIRIGTSGGI--GVPPGTVVVSSEAVdaclkpeyeqiVLGKRVIRPTQLD-EALVQEL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 134 CanaMVMASRDRGVTYRTGITASSDTFYPGQERYDtlrGYVIRKYQGSMNEW----QNLGVLNYEMESATLLTMCAALGL 209
Cdd:TIGR01719 168 L---LCGAEGLDEFTTVSGNTMCTDDFYEGQGRLD---GAFCEYTEKDKMAYlrklYALGVRNIEMESSMFAAMTSRAGF 241

                         250       260
                  ....*....|....*....|....*
gi 1779108731 210 RAGCVAGVIVNR---TQQEIPDAQL 231
Cdd:TIGR01719 242 KAAVVCVTLLNRlegDQITITRDQL 266
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 24-239 1.76e-13

nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350169  Cd Length: 255  Bit Score: 67.99  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  24 GDPERVKKIAELMDRAEHLC---SHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELAQL--GIRTFLRVGTTGAIQE 98
Cdd:cd17769     7 GDPARARLIAKLLDKEPKVFeltSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  99 DIDVGSVIVTTGSV----RLDGASQHFAPLE----Y----PAVADFECANAMV--MASRDRGVTYRTGITASSDTFYPGQ 164
Cdd:cd17769    87 DVPVGSVVVPSASVavtrNYDDDDFAGPSTSsekpYliskPVPADPELSELLEseLKASLGGEVVVEGLNASADSFYSSQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 165 ERYDT--------LRGYVIRKYqgsmnewqnLGVLNYEMESATLLTMC-----AALGLRAGCVAGVIVNRTQQEIPDAQL 231
Cdd:cd17769   167 GRQDPnfpdhnenLIDKLLKRY---------PGAASLEMETFHLFHLArcsrpAQGKIRAAAAHMVFANRTSNDFISPER 237


                  ....*...
gi 1779108731 232 MARTESHA 239
Cdd:cd17769   238 VHELERWA 245
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 21-214 6.51e-11

Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB [Nucleotide transport and metabolism, Coenzyme transport and metabolism]; Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase MtnN and futalosine hydrolase MqnB is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440538  Cd Length: 231  Bit Score: 60.31  E-value: 6.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  21 IVPGDPErVKKIAELMDRAEHLcSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEEL-AQLGIRTFLRVGTTGAIQED 99
Cdd:COG0775     6 IGAMEEE-VAALLEALEDKKEV-QIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGLDPD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731 100 IDVGSVIVTTGSVRLDGASQHFaPLEYPAV--------ADFECANAMVMASRDRGVTYRTGITASSDTFYPGQERYDTLR 171
Cdd:COG0775    84 LKIGDVVLATEVVQHDVDVTAF-GYPRGQVpgmpalfeADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLR 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1779108731 172 gyviRKYQGSmnewqnLGVlnyEMESATLLTMCAALGLRAGCV 214
Cdd:COG0775   163 ----ERFPGA------LAV---DMEGAAIAQVCYRFGVPFLVI 192
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 66-158 3.32e-08

AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350162  Cd Length: 242  Bit Score: 52.56  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  66 GIGGPSTSIAVEELAQLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDR 145
Cdd:cd17762    67 GVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREV 146

                          90
                  ....*....|...
gi 1779108731 146 GVTYRTGITASSD 158
Cdd:cd17762   147 GLDYRTGTVYTTD 159
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 21-198 3.33e-07

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350159  Cd Length: 222  Bit Score: 49.42  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  21 IVPGDPErVKKIAELMDRAEHLcSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAveelAQLGIRTF-----LRVGTTGA 95
Cdd:cd09008     4 IGAMEEE-IAPLLELLENVEEE-TIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIA----TQLLIDRFkpdaiINTGVAGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  96 IQEDIDVGSVIVTTGSVRLD-GASQHFAPLEYPA--VADFECANAMVMASRD----RGVTYRTGITASSDTFYPGQERYD 168
Cdd:cd09008    78 LDPDLKIGDVVIATKVVYHDvDATAFGYEGGQPPgmPAYFPADPELLELAKKaakeLGPKVHTGLIASGDQFVASSEKKE 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 1779108731 169 TLRgyvirkyqgsmnewQNLGVLNYEMESA 198
Cdd:cd09008   158 ELR--------------ENFPALAVEMEGA 173
PRK07115 PRK07115
AMP nucleosidase; Provisional
 66-154 1.20e-05

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 45.34  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  66 GIGGPSTSIAVEELAQLGIRTFLRVGTTGAIQEDIDVGSVIVTTGSVRLDGASQHFAPLEYPAVADFECANAMVMASRDR 145
Cdd:PRK07115   68 GMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVSSIIRDK 147


                  ....*....
gi 1779108731 146 GVTYRTGIT 154
Cdd:PRK07115  148 GLDYWTGTV 156
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 19-209 4.93e-03

nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs), as well as futalosine nucleosidase and adenosylhopane nucleosidase. Bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350170 [Multi-domain]  Cd Length: 210  Bit Score: 37.27  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  19 LAIVPGDPERVKKIAELMDRAEHLcSHREYTIWRAYIGDNAVIVCSTGIGGPSTSIAVEELA-QLGIRTFLRVGTTGAIQ 97
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKV-RLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1779108731  98 EDIDVGSVIVTTGSVRLDG-ASQHFAPLEYP-AVADFECANamvmasrdRGVTYRTGITASSDTFypgqerydtlrgyvI 175
Cdd:cd17877    80 PGLAVGDLVIADRVLYHDGdVPAGLEADEKLvALAEELAAG--------LNLKVHRGTIITVDAI--------------V 137

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1779108731 176 RKYQGSMNEWQNLGVLNYEMESATLLTMCAALGL 209
Cdd:cd17877   138 RKSAEKAALAARFPALAVDMESAAIAQVAAARGI 171
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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