NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491949012|ref|WP_005686705|]
View 

uridine phosphorylase [Haemophilus influenzae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 539.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   1 MSDVFHLNLTKAQLKGATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELA 80
Cdd:PRK11178   1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  81 QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTF 160
Cdd:PRK11178  81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 161 YPGQERYDTYSGKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAV 240
Cdd:PRK11178 161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                        250
                 ....*....|.
gi 491949012 241 SVVIAAAQALL 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: 539.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   1 MSDVFHLNLTKAQLKGATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELA 80
Cdd:PRK11178   1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  81 QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTF 160
Cdd:PRK11178  81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 161 YPGQERYDTYSGKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAV 240
Cdd:PRK11178 161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                        250
                 ....*....|.
gi 491949012 241 SVVIAAAQALL 251
Cdd:PRK11178 241 KIVVEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 5-247 2.45e-126

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: 357.91  E-value: 2.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   5 FHLNLTKAQLkgATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLGV 84
Cdd:cd17767    1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  85 RTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQ 164
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 165 ERYDTYsgkVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAVSVVI 244
Cdd:cd17767  159 GRPGPG---LPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                 ...
gi 491949012 245 AAA 247
Cdd:cd17767  236 EAL 238
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-250 1.25e-116

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 333.67  E-value: 1.25e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   1 MSDVFHLNLTKAQLkgATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELA 80
Cdd:COG2820    8 DGSQYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  81 QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTF 160
Cdd:COG2820   86 ALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 161 YPGQERYDtysgKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAaiKQTEEKAV 240
Cdd:COG2820  166 YAEQGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAI 239

                        250
                 ....*....|
gi 491949012 241 SVVIAAAQAL 250
Cdd:COG2820  240 KVALEALKKL 249
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 4-251 2.02e-115

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: 330.70  E-value: 2.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012    4 VFHLNLTKAQLKgaTLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLG 83
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   84 VRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPG 163
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  164 QERyDTYSGKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAVSVV 243
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 491949012  244 IAAAQALL 251
Cdd:TIGR01718 238 VEAVKRLL 245
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 18-252 1.02e-39

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: 137.09  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   18 TLAIVPGDPARSERIAKQLDN-PEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEE--LAQLGVRTFLRIGTTG 94
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDeTPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   95 AIQPHINVGDVLITTAAVRLDGASR-------HFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQERY 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  168 dtysgkvyrdyqglLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGV--IVNRTQQEIPNEAAIKQTEEKAVSVVIA 245
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*..
gi 491949012  246 AAQALLS 252
Cdd:pfam01048 227 LLLALLA 233
 
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: 539.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   1 MSDVFHLNLTKAQLKGATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELA 80
Cdd:PRK11178   1 MSDVFHLGLTKADLQGATLAIVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  81 QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTF 160
Cdd:PRK11178  81 QLGVRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 161 YPGQERYDTYSGKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAV 240
Cdd:PRK11178 161 YPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAV 240

                        250
                 ....*....|.
gi 491949012 241 SVVIAAAQALL 251
Cdd:PRK11178 241 KIVVEAARRLL 251
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 5-247 2.45e-126

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: 357.91  E-value: 2.45e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   5 FHLNLTKAQLkgATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLGV 84
Cdd:cd17767    1 YHIGLKPGDV--APYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  85 RTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQ 164
Cdd:cd17767   79 KTFIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 165 ERYDTYsgkVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAVSVVI 244
Cdd:cd17767  159 GRPGPG---LPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235


                 ...
gi 491949012 245 AAA 247
Cdd:cd17767  236 EAL 238
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-250 1.25e-116

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 333.67  E-value: 1.25e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   1 MSDVFHLNLTKAQLkgATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELA 80
Cdd:COG2820    8 DGSQYHLGLKPGDV--ADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  81 QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTF 160
Cdd:COG2820   86 ALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGF 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 161 YPGQERYDtysgKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAaiKQTEEKAV 240
Cdd:COG2820  166 YAEQGREL----RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVERAI 239

                        250
                 ....*....|
gi 491949012 241 SVVIAAAQAL 250
Cdd:COG2820  240 KVALEALKKL 249
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 4-251 2.02e-115

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: 330.70  E-value: 2.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012    4 VFHLNLTKAQLKgaTLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLG 83
Cdd:TIGR01718   1 VYHLGLTKNDIQ--TYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   84 VRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPG 163
Cdd:TIGR01718  79 ARTFIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  164 QERyDTYSGKVYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEIPNEAAIKQTEEKAVSVV 243
Cdd:TIGR01718 159 QER-DTYSGRVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVA 237


                  ....*...
gi 491949012  244 IAAAQALL 251
Cdd:TIGR01718 238 VEAVKRLL 245
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 19-246 6.84e-68

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: 208.68  E-value: 6.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  19 LAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLGVRTFLRIGTTGAIQP 98
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  99 HINVGDVLITTAAVRLDGASRHF-VPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQERYdtysgkvyrd 177
Cdd:cd09005   81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREE---------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491949012 178 yqglLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGVIVNRTQQEI--PNEaAIKQTEEKAVSVVIAA 246
Cdd:cd09005  151 ----SEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIgfVDE-FLSEAEKKAIEIALDA 216
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 22-247 3.39e-55

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: 177.11  E-value: 3.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  22 VPGDPARSERIAKQ-LDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLGVRTFLRIGTTGAIQPHI 100
Cdd:cd17765   18 LPGDPGRATYIAETfFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGVKRLIRVGTCGGLSSGL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 101 NVGDVLITTAAVRLDGASRHFVPLE-YPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQErydtysgkvyrdyq 179
Cdd:cd17765   98 QLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPTP-------------- 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 180 GLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGV--IVNRTQQEIPNEaAIKQTEEKAVSVVIAAA 247
Cdd:cd17765  164 DGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdLIGDPERRIDDE-ELRAGVDRMTEVALEAV 232
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 21-246 9.91e-50

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: 162.39  E-value: 9.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  21 IVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQLGVRTFLRIGTTGAIQPHI 100
Cdd:cd17764    4 IAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 101 NVGD-VLITTAAVRLDGASRHFVP-LEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQErydtysgkvyrdy 178
Cdd:cd17764   84 RVGDiVVATGASYYPGGGLGQYFPdVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDE------------- 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491949012 179 qGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAgVIVN---RTQQEIPNEAAIKQTEEKAVSVVIAA 246
Cdd:cd17764  151 -EFAERWSSLGFIAVEMECATLFTLGWLRGVKAGAVL-VVSDnlvKGGKLMLTKEELEEKVMKAAKAVLEA 219
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 21-214 6.63e-43

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: 145.64  E-value: 6.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  21 IVPGDPARSERIAKQ-LDNPEFLTSTRE---FTswlGYINGQPIVVCSTGIGGPSTSICVEELAQ-LGVRTFLRIGTTGA 95
Cdd:COG0813   18 LLPGDPLRAKYIAETfLEDAVLVNEVRGmlgYT---GTYKGKRVSVMGSGMGIPSISIYAYELITeYGVKNIIRVGTCGA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  96 IQPHINVGDVLITTAAVRLDGASRH-FVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFypgqerydtysgkv 174
Cdd:COG0813   95 LQEDVKVRDVVIAMGASTDSNVNRQrFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLF-------------- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491949012 175 YRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMV 214
Cdd:COG0813  161 YREDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAI 200
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 21-217 2.83e-42

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: 143.70  E-value: 2.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  21 IVPGDPARSERIAKQ-LDNPEFLTSTRE---FTswlGYINGQPIVVCSTGIGGPSTSICVEELAQL-GVRTFLRIGTTGA 95
Cdd:cd09006   14 LMPGDPLRAKYIAETfLEDAKLVNSVRNmlgYT---GTYKGKRVSVMGSGMGMPSIGIYAYELFKFyGVKNIIRIGTCGA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  96 IQPHINVGDVLITTAAVRLDGASRH-FVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFypgqerydtysgkv 174
Cdd:cd09006   91 YQPDLKLRDVVLAMGASTDSNYNRLrFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVF-------------- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 491949012 175 YRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGV 217
Cdd:cd09006  157 YDDDPELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 18-252 1.02e-39

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: 137.09  E-value: 1.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   18 TLAIVPGDPARSERIAKQLDN-PEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEE--LAQLGVRTFLRIGTTG 94
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDeTPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   95 AIQPHINVGDVLITTAAVRLDGASR-------HFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQERY 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  168 dtysgkvyrdyqglLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVAGV--IVNRTQQEIPNEAAIKQTEEKAVSVVIA 245
Cdd:pfam01048 161 --------------IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVsdLAAGGADGELTHEEVEEFAERAAERAAA 226


                  ....*..
gi 491949012  246 AAQALLS 252
Cdd:pfam01048 227 LLLALLA 233
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 4-239 3.00e-38

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: 134.91  E-value: 3.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   4 VFHLNLTKAQLkgATLAIVPGDPARSERIAKQLDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEEL---- 79
Cdd:cd00436   10 IYHLHLKPEDL--ADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalv 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  80 ----------AQLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASrHFVPLEYPAVANFECTTALYNAAKAKG-IE 148
Cdd:cd00436   88 nidfktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLL-NFYDHPNTDEEAELENAFIAHTSWFKGkPR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 149 PYV------------------GVTVSSDTFYPGQERYdtysgkVYRD--YQGLLKQ-----WQDLNVMNYEMESSTLFTM 203
Cdd:cd00436  167 PYVvkaspelldaltgvgyvvGITATAPGFYGPQGRQ------LRLPlaDPDLLDKlssfsYGGLRITNFEMETSAIYGL 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491949012 204 CSALGLRAGMVAGVIVNRTQQEIPN--EAAIKQTEEKA 239
Cdd:cd00436  241 SRLLGHRALSICAIIANRATGEFSKdyKKAVEKLIEKV 278
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
23-211 1.62e-35

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 126.51  E-value: 1.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  23 PGDPARSERIAKQ-LDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEELAQ-LGVRTFLRIGTTGAIQPHI 100
Cdd:PRK05819  19 PGDPLRAKYIAETfLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITdYGVKKLIRVGSCGALQEDV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 101 NVGDVLITTAA------VRLDgasrhFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYpgQERYDtysgkv 174
Cdd:PRK05819  99 KVRDVVIAMGAstdsnvNRIR-----FKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY--NPDPE------ 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 491949012 175 yrdyqgLLKQWQDLNVMNYEMESSTLFTMCSALGLRA 211
Cdd:PRK05819 166 ------MFDVLEKYGVLGVEMEAAALYGLAAKYGVKA 196
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
21-211 4.21e-25

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 99.02  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  21 IVPGDPARSERIAKQ-LDNPEFLTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEEL-AQLGVRTFLRIGTTGAIQP 98
Cdd:PRK13374  18 LMPGDPLRAKYIAETyLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELiATFGVKNIIRVGSCGATQD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  99 HINVGDVLITTAAVRLDGASR-HFVPLEYPAVANFECTTALYNAAKAKGIEPYVGVTVSSDTFYPGQErydtysgkvyrd 177
Cdd:PRK13374  98 DVKLMDVIIAQGASTDSKTNRiRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYDPDE------------ 165

                        170       180       190
                 ....*....|....*....|....*....|....
gi 491949012 178 yqGLLKQWQDLNVMNYEMESSTLFTMCSALGLRA 211
Cdd:PRK13374 166 --DAIEAMERFGILGVDMEVAGLYGLAAYLGAEA 197
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 56-215 5.43e-25

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: 98.32  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  56 NGQPIVVCSTGIGGPSTSICVEELAQLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECT 135
Cdd:cd09007   43 DGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEPDPELL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 136 TALYNAAKAKGIEPYVGVTVSSDTFypgqerydtysgkvYRDYQGLLKQWQDLNVMNYEMESSTLFTMCSALGLRAGMVA 215
Cdd:cd09007  123 DALEEALEKAGIPYVRGKTWTTDAP--------------YRETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVELAQLL 188
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 59-221 4.86e-24

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: 97.22  E-value: 4.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  59 PIVVCSTGIGGPSTSICVEELAQL----GVR--TFLRIGTTGAI--QPhinvGDVLITTAAVrlDGASRHFVPL------ 124
Cdd:cd17763   73 PVLSVSHGMGIPSLSILLHELIKLlhyaGCKdvTFIRIGTSGGIgvEP----GTVVITTEAV--DGELEPFYEQvilgkv 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 125 -EYPAVANFECTTALYNAAKAKGIEPYV-GVTVSSDTFYPGQERYD----TYSGKVYRDYqglLKQWQDLNVMNYEMESS 198
Cdd:cd17763  147 vKRPAVLDAQLAEELLECAKELDDFPTViGKTMCANDFYEGQGRLDgafcDYTEEDKMAF---LQKLYDAGVRNIEMESL 223

                        170       180
                 ....*....|....*....|...
gi 491949012 199 TLFTMCSALGLRAGMVAGVIVNR 221
Cdd:cd17763  224 CFAAFCHRAGIKAAVVCVTLLNR 246
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 24-239 4.22e-20

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: 86.09  E-value: 4.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  24 GDPARSERIAKQLDNPE--F-LTSTREFTSWLGYINGQPIVVCSTGIGGPSTSICVEElaqlgVR-------TFLRIGTT 93
Cdd:cd17769    7 GDPARARLIAKLLDKEPkvFeLTSERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVRE-----ARavvdgpmAIIRLGSC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  94 GAIQPHINVGDVLITTAAV----RLDGASRHFVPLE----Y----PAVANFECTTALYNAAKAK-GIEPYV-GVTVSSDT 159
Cdd:cd17769   82 GSLDPDVPVGSVVVPSASVavtrNYDDDDFAGPSTSsekpYliskPVPADPELSELLESELKASlGGEVVVeGLNASADS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 160 FYPGQERYDTYsgkvYRDY-QGLLKQWQD--LNVMNYEMESSTLF---TMCSALG--LRAGMVAGVIVNRTQQEIPNEAA 231
Cdd:cd17769  162 FYSSQGRQDPN----FPDHnENLIDKLLKryPGAASLEMETFHLFhlaRCSRPAQgkIRAAAAHMVFANRTSNDFISPER 237


                 ....*...
gi 491949012 232 IKQTEEKA 239
Cdd:cd17769  238 VHELERWA 245
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 59-221 1.03e-16

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: 77.49  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012   59 PIVVCSTGIGGPSTSICVEEL------AQLGVRTFLRIGTTGAIQphINVGDVLITTAAVRLDGASRHFVPLEYPAVANF 132
Cdd:TIGR01719  79 PVLCVSHGMGIPSISIMLHELikllyyARCKNPTFIRIGTSGGIG--VPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  133 -ECTTALYNAAKA------KGIEPYVGVTVSSDTFYPGQERYD----TYSGKvyrDYQGLLKQWQDLNVMNYEMESSTLF 201
Cdd:TIGR01719 157 tQLDEALVQELLLcgaeglDEFTTVSGNTMCTDDFYEGQGRLDgafcEYTEK---DKMAYLRKLYALGVRNIEMESSMFA 233

                         170       180
                  ....*....|....*....|
gi 491949012  202 TMCSALGLRAGMVAGVIVNR 221
Cdd:TIGR01719 234 AMTSRAGFKAAVVCVTLLNR 253
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 32-252 2.61e-14

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: 69.94  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  32 IAKQLDNPEFLTStREFTSWLGYINGQPIVVCSTGIGGPSTSICVEEL-AQLGVRTFLRIGTTGAIQPHINVGDVLITTA 110
Cdd:COG0775   16 LLEALEDKKEVQI-AGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGLDPDLKIGDVVLATE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 111 AVRLDGASRHFvPLEYPAV----ANFECTTALYNAAKA----KGIEPYVGVTVSSDTFypgqerydtYSGKVYRDYqgLL 182
Cdd:COG0775   95 VVQHDVDVTAF-GYPRGQVpgmpALFEADPALLEAAKEaakeSGLKVVTGTIATGDRF---------VWSAEEKRR--LR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491949012 183 KQWQDLNVMnyEMESSTLFTMCSALGLRAGMVAGvIVNRTQQEIPN--EAAIKQTEEKAVSVVIAAAQALLS 252
Cdd:COG0775  163 ERFPGALAV--DMEGAAIAQVCYRFGVPFLVIRA-ISDLAGEKAPNdfDEFLEEAAKNAAELLRALLRKLRS 231
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 66-202 1.42e-13

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: 67.96  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  66 GIGGPSTSICVEELAQLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAK 145
Cdd:cd17762   67 GVGSPNAATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREV 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491949012 146 GIEPYVGVTVSSDtfypgqerydtysgkvYR----DYQglLKQW-QDLNVMNYEMESSTLFT 202
Cdd:cd17762  147 GLDYRTGTVYTTD----------------RRnwefDEA--FKEYlRESRAIAIDMESATIFA 190
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 30-160 5.31e-11

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: 60.59  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  30 ERIAKQLDNPEFLT-STREFtsWLGYINGQPIVVCSTGIGGPSTSICVEELAQL-GVRTFLRIGTTGAIQPHINVGDVLI 107
Cdd:cd09008   12 APLLELLENVEEETiAGRTF--YEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRfKPDAIINTGVAGGLDPDLKIGDVVI 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 108 TTAAVRLD-GASRHFVPLEYPA--VANFECTTALYNAAKA----KGIEPYVGVTVSSDTF 160
Cdd:cd09008   90 ATKVVYHDvDATAFGYEGGQPPgmPAYFPADPELLELAKKaakeLGPKVHTGLIASGDQF 149
PRK07115 PRK07115
AMP nucleosidase; Provisional
 66-202 1.04e-09

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 57.28  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  66 GIGGPSTSICVEELAQLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLEYPAVANFECTTALYNAAKAK 145
Cdd:PRK07115  68 GMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVSSIIRDK 147

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012 146 GIEPYVGVTvssdtfYPGQER---YDtysgKVYRDYqglLKQwqdLNVMNYEMESSTLFT 202
Cdd:PRK07115 148 GLDYWTGTV------YTTNRRfweHD----KEFKEY---LYE---TRAQAIDMETATLFA 191
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 48-116 2.66e-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: 38.04  E-value: 2.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  48 FTSWLGYINGQPIVVCSTGIGGPSTSICVEELA-QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDG 116
Cdd:cd17877   29 FRFYRGTLGGHPVVLVESGMGKANAARAAQLLLeHFQPDLIISTGFAGGLDPGLAVGDLVIADRVLYHDG 98
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 51-143 8.77e-03

bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 36.91  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949012  51 WLGYINGQPIVVCSTGIGGPSTSICVEELA-QLGVRTFLRIGTTGAIQPHINVGDVLITTAAVRLDGASRHFVPLeYPAV 129
Cdd:PRK06698  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLIhKFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNL-FPFQ 113

                         90
                 ....*....|....
gi 491949012 130 ANFECTTALYNAAK 143
Cdd:PRK06698 114 EEFIASKELVELAR 127
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH