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Conserved domains on  [gi|899771135|emb|CQI89672|]
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uridine phosphorylase [Streptococcus agalactiae]

Protein Classification

nucleoside phosphorylase( domain architecture ID 13027136)

nucleoside phosphorylase similar to uridine phosphorylase (UP), a key enzyme in the pyrimidine salvage pathway that 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
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 12-250 1.14e-140

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: 394.50  E-value: 1.14e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEP 171
Cdd:cd17767   81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899771135 172 ERMPVSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEALR 250
Cdd:cd17767  161 PGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEALK 239
 
Name Accession Description Interval E-value
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 12-250 1.14e-140

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: 394.50  E-value: 1.14e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEP 171
Cdd:cd17767   81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899771135 172 ERMPVSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEALR 250
Cdd:cd17767  161 PGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-254 9.23e-125

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 354.47  E-value: 9.23e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   1 MQNYSGEVGLQYHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIA 80
Cdd:COG2820    1 MKESELPDGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  81 MEELKLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQ 160
Cdd:COG2820   81 VEELAALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 161 CKDAFYGQHEPERmPVSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNpmAHDTEA 240
Cdd:COG2820  161 STDGFYAEQGREL-RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVER 237

                        250
                 ....*....|....
gi 899771135 241 AIQVAVEALRTLIE 254
Cdd:COG2820  238 AIKVALEALKKLIE 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 12-253 1.62e-102

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: 297.96  E-value: 1.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:TIGR01718   2 YHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGART 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEP 171
Cdd:TIGR01718  82 FIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  172 ERMP--VSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEAL 249
Cdd:TIGR01718 162 DTYSgrVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVAVEAV 241


                  ....
gi 899771135  250 RTLI 253
Cdd:TIGR01718 242 KRLL 245
PRK11178 PRK11178
uridine phosphorylase; Provisional
 26-253 2.03e-67

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 209.13  E-value: 2.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  26 IMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTCGGIDLDV 105
Cdd:PRK11178  21 IVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGVRTFLRIGTTGAIQPHI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 106 KGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFY-GQhepERMP-----VSYE 179
Cdd:PRK11178 101 NVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpGQ---ERYDtysgrVVRR 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899771135 180 LLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEALRTLI 253
Cdd:PRK11178 178 FKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL 251
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-254 3.77e-45

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: 151.34  E-value: 3.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   23 RYVIMPGDPKRCAKIAEHFDNAV-LVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEE--LKLCGADTFIRVGTCG 99
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  100 GIDLDVKGGDIVIATGAIRMEGTSK-------EYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFY-GQHEP 171
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYfETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  172 ERMpvsyellnkweaWKRLGTKASEMESAALFVAASHLGVRCGSdFLVVGNQerNALGMDNPMAHDT-EAAIQVAVEALR 250
Cdd:pfam01048 161 IRL------------LRRLGADAVEMETAAEAQVAREAGIPFAA-IRVVSDL--AAGGADGELTHEEvEEFAERAAERAA 225


                  ....
gi 899771135  251 TLIE 254
Cdd:pfam01048 226 ALLL 229
 
Name Accession Description Interval E-value
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 12-250 1.14e-140

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: 394.50  E-value: 1.14e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:cd17767    1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEP 171
Cdd:cd17767   81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899771135 172 ERMPVSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEALR 250
Cdd:cd17767  161 PGPGLPPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVALEALK 239
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 1-254 9.23e-125

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 354.47  E-value: 9.23e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   1 MQNYSGEVGLQYHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIA 80
Cdd:COG2820    1 MKESELPDGSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  81 MEELKLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQ 160
Cdd:COG2820   81 VEELAALGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 161 CKDAFYGQHEPERmPVSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNpmAHDTEA 240
Cdd:COG2820  161 STDGFYAEQGREL-RVDPDLDEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDP--EEAVER 237

                        250
                 ....*....|....
gi 899771135 241 AIQVAVEALRTLIE 254
Cdd:COG2820  238 AIKVALEALKKLIE 251
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 12-253 1.62e-102

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: 297.96  E-value: 1.62e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:TIGR01718   2 YHLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGART 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEP 171
Cdd:TIGR01718  82 FIRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  172 ERMP--VSYELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEAL 249
Cdd:TIGR01718 162 DTYSgrVVRHFKGSMEAWQAMGVLNYEMESATLFTLCSSQGLRAGMVAGVIVNRTQQEIPNEETMKQTEEHAIKVAVEAV 241


                  ....
gi 899771135  250 RTLI 253
Cdd:TIGR01718 242 KRLL 245
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 24-248 2.64e-79

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: 237.96  E-value: 2.64e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  24 YVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTCGGIDL 103
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 104 DVKGGDIVIATGAIRMEGTSKEY-APIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGqhepermpvsyELLN 182
Cdd:cd09005   81 DIKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYR-----------ETRE 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 899771135 183 KWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALG-MDNPMAHDTEAAIQVAVEA 248
Cdd:cd09005  150 ESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGfVDEFLSEAEKKAIEIALDA 216
PRK11178 PRK11178
uridine phosphorylase; Provisional
 26-253 2.03e-67

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 209.13  E-value: 2.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  26 IMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTCGGIDLDV 105
Cdd:PRK11178  21 IVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGVRTFLRIGTTGAIQPHI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 106 KGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFY-GQhepERMP-----VSYE 179
Cdd:PRK11178 101 NVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpGQ---ERYDtysgrVVRR 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 899771135 180 LLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSDFLVVGNQERNALGMDNPMAHDTEAAIQVAVEALRTLI 253
Cdd:PRK11178 178 FKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL 251
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 13-249 7.17e-63

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: 196.76  E-value: 7.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  13 HLQIRPGDVGRYVIMPGDPKRCAKIAEHF-DNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADT 91
Cdd:cd17765    4 HIRAEPGDVAEAVLLPGDPGRATYIAETFfDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGVKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  92 FIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIE-FPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHe 170
Cdd:cd17765   84 LIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEpYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFYDPT- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 171 PERMPvsyellnkweAWKRLGTKASEMESAALFVAASHLGVRCGSDFLV---VGNQERNAlgMDNPMAHDTEAAIQVAVE 247
Cdd:cd17765  163 PDGVK----------RWRRRGVLAVEMEASALFTLAALRGLRAGCILTVsdlIGDPERRI--DDEELRAGVDRMTEVALE 230


                 ..
gi 899771135 248 AL 249
Cdd:cd17765  231 AV 232
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 13-212 3.27e-56

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: 179.93  E-value: 3.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  13 HLQIRPGDVGRYVIMPGDPKRCAKIAEHF-DNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGAD 90
Cdd:COG0813    5 HIGAKKGDIAETVLLPGDPLRAKYIAETFlEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELiTEYGVK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  91 TFIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYA-PIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGqh 169
Cdd:COG0813   85 NIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFgGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFYR-- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 899771135 170 epermpvsyELLNKWEAWKRLGTKASEMESAALFVAASHLGVR 212
Cdd:COG0813  163 ---------EDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKR 196
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 13-212 1.33e-54

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: 175.67  E-value: 1.33e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  13 HLQIRPGDVGRYVIMPGDPKRCAKIAEHF-DNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGAD 90
Cdd:cd09006    1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFlEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELfKFYGVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  91 TFIRVGTCGGIDLDVKGGDIVIATGAirmeGTSKEYA-----PIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAF 165
Cdd:cd09006   81 NIIRIGTCGAYQPDLKLRDVVLAMGA----STDSNYNrlrfgGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 899771135 166 YGQHEpermpvsyellNKWEAWKRLGTKASEMESAALFVAASHLGVR 212
Cdd:cd09006  157 YDDDP-----------ELWKKLKKYGVLAVEMEAAALYTNAARLGKK 192
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 25-252 4.61e-53

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: 171.25  E-value: 4.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  25 VIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTCGGIDLD 104
Cdd:cd17764    3 VIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLVPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 105 VKGGDIVIATGAIRME-GTSKEYAP-IEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEpermpvsyELLN 182
Cdd:cd17764   83 LRVGDIVVATGASYYPgGGLGQYFPdVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDE--------EFAE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899771135 183 KweaWKRLGTKASEMESAALFVAASHLGVRCGSdFLVVGNqerNALGMDNPMAHDTE---AAIQVAVEALRTL 252
Cdd:cd17764  155 R---WSSLGFIAVEMECATLFTLGWLRGVKAGA-VLVVSD---NLVKGGKLMLTKEEleeKVMKAAKAVLEAL 220
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
13-212 3.32e-49

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 161.95  E-value: 3.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  13 HLQIRPGDVGRYVIMPGDPKRCAKIAEHF-DNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGAD 90
Cdd:PRK05819   4 HINAKKGDIADTVLMPGDPLRAKYIAETFlEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELiTDYGVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  91 TFIRVGTCGGIDLDVKGGDIVIATGA------IRMegtskEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDA 164
Cdd:PRK05819  84 KLIRVGSCGALQEDVKVRDVVIAMGAstdsnvNRI-----RFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 899771135 165 FYgQHEPERmpvsyellnkWEAWKRLGTKASEMESAALFVAASHLGVR 212
Cdd:PRK05819 159 FY-NPDPEM----------FDVLEKYGVLGVEMEAAALYGLAAKYGVK 195
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-254 3.77e-45

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: 151.34  E-value: 3.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   23 RYVIMPGDPKRCAKIAEHFDNAV-LVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEE--LKLCGADTFIRVGTCG 99
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrlLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  100 GIDLDVKGGDIVIATGAIRMEGTSK-------EYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFY-GQHEP 171
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPlfgpeggPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYfETPAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  172 ERMpvsyellnkweaWKRLGTKASEMESAALFVAASHLGVRCGSdFLVVGNQerNALGMDNPMAHDT-EAAIQVAVEALR 250
Cdd:pfam01048 161 IRL------------LRRLGADAVEMETAAEAQVAREAGIPFAA-IRVVSDL--AAGGADGELTHEEvEEFAERAAERAA 225


                  ....
gi 899771135  251 TLIE 254
Cdd:pfam01048 226 ALLL 229
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 12-249 8.01e-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: 133.75  E-value: 8.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  12 YHLQIRPGDVGRYVIMPGDPKRCAKIAEHFDNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEEL------- 84
Cdd:cd00436   11 YHLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELdalvnid 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  85 -------KLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEGT-------------SKEYAPIEFPAV---------- 134
Cdd:cd00436   91 fktrtpkEEKTSLNIIRLGTSGALQPDIPVGSLVISSYAIGLDNLlnfydhpntdeeaELENAFIAHTSWfkgkprpyvv 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 135 -ADLEVTNALVNAAKKLGYTSHAGvvqckdAFYGqhePE----RMPVSY-ELLNKWEAWKRLGTKAS--EMESAALFVAA 206
Cdd:cd00436  171 kASPELLDALTGVGYVVGITATAP------GFYG---PQgrqlRLPLADpDLLDKLSSFSYGGLRITnfEMETSAIYGLS 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 899771135 207 SHLGVRCGSDFLVVGNqeRNALGMDNPMAHDTEAAIQVAVEAL 249
Cdd:cd00436  242 RLLGHRALSICAIIAN--RATGEFSKDYKKAVEKLIEKVLEAL 282
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
13-212 1.11e-35

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 127.14  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  13 HLQIRPGDVGRYVIMPGDPKRCAKIAEHF-DNAVLVADSREYVTYTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGAD 90
Cdd:PRK13374   5 HINAQPGDFAETVLMPGDPLRAKYIAETYlEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELiATFGVK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  91 TFIRVGTCGGIDLDVKGGDIVIATGAirmeGT-----SKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAF 165
Cdd:PRK13374  85 NIIRVGSCGATQDDVKLMDVIIAQGA----STdsktnRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 899771135 166 YGQHEpermpvsyellNKWEAWKRLGTKASEMESAALFVAASHLGVR 212
Cdd:PRK13374 161 YDPDE-----------DAIEAMERFGILGVDMEVAGLYGLAAYLGAE 196
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 19-248 4.90e-34

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: 122.21  E-value: 4.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  19 GDVGRYVIMPGDPKRCAKIAEHFDNAVlvadsreyvtYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTC 98
Cdd:cd09007   11 GDLLEYLLEEYGAEKIGELSSAGHTPL----------YRLEYDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  99 GGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYgqhepeRmpvsy 178
Cdd:cd09007   81 GSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEPDPELLDALEEALEKAGIPYVRGKTWTTDAPY------R----- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 899771135 179 ELLNKWEAWKRLGTKASEMESAALFVAASHLGVRCGSdFLVVGN---QERNALGMDNPMAHDTEAAIQVAVEA 248
Cdd:cd09007  150 ETRAKVARRRAEGCLAVEMEAAALFAVAQFRGVELAQ-LLYVSDslaGEEWDPRGRDEGKDAREKALELALEA 221
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 16-219 1.28e-17

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: 79.52  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  16 IRPGDVGRYVIMPGDPKRCAKIAEHFDNaVLVADSREYVTYTgtLNGEKVSVTSTGIGGPSASIAMEELKLCGADTFIRV 95
Cdd:cd17762   15 TPLEDFQRYILLTNFDMYVDEFAERTGV-PIRGGSVQMPAAH--LKKEGITIINFGVGSPNAATITDLLAVLRPKAVLML 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  96 GTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEVTNALVNAAKKLGYTSHAGVVQCKDafygqhepERMp 175
Cdd:cd17762   92 GHCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREVGLDYRTGTVYTTD--------RRN- 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 899771135 176 vsyellnkWE----AWKRL-GTKAS--EMESAALFVAASHLGVRCGSDFLV 219
Cdd:cd17762  163 --------WEfdeaFKEYLrESRAIaiDMESATIFAVGFANRVPYGALLLV 205
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 29-167 1.93e-17

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: 79.16  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  29 GDPKRCAKIAEHFDN--AVLVADS-REYVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLC--GADTFIRVGTCGGIDL 103
Cdd:cd17769    7 GDPARARLIAKLLDKepKVFELTSeRGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCGSLDP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899771135 104 DVKGGDIVIATGAI-------------RMEGTSKEYApIEFPAVADLEVTNALVNA--AKKLGYTSHAGVVQCKDAFYG 167
Cdd:cd17769   87 DVPVGSVVVPSASVavtrnyddddfagPSTSSEKPYL-ISKPVPADPELSELLESElkASLGGEVVVEGLNASADSFYS 164
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 19-214 3.12e-17

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: 78.73  E-value: 3.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  19 GDVgRYVIMPGDPKRCAKIAEHFDNAV------------LVADSREYVTYtgtlngeKV----SVtSTGIGGPSASIAME 82
Cdd:cd17763   21 GDV-KFVCMGGSPGRMENFAEYLAKELgiklpagaalvnLSKTTDRYSMY-------KVgpvlSV-SHGMGIPSLSILLH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  83 EL-KL-----CGADTFIRVGTCGGIdlDVKGGDIVIATGAirMEGTSKEY-------APIEFPAVADLEVTNALVNAAKK 149
Cdd:cd17763   92 ELiKLlhyagCKDVTFIRIGTSGGI--GVEPGTVVITTEA--VDGELEPFyeqvilgKVVKRPAVLDAQLAEELLECAKE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 150 LG-YTSHAGVVQCKDAFY-GQHEPERMPVSYELLNKWEAWKRL---GTKASEMESAALFVAASHLGVRCG 214
Cdd:cd17763  168 LDdFPTVIGKTMCANDFYeGQGRLDGAFCDYTEEDKMAFLQKLydaGVRNIEMESLCFAAFCHRAGIKAA 237
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 56-255 2.53e-15

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: 73.02  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  56 YTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEG--TSKEYAPIEFP 132
Cdd:COG0775   34 YLGTLGGKEVVLVNSGIGKVNAATATTLLiARFRPDAVINTGVAGGLDPDLKIGDVVLATEVVQHDVdvTAFGYPRGQVP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 133 AV-----ADLEVTNALVNAAKKLGYTSHAGVVQCKDAFygQHEPERMPVSYELLNkweawkrlGTKASEMESAALFVAAS 207
Cdd:COG0775  114 GMpalfeADPALLEAAKEAAKESGLKVVTGTIATGDRF--VWSAEEKRRLRERFP--------GALAVDMEGAAIAQVCY 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 899771135 208 HLGV-----RCGSDFlvvgnqernaLGMDNPMAHDT--EAAIQVAVEALRTLIEN 255
Cdd:COG0775  184 RFGVpflviRAISDL----------AGEKAPNDFDEflEEAAKNAAELLRALLRK 228
PRK07115 PRK07115
AMP nucleosidase; Provisional
 63-258 6.11e-13

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 66.52  E-value: 6.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  63 EKVSVTSTGIGGPSASIAMEelkLCGA---DTFIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSKEYAPIEFPAVADLEV 139
Cdd:PRK07115  60 EGITIINFGMGSPNAATIMD---LLSAlnpKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 140 TNALVNAAKKLGYTSHAGVVQCKDAFYGQHEPERMpvsyellnkwEAWKRLGTKASEMESAALFVA--ASHLGVrcGSDF 217
Cdd:PRK07115 137 QKAVSSIIRDKGLDYWTGTVYTTNRRFWEHDKEFK----------EYLYETRAQAIDMETATLFAAgfANNIPT--GALL 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 899771135 218 LVvgnqernalgMDNPMAHD---------------TEAAIQVAVEALRTLIENDKS 258
Cdd:PRK07115 205 LI----------SDLPLRPEgvktkesdnkvtktyTEEHIEIGIEALKSLRKKGKG 250
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 12-214 2.44e-12

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: 65.17  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   12 YHLQI---------RPGDVgRYVIMPGDPKRCAKIAEHF----------DNAVLVADSREYVTY-TGtlngeKVSVTSTG 71
Cdd:TIGR01719  13 YHFGIntsthdfpaVFGDV-KFVCMGGTPSRMKAFARYVgaelglscgrDYPNISERGDRFAMYkVG-----PVLCVSHG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135   72 IGGPSASIAMEEL-KL-----CGADTFIRVGTCGGIdlDVKGGDIVIATGAIRME----------GTSKEYAPIEFPAVA 135
Cdd:TIGR01719  87 MGIPSISIMLHELiKLlyyarCKNPTFIRIGTSGGI--GVPPGTVVVSSEAVDAClkpeyeqivlGKRVIRPTQLDEALV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  136 DlevtNALVNAAKKL-GYTSHAGVVQCKDAFY-GQHEPERMPVSYELLNKwEAWKR----LGTKASEMESAALFVAASHL 209
Cdd:TIGR01719 165 Q----ELLLCGAEGLdEFTTVSGNTMCTDDFYeGQGRLDGAFCEYTEKDK-MAYLRklyaLGVRNIEMESSMFAAMTSRA 239


                  ....*
gi 899771135  210 GVRCG 214
Cdd:TIGR01719 240 GFKAA 244
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 56-220 1.03e-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: 62.51  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  56 YTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGADTFIRVGTCGGIDLDVKGGDIVIAT---------GAIRMEGTSKE 125
Cdd:cd09008   32 YEGTLGGKEVVLVQSGIGKVNAAIATQLLiDRFKPDAIINTGVAGGLDPDLKIGDVVIATkvvyhdvdaTAFGYEGGQPP 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 126 YAPIEFPAvadlevTNALVNAAKKLGYTSHAGVVQCK----DAFYgqHEPERmpvsYELLNkweawKRLGTKASEMESAA 201
Cdd:cd09008  112 GMPAYFPA------DPELLELAKKAAKELGPKVHTGLiasgDQFV--ASSEK----KEELR-----ENFPALAVEMEGAA 174

                        170
                 ....*....|....*....
gi 899771135 202 LFVAASHLGVrcgsDFLVV 220
Cdd:cd09008  175 IAQVCYLNGV----PFLVI 189
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
50-213 4.02e-09

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 55.51  E-value: 4.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  50 SREYvtYTGTLNGEKVSVTSTGIGGPSASI---AMeeLKLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIR--MEGTSK 124
Cdd:PRK05584  30 GREF--YTGTLHGHEVVLVLSGIGKVAAALtatIL--IEHFKVDAVINTGVAGGLAPGLKVGDVVVADELVQhdVDVTAF 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 125 EYAPIEFPA-----VADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYgqHEPERMpvsyellnkweAWKR---LGTKASE 196
Cdd:PRK05584 106 GYPYGQVPGlpaafKADEKLVALAEKAAKELNLNVHRGLIASGDQFI--AGAEKV-----------AAIRaefPDALAVE 172

                        170
                 ....*....|....*..
gi 899771135 197 MESAALFVAASHLGVRC 213
Cdd:PRK05584 173 MEGAAIAQVCHEFGVPF 189
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 56-216 2.09e-06

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 47.31  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  56 YTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEgTSKEYAPIEFPAV 134
Cdd:PRK14697  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLiHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHD-VSKTQMKNLFPFQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 135 ADLEVTNALVNAAKK------LGYTSHAGVVQCKDAFYgqhepERMPVSYELLNKWeawkrlGTKASEMESAALFVAA-- 206
Cdd:PRK14697 114 EEFIASKELVELARKacnsssLHIEIHEGRIVSGECFV-----EDSKLKAKLIDEY------APHCTEMEGAAIGHVAyi 182

                        170
                 ....*....|...
gi 899771135 207 ---SHLGVRCGSD 216
Cdd:PRK14697 183 nevPFLVIRCISD 195
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 53-216 1.76e-05

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: 44.59  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  53 YVTYTGTLNGEKVSVTSTGIGGPSASIAMEELKLCGA-DTFIRVGTCGGIDLDVKGGDIVIATGAIRMEGTSkeyaPIEF 131
Cdd:cd17877   29 FRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQpDLIISTGFAGGLDPGLAVGDLVIADRVLYHDGDV----PAGL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 132 PavADLEVTNALVNAAKKLGYTSHAGVVQCKDAFYGQHEPERMpvsyeLLNkweawkRLGTKASEMESAAL-FVAASH-- 208
Cdd:cd17877  105 E--ADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAA-----LAA------RFPALAVDMESAAIaQVAAARgi 171

                        170
                 ....*....|
gi 899771135 209 --LGVRCGSD 216
Cdd:cd17877  172 pfLAIRAISD 181
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 56-216 3.59e-05

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 44.62  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  56 YTGTLNGEKVSVTSTGIGGPSASIAMEEL-KLCGADTFIRVGTCGGIDLDVKGGDIVIATGAIRMEgTSKEYAPIEFPAV 134
Cdd:PRK06698  35 YVGEFMGTEVIVTRCGVGKVNAAACTQTLiHKFDVDAIINTGVAGGLHPDVKVGDIVISTNVTHHD-VSKTQMKNLFPFQ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 135 ADLEVTNALVNAAKKLGYTS------HAGVVQCKDAFYgqhepERMPVSYELLNKWEAwkrlgtKASEMESAALFVAA-- 206
Cdd:PRK06698 114 EEFIASKELVELARKACNSSslhmeiHEGRIVSGECFV-----EDSKLKAKLIDEYAP------HCTEMEGAAIGHVAyi 182

                        170
                 ....*....|...
gi 899771135 207 ---SHLGVRCGSD 216
Cdd:PRK06698 183 nevPFLVIRCISD 195
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 62-220 7.69e-04

adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG; adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 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). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (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 PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350168  Cd Length: 188  Bit Score: 39.45  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135  62 GEKVSVTSTGIGGPSASIAMEELKLCGADTFIRVGTCGGIDLDVKGGDIVIATgAIRMEGTSkeyapieFPavADLEVTN 141
Cdd:cd17768   20 GDGLLVILSGAGPERARRAAERLLAAGARALISFGVAGGLDPALKPGDLVLPE-AVVADGER-------YP--TDPAWRR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899771135 142 ALVNAAKKLGyTSHAGVVQCKDAfygqhepermPVSYEllnkwEAWKRL----GTKASEMESAALFVAASHLGVrcgsDF 217
Cdd:cd17768   90 RLLRALPAGL-RVVAGPLAGSDA----------PVLSV-----ADKAALhaatGAVAVDMESGAVAAVAAEAGL----PF 149


                 ...
gi 899771135 218 LVV 220
Cdd:cd17768  150 AAI 152
 
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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