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Conserved domains on  [gi|1098556778|ref|WP_071237093|]
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MULTISPECIES: nucleoside phosphorylase [Shewanella]

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 ...
 7-228 2.25e-89

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: 263.92  E-value: 2.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARR 86
Cdd:cd17767     1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  87 VIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDE- 165
Cdd:cd17767    81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098556778 166 ---------LEICRHWHRLGVLGADMETAALLTLGRLRGLEVAAVLNNVVLYGEDVQQGINQYVDADSAMMQ 228
Cdd:cd17767   161 pgpglppelPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIR 232
 
Name Accession Description Interval E-value
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-228 2.25e-89

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: 263.92  E-value: 2.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARR 86
Cdd:cd17767     1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  87 VIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDE- 165
Cdd:cd17767    81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098556778 166 ---------LEICRHWHRLGVLGADMETAALLTLGRLRGLEVAAVLNNVVLYGEDVQQGINQYVDADSAMMQ 228
Cdd:cd17767   161 pgpglppelPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIR 232
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 4-186 1.04e-85

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 255.09  E-value: 1.04e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   4 DKQPHICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCG 83
Cdd:COG2820     9 GSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  84 ARRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRD 163
Cdd:COG2820    89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1098556778 164 DE---------LEICRHWHRLGVLGADMETAA 186
Cdd:COG2820   169 QGrelrvdpdlDEKLEAWRKLGVLNVEMETAA 200
PRK11178 PRK11178
uridine phosphorylase; Provisional
 21-185 1.44e-45

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 152.50  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  21 ILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQI 100
Cdd:PRK11178   21 IVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGVRTFLRIGTTGAIQPHI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778 101 ALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFY----RDDEL--EICRH--- 171
Cdd:PRK11178  101 NVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpgqeRYDTYsgRVVRRfkg 180

                         170
                  ....*....|....*...
gi 1098556778 172 ----WHRLGVLGADMETA 185
Cdd:PRK11178  181 smeeWQAMGVMNYEMESA 198
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 8-186 4.38e-45

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: 151.20  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   8 HICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRV 87
Cdd:TIGR01718   3 HLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGARTF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  88 IRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDELE 167
Cdd:TIGR01718  83 IRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQERD 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1098556778 168 -----ICRH-------WHRLGVLGADMETAA 186
Cdd:TIGR01718 163 tysgrVVRHfkgsmeaWQAMGVLNYEMESAT 193
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-186 3.67e-30

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: 112.05  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  20 VILCGEPQRVNRIAALLDDG-RLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELY--QCGARRVIRVGSAGAL 96
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDEtPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlkEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  97 QPQIALGELILAEAAVRDDGGS-------GCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDELEIc 169
Cdd:pfam01048  83 NPDLKVGDVVIPTDAINHDGRSplfgpegGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEI- 161

                         170
                  ....*....|....*..
gi 1098556778 170 RHWHRLGVLGADMETAA 186
Cdd:pfam01048 162 RLLRRLGADAVEMETAA 178
 
Name Accession Description Interval E-value
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 7-228 2.25e-89

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: 263.92  E-value: 2.25e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARR 86
Cdd:cd17767     1 YHIGLKPGDVAPYVLLPGDPGRVERIAELLDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQLGAKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  87 VIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDE- 165
Cdd:cd17767    81 FIRVGTCGALQPDIKLGDLVIATGAVRDEGTSKHYVPPEYPAVADPEVVLALVEAAEELGVPYHVGITASKDSFYGGQGr 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098556778 166 ---------LEICRHWHRLGVLGADMETAALLTLGRLRGLEVAAVLNNVVLYGEDVQQGINQYVDADSAMMQ 228
Cdd:cd17767   161 pgpglppelPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIR 232
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 4-186 1.04e-85

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 255.09  E-value: 1.04e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   4 DKQPHICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCG 83
Cdd:COG2820     9 GSQYHLGLKPGDVADYVILPGDPGRVELIASYLDDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAALG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  84 ARRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRD 163
Cdd:COG2820    89 AKTFIRVGTSGALQPDIPVGDLVIATGAVRLDGTSNFYAPAEYPAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1098556778 164 DE---------LEICRHWHRLGVLGADMETAA 186
Cdd:COG2820   169 QGrelrvdpdlDEKLEAWRKLGVLNVEMETAA 200
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 18-186 2.18e-46

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: 153.53  E-value: 2.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  18 EQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQ 97
Cdd:cd17764     1 ERVIAVGDPGRVELLSTLLEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIMLGAKVIIRLGTAGGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  98 PQIALGELILAEAAV-RDDGGSGCYAPP-GYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDElEICRHWHRL 175
Cdd:cd17764    81 PELRVGDIVVATGASyYPGGGLGQYFPDvCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDE-EFAERWSSL 159

                         170
                  ....*....|.
gi 1098556778 176 GVLGADMETAA 186
Cdd:cd17764   160 GFIAVEMECAT 170
PRK11178 PRK11178
uridine phosphorylase; Provisional
 21-185 1.44e-45

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 152.50  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  21 ILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQI 100
Cdd:PRK11178   21 IVPGDPERVEKIAALMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGVRTFLRIGTTGAIQPHI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778 101 ALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFY----RDDEL--EICRH--- 171
Cdd:PRK11178  101 NVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYpgqeRYDTYsgRVVRRfkg 180

                         170
                  ....*....|....*...
gi 1098556778 172 ----WHRLGVLGADMETA 185
Cdd:PRK11178  181 smeeWQAMGVMNYEMESA 198
Uridine-psphlse TIGR01718
uridine phosphorylase; This model represents a family of bacterial and archaeal uridine ...
 8-186 4.38e-45

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: 151.20  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   8 HICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRV 87
Cdd:TIGR01718   3 HLGLTKNDIQTYVILPGDPDRVEKIAAHMDKPVKVASNREFVTYRGELDGKPVIVCSTGIGGPSTAIAVEELAQLGARTF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  88 IRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDELE 167
Cdd:TIGR01718  83 IRVGTTGAIQPHINVGDVLITTAAVRLDGASLHYAPLEFPAVADFEVTTALVEAAESIGVRHHVGVVASSDTFYPGQERD 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1098556778 168 -----ICRH-------WHRLGVLGADMETAA 186
Cdd:TIGR01718 163 tysgrVVRHfkgsmeaWQAMGVLNYEMESAT 193
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 8-186 6.13e-43

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


Pssm-ID: 350165  Cd Length: 234  Bit Score: 145.14  E-value: 6.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   8 HICLSPAQVSEQVILCGEPQRVNRIAA-LLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARR 86
Cdd:cd17765     4 HIRAEPGDVAEAVLLPGDPGRATYIAEtFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELAQLGVKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  87 VIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAP-PGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYrDDE 165
Cdd:cd17765    84 LIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGgEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFY-DPT 162

                         170       180
                  ....*....|....*....|.
gi 1098556778 166 LEICRHWHRLGVLGADMETAA 186
Cdd:cd17765   163 PDGVKRWRRRGVLAVEMEASA 183
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 7-186 5.52e-41

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: 140.25  E-value: 5.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIAA-LLDDGRLlaeNREFRSMGGF---YQGVAVTVCSTGIGAPSAIIALEELYQC 82
Cdd:COG0813     4 PHIGAKKGDIAETVLLPGDPLRAKYIAEtFLEDAVL---VNEVRGMLGYtgtYKGKRVSVMGSGMGIPSISIYAYELITE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  83 -GARRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPG-YPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSF 160
Cdd:COG0813    81 yGVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGdFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLF 160

                         170       180
                  ....*....|....*....|....*.
gi 1098556778 161 YRDDElEICRHWHRLGVLGADMETAA 186
Cdd:COG0813   161 YREDP-DLLEKLAKYGVLAVEMEAAA 185
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 20-186 1.38e-38

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: 133.57  E-value: 1.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  20 VILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQ 99
Cdd:cd09005     2 AIIPGDPERVDVIDSKLENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALGVDTIIRVGSCGALRED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778 100 IALGELILAEAAVRDDGGSGCY-APPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDElEICRHWHRLGVL 178
Cdd:cd09005    82 IKVGDLVIADGAIRGDGVTPYYvVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETR-EESEKLRKLGAL 160


                  ....*...
gi 1098556778 179 GADMETAA 186
Cdd:cd09005   161 AVEMETSA 168
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 8-186 2.02e-34

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: 122.90  E-value: 2.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   8 HICLSPAQVSEQVILCGEPQRVNRIA-ALLDDGRLLaeNrEFRSMGGF---YQGVAVTVCSTGIGAPSAIIALEELYQC- 82
Cdd:cd09006     1 HIEAKKGDIAKTVLMPGDPLRAKYIAeTFLEDAKLV--N-SVRNMLGYtgtYKGKRVSVMGSGMGMPSIGIYAYELFKFy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  83 GARRVIRVGSAGALQPQIALGELILAEAA------VRDDGGSGCYAPpgypaLASRQLINAMAAYLQRRDCRFHSGIVRS 156
Cdd:cd09006    78 GVKNIIRIGTCGAYQPDLKLRDVVLAMGAstdsnyNRLRFGGGDFAP-----IADFELLRKAVETAKELGIPVHVGNVFS 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1098556778 157 HDSFYRDDELEIcRHWHRLGVLGADMETAA 186
Cdd:cd09006   153 SDVFYDDDPELW-KKLKKYGVLAVEMEAAA 181
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 55-186 1.99e-33

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: 120.28  E-value: 1.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  55 YQGVAVTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQL 134
Cdd:cd09007    42 YDGEEVGVVGPPVGAPAAVLVLEELIALGAKKFIVVGSCGSLDPDLAVGDIILPTSALRDEGTSYHYLPPSRYIEPDPEL 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1098556778 135 INAMAAYLQRRDCRFHSGIVRSHDSFYRDDELEIcRHWHRLGVLGADMETAA 186
Cdd:cd09007   122 LDALEEALEKAGIPYVRGKTWTTDAPYRETRAKV-ARRRAEGCLAVEMEAAA 172
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 20-186 3.67e-30

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: 112.05  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  20 VILCGEPQRVNRIAALLDDG-RLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELY--QCGARRVIRVGSAGAL 96
Cdd:pfam01048   3 AIIGGSPEELALLAELLDDEtPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlkEFGVDAIIRTGTAGGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  97 QPQIALGELILAEAAVRDDGGS-------GCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDELEIc 169
Cdd:pfam01048  83 NPDLKVGDVVIPTDAINHDGRSplfgpegGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAEI- 161

                         170
                  ....*....|....*..
gi 1098556778 170 RHWHRLGVLGADMETAA 186
Cdd:pfam01048 162 RLLRRLGADAVEMETAA 178
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
7-186 5.09e-29

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 109.18  E-value: 5.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIA-ALLDDGRLLaenREFRSMGGF---YQGVAVTVCSTGIGAPSAIIALEELYQ- 81
Cdd:PRK05819    3 PHINAKKGDIADTVLMPGDPLRAKYIAeTFLEDVVCV---NEVRGMLGFtgtYKGKRVSVMGTGMGIPSISIYANELITd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  82 CGARRVIRVGSAGALQPQIALGELILAEAA------VRDDGGSGCYAPpgypaLASRQLINAMAAYLQRRDCRFHSGIVR 155
Cdd:PRK05819   80 YGVKKLIRVGSCGALQEDVKVRDVVIAMGAstdsnvNRIRFKGHDFAP-----IADFDLLRKAYDAAKEKGITVHVGNVF 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1098556778 156 SHDSFYRDDElEICRHWHRLGVLGADMETAA 186
Cdd:PRK05819  155 SADLFYNPDP-EMFDVLEKYGVLGVEMEAAA 184
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
7-202 5.89e-27

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 103.64  E-value: 5.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   7 PHICLSPAQVSEQVILCGEPQRVNRIA-ALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEEL-YQCGA 84
Cdd:PRK13374    4 PHINAQPGDFAETVLMPGDPLRAKYIAeTYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELiATFGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  85 RRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPG-YPALASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRD 163
Cdd:PRK13374   84 KNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHdFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFYDP 163

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1098556778 164 DElEICRHWHRLGVLGADMETAALLTLGRLRGLEVAAVL 202
Cdd:PRK13374  164 DE-DAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAIL 201
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 8-112 8.70e-24

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: 96.39  E-value: 8.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778   8 HICLSPAQVSEQVILCGEPQRVNRIAALLDDGRLLAENREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELY------- 80
Cdd:cd00436    12 HLHLKPEDLADTIILVGDPGRVPKVSKHFDSIEFKKQNREFVTHTGTYKGKRITVISTGIGTDNIDIVLNELDalvnidf 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1098556778  81 -------QCGARRVIRVGSAGALQPQIALGELILAEAAV 112
Cdd:cd00436    92 ktrtpkeEKTSLNIIRLGTSGALQPDIPVGSLVISSYAI 130
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 32-186 4.30e-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: 71.87  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  32 IAALLDdgrlLAENREFRSMGG--FYQGVA----VTVCSTGIGAPSAIIALEELYQ-CGARRVIRVGSAGALQPQIALGE 104
Cdd:COG0775    13 VAALLE----ALEDKKEVQIAGftFYLGTLggkeVVLVNSGIGKVNAATATTLLIArFRPDAVINTGVAGGLDPDLKIGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778 105 LILAEAAVRDDG-----GSGCYAPPGYPAL--ASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDEL--EICRHWhrL 175
Cdd:COG0775    89 VVLATEVVQHDVdvtafGYPRGQVPGMPALfeADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEkrRLRERF--P 166

                         170
                  ....*....|.
gi 1098556778 176 GVLGADMETAA 186
Cdd:COG0775   167 GALAVDMEGAA 177
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 12-185 1.99e-12

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: 64.50  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  12 SPAQVSEQVILCGEPQRVNRIAALlDDGRLLAENREFRSMGGFYQGVavTVCSTGIGAPSAIIALEELYQCGARRVIRVG 91
Cdd:cd17762    16 PLEDFQRYILLTNFDMYVDEFAER-TGVPIRGGSVQMPAAHLKKEGI--TIINFGVGSPNAATITDLLAVLRPKAVLMLG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  92 SAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMAAYLQRRDCRFHSGIVRSHDsfYR----DDELe 167
Cdd:cd17762    93 HCGGLRNSQEIGDFVLPIAAIRGEGTSDDYLPPEVPALPSFELQRALSDALREVGLDYRTGTVYTTD--RRnwefDEAF- 169

                         170       180
                  ....*....|....*....|.
gi 1098556778 168 icrhWHRLG---VLGADMETA 185
Cdd:cd17762   170 ----KEYLResrAIAIDMESA 186
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 20-161 2.72e-12

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: 64.52  E-value: 2.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  20 VILCGEPQRVNRIAALLDDGRLLAE---NREFRSMGGFYQGVAVTVCSTGIGAPSAIIALEELYQC--GARRVIRVGSAG 94
Cdd:cd17769     3 IITVGDPARARLIAKLLDKEPKVFEltsERGFLTITGRYKGVPVSIVAIGMGAPMMDFFVREARAVvdGPMAIIRLGSCG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  95 ALQPQIALGELILAEAAV---------RDDGGSGCYAPPgY----PALASRQLINAMAAYLQR--RDCRFHSGIVRSHDS 159
Cdd:cd17769    83 SLDPDVPVGSVVVPSASVavtrnydddDFAGPSTSSEKP-YliskPVPADPELSELLESELKAslGGEVVVEGLNASADS 161


                  ..
gi 1098556778 160 FY 161
Cdd:cd17769   162 FY 163
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 21-186 2.97e-11

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: 60.77  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  21 ILCGEPQRVNRIAALLDDGRLLAENReFRSMGGFYQGVAVTVCSTGIGAPSAIIALEEL-YQCGARRVIRVGSAGALQPQ 99
Cdd:cd17877     3 IIAAMPEEISPLLRRIEVLQKVRLGG-FRFYRGTLGGHPVVLVESGMGKANAARAAQLLlEHFQPDLIISTGFAGGLDPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778 100 IALGELILAEAAVRDDGGSGcyappgyPALASRQLINAMAAYL-QRRDCRFHSGIVRSHDSFYR--DDELEICrhwHRLG 176
Cdd:cd17877    82 LAVGDLVIADRVLYHDGDVP-------AGLEADEKLVALAEELaAGLNLKVHRGTIITVDAIVRksAEKAALA---ARFP 151

                         170
                  ....*....|
gi 1098556778 177 VLGADMETAA 186
Cdd:cd17877   152 ALAVDMESAA 161
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 45-186 5.51e-10

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: 57.51  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  45 NREFRSmgGFYQGVAVTVCSTGIG-APSAIIALEELYQCGARRVIRVGSAGALQPQIALGELILAEAAV---------RD 114
Cdd:cd09008    28 GRTFYE--GTLGGKEVVLVQSGIGkVNAAIATQLLIDRFKPDAIINTGVAGGLDPDLKIGDVVIATKVVyhdvdatafGY 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098556778 115 DGGSGCYAPPGYPalASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRDDELeicRHW--HRLGVLGADMETAA 186
Cdd:cd09008   106 EGGQPPGMPAYFP--ADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEK---KEElrENFPALAVEMEGAA 174
PRK07115 PRK07115
AMP nucleosidase; Provisional
 60-185 1.05e-09

AMP nucleosidase; Provisional


Pssm-ID: 235940  Cd Length: 258  Bit Score: 57.28  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  60 VTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQIALGELILAEAAVRDDGGSGCYAPPGYPALASRQLINAMA 139
Cdd:PRK07115   62 ITIINFGMGSPNAATIMDLLSALNPKAVLFLGKCGGLKSKYQVGDYFLPIAAIRGEGTSDDYFPPEVPALPNFVLQKAVS 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098556778 140 AYLQRRDCRFHSGIVRS-------HDSFYRddeleicRHWHRLGVLGADMETA 185
Cdd:PRK07115  142 SIIRDKGLDYWTGTVYTtnrrfweHDKEFK-------EYLYETRAQAIDMETA 187
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 60-186 1.25e-07

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: 50.23  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  60 VTVCSTGIGAPSAIIALEELYQCGARRVIRVGSAGALQPQIALGELILAEaAVRDDGGSgcyaPPGYPALaSRQLINAMA 139
Cdd:cd17768    23 LLVILSGAGPERARRAAERLLAAGARALISFGVAGGLDPALKPGDLVLPE-AVVADGER----YPTDPAW-RRRLLRALP 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1098556778 140 AYLqrrdcRFHSGIVRSHDsfyrddelEIC------RHWHRL-GVLGADMETAA 186
Cdd:cd17768    97 AGL-----RVVAGPLAGSD--------APVlsvadkAALHAAtGAVAVDMESGA 137
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
45-186 4.20e-07

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 49.35  E-value: 4.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098556778  45 NREFRSmgGFYQGVAVTVCSTGIG----APSAIIALEElyqCGARRVIRVGSAGALQPQIALGELILAEAAVRDD----- 115
Cdd:PRK05584   30 GREFYT--GTLHGHEVVLVLSGIGkvaaALTATILIEH---FKVDAVINTGVAGGLAPGLKVGDVVVADELVQHDvdvta 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1098556778 116 -GgsgcYAP---PGYPAL--ASRQLINAMAAYLQRRDCRFHSGIVRSHDSFYRD-DELEICRHwHRLGVLGADMETAA 186
Cdd:PRK05584  105 fG----YPYgqvPGLPAAfkADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGaEKVAAIRA-EFPDALAVEMEGAA 177
 
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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