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Conserved domains on  [gi|226192663|pdb|3EUE|A]
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Chain A, Uridine phosphorylase 1

Protein Classification

uridine phosphorylase( domain architecture ID 13027119)

uridine phosphorylase catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 49-323 0e+00

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: 512.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       49 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 127
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      128 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 207
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      208 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 287
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                       250       260       270
                ....*....|....*....|....*....|....*.
3EUE_A      288 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 323
Cdd:cd17763 241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 49-323 0e+00

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: 512.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       49 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 127
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      128 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 207
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      208 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 287
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                       250       260       270
                ....*....|....*....|....*....|....*.
3EUE_A      288 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 323
Cdd:cd17763 241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 41-327 0e+00

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: 504.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A         41 NPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCpGRDYPNICAGTDRYAMYKVGP 120
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC-GRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        121 VLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDL 200
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        201 NKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSAC 279
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
3EUE_A        280 GLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSK 327
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 116-304 1.88e-28

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 110.26  E-value: 1.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      116 YKVGPVLSVSHGMGIPSISIMLHELikllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKA 183
Cdd:COG2820  60 YKGKRITVISTGIGGPSAAIAVEEL------AALGAKTFIRVGTSGALqpDIPVGDLVIATGAVrldgtsnfyaPAEYPA 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      184 EFEqivlgkrvirkTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVR 263
Cdd:COG2820 134 VAD-----------FELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVL 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EUE_A      264 NIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRN 304
Cdd:COG2820 193 NVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 72-322 6.37e-24

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: 97.80  E-value: 6.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A         72 KFVCVGGSPSRMKAFIRCVGAELGldcpgrdYPNICAGTDRYA-MYKVGPVLSVSHGMGIPSISIML-HELIKLLyyarc 149
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETP-------VGPPSRGGKFYTgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEF----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        150 sNV-TIIRIGTSGGI--GLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGN 224
Cdd:pfam01048  69 -GVdAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        225 TMCTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QI 299
Cdd:pfam01048 147 YATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTH 210

                         250       260
                  ....*....|....*....|...
3EUE_A        300 SSPRNVLSEYQQRPQRLVSYFIK 322
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
PRK11178 PRK11178
uridine phosphorylase; Provisional
 120-293 6.90e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.60  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       120 PVLSVSHGMGIPSISIMLHELIKLlyyarcsNV-TIIRIGTSGGI--GLEPGTVVITEQAVdTCFKAEFEQIVLGKRVIR 196
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQL-------GVrTFLRIGTTGAIqpHINVGDVLVTTASV-RLDGASLHFAPLEFPAVA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       197 KTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMC 276
Cdd:PRK11178 131 DFECTTALVE-----AAKSIGATTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMC 204

                        170
                 ....*....|....*..
3EUE_A       277 SACGLQAAVVCVTLLNR 293
Cdd:PRK11178 205 ASQGLRAGMVAGVIVNR 221
 
Name Accession Description Interval E-value
UP_hUPP-like cd17763
uridine phosphorylases similar to a human UPP1 and UPP2; Uridine phosphorylase (UP) catalyzes ...
 49-323 0e+00

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: 512.46  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       49 EDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCP-GRDYPNICAGTDRYAMYKVGPVLSVSHG 127
Cdd:cd17763   1 VDFLYHLGLDTSSHDLKKMFGDVKFVCMGGSPGRMENFAEYLAKELGIKLPaGAALVNLSKTTDRYSMYKVGPVLSVSHG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      128 MGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQE 207
Cdd:cd17763  81 MGIPSLSILLHELIKLLHYAGCKDVTFIRIGTSGGIGVEPGTVVITTEAVDGELEPFYEQVILGKVVKRPAVLDAQLAEE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      208 LLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVC 287
Cdd:cd17763 161 LLECAKELDDFPTVIGKTMCANDFYEGQGRLDGAFCDYTEEDKMAFLQKLYDAGVRNIEMESLCFAAFCHRAGIKAAVVC 240

                       250       260       270
                ....*....|....*....|....*....|....*.
3EUE_A      288 VTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKK 323
Cdd:cd17763 241 VTLLNRLEGDQITSSKETLEEWQQRPQRLVSRYIKK 276
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
 41-327 0e+00

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: 504.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A         41 NPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCpGRDYPNICAGTDRYAMYKVGP 120
Cdd:TIGR01719   1 NPNLDKMKEDILYHFGINTSTHDFPAVFGDVKFVCMGGTPSRMKAFARYVGAELGLSC-GRDYPNISERGDRFAMYKVGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        121 VLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDL 200
Cdd:TIGR01719  80 VLCVSHGMGIPSISIMLHELIKLLYYARCKNPTFIRIGTSGGIGVPPGTVVVSSEAVDACLKPEYEQIVLGKRVIRPTQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        201 NKKLVQELLLCSAE-LSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSAC 279
Cdd:TIGR01719 160 DEALVQELLLCGAEgLDEFTTVSGNTMCTDDFYEGQGRLDGAFCEYTEKDKMAYLRKLYALGVRNIEMESSMFAAMTSRA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
3EUE_A        280 GLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSK 327
Cdd:TIGR01719 240 GFKAAVVCVTLLNRLEGDQITITRDQLHEFEQRPQRLVSRYIKKKLSK 287
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 73-320 9.42e-47

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: 157.45  E-value: 9.42e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       73 FVCVGGSPSRMKAFircvgaelglDCPGRDYPNICAGtDRYAMYKVG----PVLSVSHGMGIPSISIMLHELIKLLyyar 148
Cdd:cd09005   1 YAIIPGDPERVDVI----------DSKLENPQKVSSF-RGYTMYTGKyngkRVTVVNGGMGSPSAAIVVEELCALG---- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      149 csNVTIIRIGTSGGIGLE--PGTVVITEQAVDTCFKAEFEqivlGKRVIRKTDLNKKLVQELLLCSAELsEFTTVVGNTM 226
Cdd:cd09005  66 --VDTIIRVGSCGALREDikVGDLVIADGAIRGDGVTPYY----VVGPPFAPEADPELTAALEEAAKEL-GLTVHVGTVW 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      227 CTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDqISSPRNVL 306
Cdd:cd09005 139 TTDAFYRET---------------REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGE-IGFVDEFL 202

                       250
                ....*....|....
3EUE_A      307 SEYQQRPQRLVSYF 320
Cdd:cd09005 203 SEAEKKAIEIALDA 216
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 116-304 1.88e-28

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 110.26  E-value: 1.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      116 YKVGPVLSVSHGMGIPSISIMLHELikllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKA 183
Cdd:COG2820  60 YKGKRITVISTGIGGPSAAIAVEEL------AALGAKTFIRVGTSGALqpDIPVGDLVIATGAVrldgtsnfyaPAEYPA 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      184 EFEqivlgkrvirkTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgalcsYTEKDKQAYLEAAYAAGVR 263
Cdd:COG2820 134 VAD-----------FELTRALVE-----AAEELGVDYHVGITASTDGFYAEQGREL-----RVDPDLDEKLEAWRKLGVL 192

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3EUE_A      264 NIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRN 304
Cdd:COG2820 193 NVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE 233
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 72-322 6.37e-24

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: 97.80  E-value: 6.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A         72 KFVCVGGSPSRMKAFIRCVGAELGldcpgrdYPNICAGTDRYA-MYKVGPVLSVSHGMGIPSISIML-HELIKLLyyarc 149
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETP-------VGPPSRGGKFYTgTLGGVPVVLVRHGIGPPNAAILAaIRLLKEF----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        150 sNV-TIIRIGTSGGI--GLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTD--LNKKLVQELLLCSAELsEFTTVVGN 224
Cdd:pfam01048  69 -GVdAIIRTGTAGGLnpDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPapADPELRALAKEAAERL-GIPVHRGV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A        225 TMCTLDFYEGQgrldgalcsytekdkQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVtLLNRLEGD-----QI 299
Cdd:pfam01048 147 YATGDGFYFET---------------PAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRV-VSDLAAGGadgelTH 210

                         250       260
                  ....*....|....*....|...
3EUE_A        300 SSPRNVLSEYQQRPQRLVSYFIK 322
Cdd:pfam01048 211 EEVEEFAERAAERAAALLLALLA 233
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 120-299 6.80e-22

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: 92.51  E-value: 6.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      120 PVLSVSHGMGIPSISIMLHELIkllyyaRCSNVTIIRIGTSGGI--GLEPGTVVITEQAV----------DTCFKAefeq 187
Cdd:cd17767  53 PVSVCSTGIGGPSAAIAVEELA------QLGAKTFIRVGTCGALqpDIKLGDLVIATGAVrdegtskhyvPPEYPA---- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      188 ivlgkrvIRKTDLNKKLVQelllcSAELSEFTTVVGnTMCTLD-FYEGQGRLDgalcSYTEKDKQAYLEAAYAAGVRNIE 266
Cdd:cd17767 123 -------VADPEVVLALVE-----AAEELGVPYHVG-ITASKDsFYGGQGRPG----PGLPPELPELLEEWQRAGVLNSE 185

                       170       180       190
                ....*....|....*....|....*....|...
3EUE_A      267 MESSVFAAMCSACGLQAAVVCVTLLNRLEGDQI 299
Cdd:cd17767 186 MESAALFTLASLRGVRAGAVLAVVGNRVTDEAP 218
UP_TbUP-like cd00436
uridine phosphorylases similar to Trypanosoma brucei UP; Uridine phosphorylase (UP) catalyzes ...
 124-296 5.70e-17

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: 79.44  E-value: 5.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      124 VSHGMGIPSISIMLHEL------------IKllyyARCSNVTIIRIGTSGGI--GLEPGTVVITEQAV--DTC-----FK 182
Cdd:cd00436  67 ISTGIGTDNIDIVLNELdalvnidfktrtPK----EEKTSLNIIRLGTSGALqpDIPVGSLVISSYAIglDNLlnfydHP 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      183 AEFEQIVLGKRVIRKTDLNKKLVQ--------ELLlcsAELSEFTTVVGNTMCTLDFYEGQGR----------LDGALCS 244
Cdd:cd00436 143 NTDEEAELENAFIAHTSWFKGKPRpyvvkaspELL---DALTGVGYVVGITATAPGFYGPQGRqlrlpladpdLLDKLSS 219

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
3EUE_A      245 YTEKDKQayleaayaagVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEG 296
Cdd:cd00436 220 FSYGGLR----------ITNFEMETSAIYGLSRLLGHRALSICAIIANRATG 261
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 115-287 1.30e-12

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: 66.27  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      115 MYKVGPVlSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGIG--LEPGTVVITEQA-------------V 177
Cdd:cd09006  48 TYKGKRV-SVmGSGMGMPSIGIYAYELFK--FY----GVkNIIRIGTCGAYQpdLKLRDVVLAMGAstdsnynrlrfggG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      178 DTCFKAEFEqivlgkrvirktdLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEgqgrldgalcsytekDKQAYLEAA 257
Cdd:cd09006 121 DFAPIADFE-------------LLRKAVE-----TAKELGIPVHVGNVFSSDVFYD---------------DDPELWKKL 167

                       170       180       190
                ....*....|....*....|....*....|
3EUE_A      258 YAAGVRNIEMESSVFAAMCSACGLQAAVVC 287
Cdd:cd09006 168 KKYGVLAVEMEAAALYTNAARLGKKALAIL 197
PRK11178 PRK11178
uridine phosphorylase; Provisional
 120-293 6.90e-11

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 61.60  E-value: 6.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       120 PVLSVSHGMGIPSISIMLHELIKLlyyarcsNV-TIIRIGTSGGI--GLEPGTVVITEQAVdTCFKAEFEQIVLGKRVIR 196
Cdd:PRK11178  59 PVIVCSTGIGGPSTSIAVEELAQL-------GVrTFLRIGTTGAIqpHINVGDVLVTTASV-RLDGASLHFAPLEFPAVA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A       197 KTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDgALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMC 276
Cdd:PRK11178 131 DFECTTALVE-----AAKSIGATTHVGVTASSDTFYPGQERYD-TYSGRVVRRFKGSMEEWQAMGVMNYEMESATLLTMC 204

                        170
                 ....*....|....*..
3EUE_A       277 SACGLQAAVVCVTLLNR 293
Cdd:PRK11178 205 ASQGLRAGMVAGVIVNR 221
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 116-287 1.72e-10

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: 60.13  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      116 YKVGPVlSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGI--GLEPGTVVI-----TEQAVDtcfkaefE 186
Cdd:COG0813  53 YKGKRV-SVmGSGMGIPSISIYAYELIT--EY----GVkNIIRVGTCGALqeDVKVRDVVIamgasTDSNVN-------R 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      187 QIVLGKRVIRKTD--LNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEgqgrldgalcsyTEKDKQAYLeAAYaaGVRN 264
Cdd:COG0813 119 QRFGGGDFAPIADfeLLRKAVE-----AAKELGIKVHVGNVFSSDLFYR------------EDPDLLEKL-AKY--GVLA 178

                       170       180
                ....*....|....*....|...
3EUE_A      265 IEMESSVFAAMCSACGLQAAVVC 287
Cdd:COG0813 179 VEMEAAALYTLAAKYGKRALAIL 201
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 116-308 2.32e-08

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: 53.85  E-value: 2.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      116 YKVGPVlSV-SHGMGIPSISIMLHELIKLLyyARcsnvTIIRIGTSGGI--GLEPGTVVITEQAV--DTCFKAEFEQIvl 190
Cdd:cd17765  52 YKGKPV-SVqTTGMGCPSAAIVVEELAQLG--VK----RLIRVGTCGGLssGLQLGDLIVATAAVpaDGTTRALLGGE-- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      191 GKRVIRKTDLNKKLVQelllcSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYtekdkqayleaayaaGVRNIEMESS 270
Cdd:cd17765 123 PYAPAADFELVEALYR-----AARAAGMPVHVGPVATSDLFYDPTPDGVKRWRRR---------------GVLAVEMEAS 182

                       170       180       190
                ....*....|....*....|....*....|....*...
3EUE_A      271 VFAAMCSACGLQAAVVCvTLLNRLEGDQISSPRNVLSE 308
Cdd:cd17765 183 ALFTLAALRGLRAGCIL-TVSDLIGDPERRIDDEELRA 219
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
115-163 8.69e-08

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 52.17  E-value: 8.69e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
3EUE_A       115 MYKvGPVLSV-SHGMGIPSISIMLHELIKllYYarcsNV-TIIRIGTSGGI 163
Cdd:PRK05819  51 TYK-GKRVSVmGTGMGIPSISIYANELIT--DY----GVkKLIRVGSCGAL 94
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 116-176 9.62e-08

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: 51.84  E-value: 9.62e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3EUE_A      116 YKVGPVLSVSHGMGIPSISIMLHELIKLlyYARcsnvTIIRIGTSGGI--GLEPGTVVITEQA 176
Cdd:cd17764  38 YKGEEVTIATHGIGGPSAAIVFEELIML--GAK----VIIRLGTAGGLvpELRVGDIVVATGA 94
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 115-300 2.87e-06

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: 47.96  E-value: 2.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      115 MYKVGPVLSVSHGMGIPSISIMLHElikllyyarCSNVT-----IIRIGTSGGIG--LEPGTVVITEQAV-------DTC 180
Cdd:cd17769  40 RYKGVPVSIVAIGMGAPMMDFFVRE---------ARAVVdgpmaIIRLGSCGSLDpdVPVGSVVVPSASVavtrnydDDD 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EUE_A      181 FKAEFEQIV----LGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGnTMCTldFYEGQGRLDGalcSYTEKDKQ--AYL 254
Cdd:cd17769 111 FAGPSTSSEkpylISKPVPADPELSELLESELKASLGGEVVVEGLNA-SADS--FYSSQGRQDP---NFPDHNENliDKL 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
3EUE_A      255 EAAYaAGVRNIEMESSVF---AAMCSACG--LQAAVVCVTLLNRLEGDQIS 300
Cdd:cd17769 185 LKRY-PGAASLEMETFHLfhlARCSRPAQgkIRAAAAHMVFANRTSNDFIS 234
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
116-163 1.04e-04

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 42.78  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
3EUE_A       116 YKvGPVLSV-SHGMGIPSISIMLHELIKLLYYARcsnvtIIRIGTSGGI 163
Cdd:PRK13374  53 YK-GKKVSVmGHGMGIPSMVIYVHELIATFGVKN-----IIRVGSCGAT 95
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 116-163 2.21e-04

purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called inosine phosphorylase) is a purine salvage enzyme. Purine nucleosides, such as guanosine, inosine, or xanthosine, plus orthophosphate, can be converted to their respective purine bases (guanine, hypoxanthine, or xanthine) plus ribose-1-phosphate. This family of purine nucleoside phosphorylase is restricted to the bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 188024  Cd Length: 232  Bit Score: 42.07  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
3EUE_A        116 YKVGPVLSVSHGMGIPSISIMLHELIKlLYYARcsnvTIIRIGTSGGI 163
Cdd:TIGR00107  49 YKGKKISVMGHGMGIPSISIYVYELIK-FYEVK----TIIRVGSCGAI 91
 
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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