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Conserved domains on  [gi|674708283|ref|WP_031600735|]
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MULTISPECIES: 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [Bacillus]

Protein Classification

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase( domain architecture ID 10019819)

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose or ribosylhomocysteine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-230 1.30e-146

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


:

Pssm-ID: 130765  Cd Length: 228  Bit Score: 407.95  E-value: 1.30e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283    2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   82 HTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELDGiQVAKGTIATGDSFMNDPKRVEE 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNL-NAVRGLIVSGDAFINGSVGLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674708283  162 VRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:TIGR01704 160 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
 
Name Accession Description Interval E-value
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-230 1.30e-146

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130765  Cd Length: 228  Bit Score: 407.95  E-value: 1.30e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283    2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   82 HTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELDGiQVAKGTIATGDSFMNDPKRVEE 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNL-NAVRGLIVSGDAFINGSVGLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674708283  162 VRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:TIGR01704 160 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-231 1.91e-117

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 334.01  E-value: 1.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   1 MRLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGF 80
Cdd:PRK05584   1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  81 HHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVE 160
Cdd:PRK05584  81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKEL-NLNVHRGLIASGDQFIAGAEKVA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674708283 161 EVRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRIH 231
Cdd:PRK05584 160 AIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-230 1.71e-97

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: 283.73  E-value: 1.71e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   1 MRLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGF 80
Cdd:COG0775    1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  81 HHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSElDGIQVAKGTIATGDSFMNDPKRVE 160
Cdd:COG0775   81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKE-SGLKVVTGTIATGDRFVWSAEEKR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283 161 EVRARFSD----------LYavemeaaavaQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:COG0775  160 RLRERFPGalavdmegaaIA----------QVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-226 2.18e-94

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: 275.53  E-value: 2.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   3 LAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHH 82
Cdd:cd09008    1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  83 TLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEV 162
Cdd:cd09008   81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKEL-GPKVHTGLIASGDQFVASSEKKEEL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674708283 163 RARFSdlyavemeaaaVA----------QVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKV 226
Cdd:cd09008  160 RENFP-----------ALavemegaaiaQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-228 1.40e-46

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: 154.04  E-value: 1.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283    2 RLAVIGAMEEEVTILRDKLENAKTE--TIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTL-LLDRYKPDYVINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   79 GFHHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKR 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERL-GIPVHRGVYATGDGFYFETPA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  159 VEEVRARF---------SDLYavemeaaavaQVCHQFKTPFVVIRALSDIA-----GKESHVSFDQFLEQAAVHSTELVL 224
Cdd:pfam01048 160 EIRLLRRLgadavemetAAEA----------QVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLL 229


                  ....
gi 674708283  225 KVIK 228
Cdd:pfam01048 230 ALLA 233
 
Name Accession Description Interval E-value
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-230 1.30e-146

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria. This enzyme is widely distributed in bacteria, especially those that lack adenosylhomocysteinase (EC 3.3.1.1). One clade of bacteria including Agrobacterium, Mesorhizobium, Sinorhizobium and Brucella includes sequences annotated as MTA/SAH nucleotidase, but differs significantly in homology and has no independent experimental evidence. There are homologs of this enzyme in plants, some of which score between trusted and noise cutoffs here, but there is no experimental evidence to validate this function at this time. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130765  Cd Length: 228  Bit Score: 407.95  E-value: 1.30e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283    2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   82 HTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELDGiQVAKGTIATGDSFMNDPKRVEE 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNL-NAVRGLIVSGDAFINGSVGLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674708283  162 VRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:TIGR01704 160 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-231 1.91e-117

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 334.01  E-value: 1.91e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   1 MRLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGF 80
Cdd:PRK05584   1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  81 HHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVE 160
Cdd:PRK05584  81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKEL-NLNVHRGLIASGDQFIAGAEKVA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674708283 161 EVRARFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRIH 231
Cdd:PRK05584 160 AIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-230 1.71e-97

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: 283.73  E-value: 1.71e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   1 MRLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGF 80
Cdd:COG0775    1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  81 HHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSElDGIQVAKGTIATGDSFMNDPKRVE 160
Cdd:COG0775   81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKE-SGLKVVTGTIATGDRFVWSAEEKR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283 161 EVRARFSD----------LYavemeaaavaQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:COG0775  160 RLRERFPGalavdmegaaIA----------QVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-226 2.18e-94

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: 275.53  E-value: 2.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   3 LAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHH 82
Cdd:cd09008    1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  83 TLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEV 162
Cdd:cd09008   81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKEL-GPKVHTGLIASGDQFVASSEKKEEL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674708283 163 RARFSdlyavemeaaaVA----------QVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKV 226
Cdd:cd09008  160 RENFP-----------ALavemegaaiaQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-226 6.38e-51

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: 164.39  E-value: 6.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   3 LAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHH 82
Cdd:cd17877    1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  83 TLNVGDVVISTDVRHHDVDVtafdyeygqvpglPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEV 162
Cdd:cd17877   81 GLAVGDLVIADRVLYHDGDV-------------PAGLEADEKLVALAEELAAGL-NLKVHRGTIITVDAIVRKSAEKAAL 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674708283 163 RARFSDLyAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFL-EQAAVHSTELVLKV 226
Cdd:cd17877  147 AARFPAL-AVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFLdEEGAVRPGAVLLTL 210
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-228 1.40e-46

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: 154.04  E-value: 1.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283    2 RLAVIGAMEEEVTILRDKLENAKTE--TIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTL-LLDRYKPDYVINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   79 GFHHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKR 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERL-GIPVHRGVYATGDGFYFETPA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  159 VEEVRARF---------SDLYavemeaaavaQVCHQFKTPFVVIRALSDIA-----GKESHVSFDQFLEQAAVHSTELVL 224
Cdd:pfam01048 160 EIRLLRRLgadavemetAAEA----------QVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLL 229


                  ....
gi 674708283  225 KVIK 228
Cdd:pfam01048 230 ALLA 233
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 2-230 8.13e-46

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 152.09  E-value: 8.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:PRK14697   3 RIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  82 HTLNVGDVVISTDVRHHDVDVTafdyEYGQVPGLPAAYAADEKLISITEEAV-SELDGIQVAKGTIATGDSFMNDPKrve 160
Cdd:PRK14697  83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACnSSSLHIEIHEGRIVSGECFVEDSK--- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674708283 161 eVRARFSDLYAVEMEAAAVAQVCHQF---KTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:PRK14697 156 -LKAKLIDEYAPHCTEMEGAAIGHVAyinEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKNI 227
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 2-230 2.87e-38

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 138.22  E-value: 2.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:PRK06698   3 RIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  82 HTLNVGDVVISTDVRHHDVDVTAFDYEYgqvpGLPAAYAADEKLISITEEAV-SELDGIQVAKGTIATGDSFMNDPKrve 160
Cdd:PRK06698  83 PDVKVGDIVISTNVTHHDVSKTQMKNLF----PFQEEFIASKELVELARKACnSSSLHMEIHEGRIVSGECFVEDSK--- 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674708283 161 eVRARFSDLYAVEMEAAAVAQVCHQF---KTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIKRI 230
Cdd:PRK06698 156 -LKAKLIDEYAPHCTEMEGAAIGHVAyinEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKTI 227
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 3-224 2.83e-29

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: 108.92  E-value: 2.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   3 LAVIGAMEEEVTILRDKLENAKTETIAH-CEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDrYKPDYVINTGSAGGFH 81
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRgYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCA-LGVDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  82 HTLNVGDVVISTDVRHHDVDVTAFdyeygqVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDpkRVEE 161
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYY------VVGPPFAPEADPELTAALEEAAKEL-GLTVHVGTVWTTDAFYRE--TREE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674708283 162 VRARFSDLYAVEM-EAAAVAQVCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVL 224
Cdd:cd09005  151 SEKLRKLGALAVEmETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIAL 214
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 2-201 8.68e-21

futalosine nucleosidase which catalyzes the hydrolysis of futalosine to dehypoxanthinylfutalosine and a hypoxanthine base; similar to Thermus thermophiles MqnB; Futalosine nucleosidase (MqnB, EC 3.2.2.26, also known as futalosine hydrolase) functions in an alternative menaquinone biosynthetic pathway (the futalosine pathway) which operates in some bacteria, including Streptomyces coelicolor and Thermus thermophiles. This domain model 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), homohexomeric (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: 350166  Cd Length: 217  Bit Score: 86.82  E-value: 8.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   2 RLAVIGAMEEEvtilrdklENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:cd17766    1 MILIVTAVPLE--------TNLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  82 HT-LNVGDVVISTDVRH-----------HDVDVTAFdyeyGQVPglpaaYAADEKLISITEEAVSELDGIQVAKGTI--- 146
Cdd:cd17766   73 GSgLSVGDLVVASEEIAadlgvetpegfLSLDELGF----GLLR-----IGTDPYLNRFPLSALLLAAGLQVKTGPFltv 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674708283 147 --ATGDSfmndpKRVEEVRARFSDL------YavemeaaAVAQVCHQFKTPFVVIRALSDIAG 201
Cdd:cd17766  144 stVTGTA-----ERAAELQRRFPAIaenmegA-------AVAHAALLYGVPFLEIRGISNPVG 194
fut_nucase TIGR03664
futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine ...
 36-201 1.21e-14

futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine futalosine in a pathway for the biosynthesis of menaquinone distinct from the pathway observed in E. coli.


Pssm-ID: 274710  Cd Length: 222  Bit Score: 70.41  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   36 GEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVISTDV-----------RHHDVDVTA 104
Cdd:TIGR03664  24 GSVGGAGFDVLVTGVGPVNAAAATARLLARAPYELVINAGIAGGFPGKAAVGDLVVADSEiaadlgaetpeGFLPLEALG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  105 FDYEYGQVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEVRARFsDLYAVEMEAAAVAQVCH 184
Cdd:TIGR03664 104 FPQLPGGGRSYFNRIPLDPDLVERAVQLARAL-GLPVARGPFLTVSTVSGTAARAEALARRF-GAVAENMEGAAVALAAL 181

                         170
                  ....*....|....*..
gi 674708283  185 QFKTPFVVIRALSDIAG 201
Cdd:TIGR03664 182 RYGVPFLELRGISNLVG 198
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 2-228 1.47e-13

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 67.64  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   2 RLAVIGAMEEEVTILRDKLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFH 81
Cdd:PRK06714   3 RIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  82 HTLNVGDVVISTDVRHHDVDVTafdyeyGQVPGLPAAYAADEKLISITEEAVSELDGIQ----VAKGTIATGDSfmndPK 157
Cdd:PRK06714  83 NKVKNGHIVVALNAIQHDVTAA------GSGEDVFNLYNGRTAPIETTKSLVRRIKKIRsydpIHFGTFLSGDQ----RI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674708283 158 RVEEVRARFSDLYAVEMEAAAVAQ---VCHQFKTPFVVIRALSDIAGKESHVSFDQFLEQAAVHSTELVLKVIK 228
Cdd:PRK06714 153 RSSEMRYLLHTVYGALAVDQEVAAfayVCQINKKPFLCLKAASDQANDKTKEEQKIFKMLACERACEHLIAFLR 226
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 2-231 2.01e-12

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 64.64  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   2 RLAVIGAMEEEVTILRDKL-----ENAKTETIAHCEFTTGEYEGTEVILLKSG---------IGKVNAAISTTLLLDRYK 67
Cdd:PLN02584  10 TVLIVIAMQAEAMPLVNALglvedVDSPFPKGVPWVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQALK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  68 PDYVINTGSAGGFHHT-LNVGDVVISTDVRHHD--VDVTAFDyEYGQvpGLPAAYAadeklisiTEEAVSELDgiqVAKG 144
Cdd:PLN02584  90 PDLIINAGTAGGFKAKgAAIGDVFLATAVANHDrrIPIPVFD-KYGV--GTRDAFP--------TPNLIKALG---LKEG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283 145 TIATGDSFMNDPKRVEEVRArfSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDI--AGKESHVSFDQFLEQAAVHSTEL 222
Cdd:PLN02584 156 VLSTGNSLDMTEQDEESIKA--NDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIvdGDKPTAEEFLENLSAAAAALQGA 233


                 ....*....
gi 674708283 223 VLKVIKRIH 231
Cdd:PLN02584 234 VPKVLDFIS 242
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 1-204 8.31e-12

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 62.49  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283   1 MRLAVIGAMEEEVTILRD-KLENAKTETIAHCEFTTGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGG 79
Cdd:PRK07164   4 KIIAIIYADNNEFVNLENfEFILLKNIESFQKKIAIFRYKNYNILYINTGIGLINAALATQKLIEKYQIEIIINYGAVGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  80 FHHtLNVGDVVISTDVRHHDVdVTAFdYEYGQVPGLPAAYAADeklisITEEAVSELDgiqvakgtIATGDSFMNDPKRV 159
Cdd:PRK07164  84 NIN-IDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYENN-----KINKNFNKIH--------LGSSNSFIFDLDKL 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 674708283 160 EEVRaRFSDLYAVEMEAAAVAQVCHQFKTPFVVIRALSDIAGKES 204
Cdd:PRK07164 148 KIIK-DFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNS 191
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 11-170 6.99e-10

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 57.48  E-value: 6.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  11 EEVTILRDKLENAKTETiAHCEFT--TGEYEGTEVILLKSGIGKVNAAISTTLLlDRYKPDYVINTGSAGGFHHTLNVGD 88
Cdd:COG2820   32 GRVELIASYLDDVELVA-ENREFRtyTGTYKGKRITVISTGIGGPSAAIAVEEL-AALGAKTFIRVGTSGALQPDIPVGD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  89 VVISTD-VRHhdvDVTAFDYeygqvpgLPAAY--AADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEVRAR 165
Cdd:COG2820  110 LVIATGaVRL---DGTSNFY-------APAEYpaVADFELTRALVEAAEEL-GVDYHVGITASTDGFYAEQGRELRVDPD 178


                 ....*
gi 674708283 166 FSDLY 170
Cdd:COG2820  179 LDEKL 183
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 35-166 9.38e-10

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: 56.64  E-value: 9.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  35 TGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVISTDVrhhdvdVTAFDYEYGQVPG 114
Cdd:cd09006   46 TGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVKNIIRIGTCGAYQPDLKLRDVVLAMGA------STDSNYNRLRFGG 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 674708283 115 LPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEVRARF 166
Cdd:cd09006  120 GDFAPIADFELLRKAVETAKEL-GIPVHVGNVFSSDVFYDDDPELWKKLKKY 170
PRK05634 PRK05634
nucleosidase; Provisional
 45-216 9.21e-09

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 53.15  E-value: 9.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  45 LLKSGIGKVNAAISTTLLLDRYK--PDYVINTGSAGGFHHTLNvGDVVISTdVRHHDVDVTAFDyeygQVPGLPAAyaad 122
Cdd:PRK05634  25 LLITGIGKVAAAVALTRALARRGvlPPRVVNIGTAGALRDGLS-GVFEPSH-VINHDFSSDLIR----ALTGHPVA---- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283 123 eklisiteeAVSELDGiqVAKGTIATGDSFMNDPKrVEEVRARFSDLyaVEMEAAAVAQVCHQFKTPFVVIRALSDIAGK 202
Cdd:PRK05634  95 ---------NRLELPT--GDGAVLATGDAFISDTA-TRDRLAQRADL--VDMEGYAVAAVAAEFGVPCRLVKHVSDSADE 160

                        170
                 ....*....|....
gi 674708283 203 ESHVSFDQFLEQAA 216
Cdd:PRK05634 161 SALGSWPEAVDASA 174
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 20-169 5.49e-08

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: 51.68  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  20 LENAktETIAHC-EFTT--GEYEGTEVILLKSGIGKVNAAISTTLLLdRYKPDYVINTGSAGGFHHTLNVGDVVISTD-V 95
Cdd:cd17767   30 LDDA--EEVADNrEYRTytGTYKGVPVSVCSTGIGGPSAAIAVEELA-QLGAKTFIRVGTCGALQPDIKLGDLVIATGaV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  96 RHhdvDVTAFDYeygqVP-GLPAayAADEKLISITEEAVSELdGIQVAKGTIATGDSF--------MNDPKRVEEVRARF 166
Cdd:cd17767  107 RD---EGTSKHY----VPpEYPA--VADPEVVLALVEAAEEL-GVPYHVGITASKDSFyggqgrpgPGLPPELPELLEEW 176


                 ...
gi 674708283 167 SDL 169
Cdd:cd17767  177 QRA 179
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 35-166 4.00e-07

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: 49.34  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  35 TGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVI----STDvrhhdvDVTAFDYeyg 110
Cdd:COG0813   50 TGTYKGKRVSVMGSGMGIPSISIYAYELITEYGVKNIIRVGTCGALQEDVKVRDVVIamgaSTD------SNVNRQR--- 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 674708283 111 qVPGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEVRARF 166
Cdd:COG0813  121 -FGGGDFAPIADFELLRKAVEAAKEL-GIKVHVGNVFSSDLFYREDPDLLEKLAKY 174
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 46-207 4.86e-07

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 48.89  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  46 LKSGIGKVNAAISTTLLLDRYK-----PDYVINTGSAGGfhHTLNVGDVVISTDVRHHDVDVTAFDYEYGQVP--GLPAa 118
Cdd:PRK06026  34 LMTGVGPVEAAVNLTAALARLKaagdlPDLVVSLGSAGS--AKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPflDLPA- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283 119 yaadeklisiTEEAVSELDGIQVAK----GTIATGDSFmndpkrvEEVRARFSDLyavemEAAAVAQVCHQFKTPFVVIR 194
Cdd:PRK06026 111 ----------TVELPLRIPGIPEASlstgGNIVSGAAY-------DAIDADMVDM-----ETYAVLRACQAFGVPLIGLR 168

                        170
                 ....*....|...
gi 674708283 195 ALSDIAGKESHVS 207
Cdd:PRK06026 169 GISDGAAELKHVG 181
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 35-165 9.81e-05

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: 42.21  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  35 TGEYEGTEVILLKSGIGKVNAAISTTLLLdRYKPDYVINTGSAGGFHHTLNVGDVVIstdvrhhdvdVTAFDYEYGQV-- 112
Cdd:cd17764   35 TGKYKGEEVTIATHGIGGPSAAIVFEELI-MLGAKVIIRLGTAGGLVPELRVGDIVV----------ATGASYYPGGGlg 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 674708283 113 ---PGLPAAYAADEKLISITEEAVSELdGIQVAKGTIATGDSF-MNDPKRVEEVRAR 165
Cdd:cd17764  104 qyfPDVCPPASPDPELTLELVESLSKR-GLKYYVGPVFSSDAFyAEDEEFAERWSSL 159
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
35-176 1.09e-03

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 39.07  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  35 TGEYEGTEVILLKSGIGKVNAAISTTLLLDRYKPDYVINTGSAGGFHHTLNVGDVVI----STDVRHHDVDVTAFDYeyg 110
Cdd:PRK05819  49 TGTYKGKRVSVMGTGMGIPSISIYANELITDYGVKKLIRVGSCGALQEDVKVRDVVIamgaSTDSNVNRIRFKGHDF--- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674708283 111 qvpglpaAYAADEKLISITEEAVSELdGIQVAKGTIATGDSFMNDPKRVEEVRARFSDLyAVEMEA 176
Cdd:PRK05819 126 -------APIADFDLLRKAYDAAKEK-GITVHVGNVFSADLFYNPDPEMFDVLEKYGVL-GVEMEA 182
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 71-170 2.84e-03

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: 37.94  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674708283  71 VINTGSAGGFHHTLNVGDVVISTD----VRHHDvdvtaFDYEYGQVPGLPAAY------AADEKLIS-ITEEAVSELDGI 139
Cdd:cd17769   75 IIRLGSCGSLDPDVPVGSVVVPSAsvavTRNYD-----DDDFAGPSTSSEKPYliskpvPADPELSElLESELKASLGGE 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 674708283 140 QVAKGTIATGDSFM-----NDP-------KRVEEVRARFSDLY 170
Cdd:cd17769  150 VVVEGLNASADSFYssqgrQDPnfpdhneNLIDKLLKRYPGAA 192
 
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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