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Conserved domains on  [gi|16128152|ref|NP_414701|]
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase( domain architecture ID 10012466)

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

EC:  3.2.2.9
Gene Ontology:  GO:0008782|GO:0008930|GO:0019509|GO:0019284|GO:0046124
PubMed:  25806409|21166890|11743878

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 7.86e-127

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


:

Pssm-ID: 180148  Cd Length: 230  Bit Score: 357.89  E-value: 7.86e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGL 80
Cdd:PRK05584   1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   81 APTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584  81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  161 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 7.86e-127

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 357.89  E-value: 7.86e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGL 80
Cdd:PRK05584   1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   81 APTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584  81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  161 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-230 8.72e-96

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: 279.49  E-value: 8.72e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGL 80
Cdd:COG0775   1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  81 APTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775  81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152 161 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:COG0775 161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLR 230
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-225 1.69e-91

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: 268.21  E-value: 1.69e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   3 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAP 82
Cdd:cd09008   1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008  81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128152 163 HNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESL 225
Cdd:cd09008 161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-229 4.33e-84

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: 249.64  E-value: 4.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152     2 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    82 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128152   162 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-226 2.71e-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: 153.27  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152     2 KIGIIGAMEEEVTLLRDKIENRQTI--SLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLL-EHCKPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    79 GLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128152   159 AKIRHNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVA-----DQQSHLSFDEFLAVAAKQSSLMVESLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-230 7.86e-127

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 357.89  E-value: 7.86e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGL 80
Cdd:PRK05584   1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   81 APTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:PRK05584  81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  161 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-230 8.72e-96

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: 279.49  E-value: 8.72e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   1 MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGL 80
Cdd:COG0775   1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  81 APTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAK 160
Cdd:COG0775  81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152 161 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:COG0775 161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKLR 230
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-225 1.69e-91

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: 268.21  E-value: 1.69e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   3 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAP 82
Cdd:cd09008   1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  83 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd09008  81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSEKKEELR 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128152 163 HNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESL 225
Cdd:cd09008 161 ENFP-ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-229 4.33e-84

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: 249.64  E-value: 4.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152     2 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    82 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128152   162 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 229
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-211 2.84e-68

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: 208.69  E-value: 2.84e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   3 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAP 82
Cdd:cd17877   1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  83 TLKVGDIVVSDEARYHDADVtafgyeygqlpgcPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIR 162
Cdd:cd17877  81 GLAVGDLVIADRVLYHDGDV-------------PAGLEADEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSAEKAALA 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 16128152 163 HNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFL 211
Cdd:cd17877 148 ARFP-ALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFL 195
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 3-225 5.72e-48

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: 157.07  E-value: 5.72e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   3 IGIIGAMEEEVTLLRDKIENRQTISLG-GCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCkPDVIINTGSAGGLA 81
Cdd:cd09005   1 YAIIPGDPERVDVIDSKLENPQKVSSFrGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALG-VDTIIRVGSCGALR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  82 PTLKVGDIVVSDEARYHDADVTAFGyeygqlPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGS-VGLAK 160
Cdd:cd09005  80 EDIKVGDLVIADGAIRGDGVTPYYV------VGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETrEESEK 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128152 161 IRHNFpqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESL 225
Cdd:cd09005 154 LRKLG--ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIALDA 216
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-226 2.71e-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: 153.27  E-value: 2.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152     2 KIGIIGAMEEEVTLLRDKIENRQTI--SLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLL-EHCKPDVIINTGSAG 78
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVgpPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIRLlKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    79 GLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGL 158
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128152   159 AKIRHNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAISDVA-----DQQSHLSFDEFLAVAAKQSSLMVESLV 226
Cdd:pfam01048 161 IRLLRRLG-ADAVEMETAAEAQVAREAGIPFAAIRVVSDLAaggadGELTHEEVEEFAERAAERAAALLLALL 232
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 2-225 4.75e-37

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 129.75  E-value: 4.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    2 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:PRK14697   3 RIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   82 PTLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADDKLIAAAEACIAELNLN--AVRGLIVSGDAFINGSVGLA 159
Cdd:PRK14697  83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNSSSLHieIHEGRIVSGECFVEDSKLKA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128152  160 KIRHNF-PQaiAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQ-SSLMVESL 225
Cdd:PRK14697 159 KLIDEYaPH--CTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYcSEIIVEML 224
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 2-230 9.16e-33

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 123.20  E-value: 9.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    2 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:PRK06698   3 RIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   82 PTLKVGDIVVSDEARYHDADVTafgyEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAV--RGLIVSGDAFINGSVGLA 159
Cdd:PRK06698  83 PDVKVGDIVISTNVTHHDVSKT----QMKNLFPFQEEFIASKELVELARKACNSSSLHMEihEGRIVSGECFVEDSKLKA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128152  160 KIRHNFpQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLA 230
Cdd:PRK06698 159 KLIDEY-APHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKTIS 228
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 2-196 1.60e-17

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: 77.96  E-value: 1.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   2 KIGIIGAMEEEvtllrdkiENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:cd17766   1 MILIVTAVPLE--------TNLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  82 PT-LKVGDIVVSDEARYHD---------ADVTAFGYEYGQLPGCPAGFKAddkliaAAEACIAELNLNAVRGLIVSGDAf 151
Cdd:cd17766  73 GSgLSVGDLVVASEEIAADlgvetpegfLSLDELGFGLLRIGTDPYLNRF------PLSALLLAAGLQVKTGPFLTVST- 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16128152 152 INGSVGLAK-IRHNFPqAIAVEMEATAIAHVCHNFNVPFVVVRAIS 196
Cdd:cd17766 146 VTGTAERAAeLQRRFP-AIAENMEGAAVAHAALLYGVPFLEIRGIS 190
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 2-203 2.84e-15

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 72.26  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    2 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 81
Cdd:PRK06714   3 RIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   82 PTLKVGDIVVSDEARYHdaDVTAFGY---EYGQLPGCPAGFKADDKLIAAAEACIAELNLNavRGLIVSGDAFINGSVgL 158
Cdd:PRK06714  83 NKVKNGHIVVALNAIQH--DVTAAGSgedVFNLYNGRTAPIETTKSLVRRIKKIRSYDPIH--FGTFLSGDQRIRSSE-M 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 16128152  159 AKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQS 203
Cdd:PRK06714 158 RYLLHTVYGALAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKT 202
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 69-201 1.57e-14

hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 family of phosphorylases typically acting on nucleotide-sugar substrates. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of hopene, the cyclization product of the polyisoprenoid squalene. This gene is adjacent to the genes PhnA-E and squalene-hopene cyclase (which would be HpnF) in Zymomonas mobilis and their association with hopene biosynthesis has been noted in the literature. Extending the gene symbol sequence, we suggest the symbol HpnG for the product of this gene. Hopanoids are known to be components of the plasma membrane and to have polar sugar head groups in Z. mobilis and other species.


Pssm-ID: 274594  Cd Length: 212  Bit Score: 69.67  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    69 DVIINTGSAGGLAPTLKVGDIVVSDEARYHD----ADVTAFGYEYGQLPGCPagfkaddkliaaaeaciaelnlNAVRGL 144
Cdd:TIGR03468  47 AGLVSFGTAGALDPALQPGDLVVPEEVRADGdrfpTDPAWRRRLLEALPAGL----------------------RVHRGV 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128152   145 IVSGDAfINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQ 201
Cdd:TIGR03468 105 LAASDT-VVSTAAAKAALARATGAAAVDMESGAVAAVAAAAGLPFAVIRVISDPADR 160
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 2-216 2.13e-14

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 70.04  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    2 KIGIIGAMEEEVTLLRDKI---ENRQTISLGG--CEIYTGQLNGTEVALLKSG---------IGKVAAALGATLLLEHCK 67
Cdd:PLN02584  10 TVLIVIAMQAEAMPLVNALglvEDVDSPFPKGvpWVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQALK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   68 PDVIINTGSAGGL-APTLKVGDIVVSDEARYHD-----ADVTAFGYEYGQLPGCPAGFKAddkliaaaeaciaelnLNAV 141
Cdd:PLN02584  90 PDLIINAGTAGGFkAKGAAIGDVFLATAVANHDrripiPVFDKYGVGTRDAFPTPNLIKA----------------LGLK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128152  142 RGLIVSGDAFINGSVGLAKIRHNfpQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVAD--QQSHLSFDEFLAVAAK 216
Cdd:PLN02584 154 EGVLSTGNSLDMTEQDEESIKAN--DATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDgdKPTAEEFLENLSAAAA 228
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 1-203 2.57e-14

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 69.43  E-value: 2.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152    1 MKIGIIGAMEEE-VTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGG 79
Cdd:PRK07164   4 KIIAIIYADNNEfVNLENFEFILLKNIESFQKKIAIFRYKNYNILYINTGIGLINAALATQKLIEKYQIEIIINYGAVGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   80 LApTLKVGDIVVSDEARYHDAdVTAFgYEYGQLPGCPAGFKADDKliaaaeaciaelNLNAVRGLIVSGDAFINGSVGLa 159
Cdd:PRK07164  84 NI-NIDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYENNKI------------NKNFNKIHLGSSNSFIFDLDKL- 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 16128152  160 KIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQS 203
Cdd:PRK07164 148 KIIKDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNS 191
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 66-201 2.51e-11

adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG; adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD), or homodimeric such as human and Trypanosoma brucei UP. The PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350168  Cd Length: 188  Bit Score: 60.63  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  66 CKPDVIINTGSAGGLAPTLKVGDIVVSDEAryHDADVTAfgyeygqlpgcpagfkADDKLIAAAEACIAELNLNAVRGLI 145
Cdd:cd17768  45 AGARALISFGVAGGLDPALKPGDLVLPEAV--VADGERY----------------PTDPAWRRRLLRALPAGLRVVAGPL 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128152 146 VSGDAFInGSVGlAKIR-HNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQ 201
Cdd:cd17768 107 AGSDAPV-LSVA-DKAAlHAATGAVAVDMESGAVAAVAAEAGLPFAAIRAIADPADR 161
PRK05634 PRK05634
nucleosidase; Provisional
 41-217 1.06e-09

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 55.84  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   41 TEVALLKSGIGKVAAALGATLL--LEHCKPDVIINTGSAGGLAPTLkvGDIVVSDEARYHDADVTAF----GYEYGQLPG 114
Cdd:PRK05634  21 AGLPLLITGIGKVAAAVALTRAlaRRGVLPPRVVNIGTAGALRDGL--SGVFEPSHVINHDFSSDLIraltGHPVANRLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  115 CPAGFKAddkliaaaeaciaelnlnavrgLIVSGDAFINGSVG---LAKirhnfpQAIAVEMEATAIAHVCHNFNVPFVV 191
Cdd:PRK05634  99 LPTGDGA----------------------VLATGDAFISDTATrdrLAQ------RADLVDMEGYAVAAVAAEFGVPCRL 150

                        170       180
                 ....*....|....*....|....*.
gi 16128152  192 VRAISDVADQQSHLSFDEFLAVAAKQ 217
Cdd:PRK05634 151 VKHVSDSADESALGSWPEAVDASARE 176
PRK07077 PRK07077
phosphorylase;
71-200 5.27e-09

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 54.66  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   71 IINTGSAGGLAPTLKVGDIVVSDEaryhdadVTAFGYEYGQLPGCPAGFKADDKLIAAAEaciaelnlNAVRGLIVSGDA 150
Cdd:PRK07077  57 IVSFGVAGGLDPDLAPGDLVVATA-------VDAPFGRVDTDARWSARLAAALELTPVAR--------RVVRGGLAGVEA 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 16128152  151 FINGSVGLAKIRHNfPQAIAVEME---ATAIAHVCHnfnVPFVVVRAISDVAD 200
Cdd:PRK07077 122 PVVGAAAKAALHRA-TGALAVDMEshiAAAFAAARG---LPFAACRVIVDPAW 170
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 69-223 2.04e-08

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: 52.79  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  69 DVIINTGSAGGLAPTLKVGDIVVSDEArYHDadvTAFGYEYGqLPGCPAgFKADDKLIAAAEACIAELNLNAVRGLIVSG 148
Cdd:cd09006  80 KNIIRIGTCGAYQPDLKLRDVVLAMGA-STD---SNYNRLRF-GGGDFA-PIADFELLRKAVETAKELGIPVHVGNVFSS 153

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128152 149 DAFINGSVGLAKIRHNFpQAIAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHLSFDEFLAVAAKQSSL--MVE 223
Cdd:cd09006 154 DVFYDDDPELWKKLKKY-GVLAVEMEAAALYTNAARLGKKALAILTVSD------SLVTGEELSAEERETSFtnMIE 223
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 68-232 6.98e-08

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 51.20  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   68 PDVIINTGSAGglAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLP--GCPAgfkadDKLIAAAEACIAELNLnAVRGLI 145
Cdd:PRK06026  61 PDLVVSLGSAG--SAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPflDLPA-----TVELPLRIPGIPEASL-STGGNI 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  146 VSGDAFingsvglakirhnfpQAIA---VEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLS-FDEFLAVAAKQSSLM 221
Cdd:PRK06026 133 VSGAAY---------------DAIDadmVDMETYAVLRACQAFGVPLIGLRGISDGAAELKHVGdWTEYLHVIDEKLAGA 197

                        170
                 ....*....|.
gi 16128152  222 VESLVQKLAHG 232
Cdd:PRK06026 198 VDRLERALEDG 208
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 34-197 2.58e-07

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 49.78  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  34 YTGQLNGTEVALLKSGIG------------KvaaalgatlllehCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDAd 101
Cdd:COG2820  56 YTGTYKGKRITVISTGIGgpsaaiaveelaA-------------LGAKTFIRVGTSGALQPDIPVGDLVIATGAVRLDG- 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152 102 VTAF--GYEYgqlpgcPAgfKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQ---------AIA 170
Cdd:COG2820 122 TSNFyaPAEY------PA--VADFELTRALVEAAEELGVDYHVGITASTDGFYAEQGRELRVDPDLDEkleawrklgVLN 193

                       170       180
                ....*....|....*....|....*..
gi 16128152 171 VEMEATAIAHVCHNFNVPFVVVRAISD 197
Cdd:COG2820 194 VEMETAALFTLARLRGHRAGSVLAVSA 220
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 21-175 8.34e-07

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: 47.99  E-value: 8.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  21 ENRqtislgGCEIYTGQLNGTEVALLKSGIGKvaaalgatlllehckPD--------------VIINTGSAGGLAPTLKV 86
Cdd:cd17764  27 ENR------GLLVYTGKYKGEEVTIATHGIGG---------------PSaaivfeelimlgakVIIRLGTAGGLVPELRV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  87 GDIVVSDEARYHDadvtafGYEYGQ-LPG-CPAGfKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHN 164
Cdd:cd17764  86 GDIVVATGASYYP------GGGLGQyFPDvCPPA-SPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSS 158

                       170
                ....*....|.
gi 16128152 165 FpQAIAVEMEA 175
Cdd:cd17764 159 L-GFIAVEMEC 168
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
 70-194 3.35e-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: 46.80  E-value: 3.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  70 VIINTGSAGGLAPTLKVGDIVVSDEA-----RYHDADvTAFGYEYGQLP---GCPagFKADD--KLIAAAEACIAELNLN 139
Cdd:cd17769  74 AIIRLGSCGSLDPDVPVGSVVVPSASvavtrNYDDDD-FAGPSTSSEKPyliSKP--VPADPelSELLESELKASLGGEV 150

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128152 140 AVRGLIVSGDAFInGSVG-------------LAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRA 194
Cdd:cd17769 151 VVEGLNASADSFY-SSQGrqdpnfpdhnenlIDKLLKRYPGAASLEMETFHLFHLARCSRPAQGKIRA 217
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 71-178 1.60e-05

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: 44.60  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  71 IINTGSAGGLAPTLKVGDIVVSDEAryHDADVTAFGYEYGQlPGCPAgfkADDKLIAAAEACIAELNLNAVRGLIVSGDA 150
Cdd:cd17765  84 LIRVGTCGGLSSGLQLGDLIVATAA--VPADGTTRALLGGE-PYAPA---ADFELVEALYRAARAAGMPVHVGPVATSDL 157

                        90       100
                ....*....|....*....|....*...
gi 16128152 151 FINGSVGLAKIRHNFPqAIAVEMEATAI 178
Cdd:cd17765 158 FYDPTPDGVKRWRRRG-VLAVEMEASAL 184
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 69-223 2.71e-05

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: 43.95  E-value: 2.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  69 DVIINTGSAGGLAPTLKVGDIVVSDEArYHD---ADVTAFGYEYgqLPGcpagfkADDKLIAAAEACIAELNLNAVRGLI 145
Cdd:COG0813  84 KNIIRVGTCGALQEDVKVRDVVIAMGA-STDsnvNRQRFGGGDF--API------ADFELLRKAVEAAKELGIKVHVGNV 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152 146 VSGDAFINGSVGLAKIRHNFpQAIAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHLSFDEFLAVAAKQSSL--MVE 223
Cdd:COG0813 155 FSSDLFYREDPDLLEKLAKY-GVLAVEMEAAALYTLAAKYGKRALAILTVSD------HLVTGEETTAEERQTTFndMME 227
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 2-197 1.17e-04

uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 41.70  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   2 KIGIIGAMEEEVTLLRDKIENR---QTISLGGCEIYTGQLNGTEVALLKSGIG---------KVAAALgatlllehCKpd 69
Cdd:cd09007   3 EKCVLVFSGDLLEYLLEEYGAEkigELSSAGHTPLYRLEYDGEEVGVVGPPVGapaavlvleELIALG--------AK-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  70 VIINTGSAGGLAPTLKVGDIVVSDEA-R-----YHdadvtafgYeygqLPgcPAGF-KADDKLIAAAEACIAELNLNAVR 142
Cdd:cd09007  73 KFIVVGSCGSLDPDLAVGDIILPTSAlRdegtsYH--------Y----LP--PSRYiEPDPELLDALEEALEKAGIPYVR 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128152 143 GLIVSGDAFINGSVGLAKIRHNfpQ-AIAVEMEATAIAHVCHNFNVPFVVVRAISD 197
Cdd:cd09007 139 GKTWTTDAPYRETRAKVARRRA--EgCLAVEMEAAALFAVAQFRGVELAQLLYVSD 192
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
71-223 1.51e-03

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 38.68  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   71 IINTGSAGGLAPTLKVGDIVVSDEA---------RYHDADVTAFgyeygqlpgcpagfkADDKLIAAAEACIAELNLNAV 141
Cdd:PRK05819  85 LIRVGSCGALQEDVKVRDVVIAMGAstdsnvnriRFKGHDFAPI---------------ADFDLLRKAYDAAKEKGITVH 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  142 RGLIVSGDAFINGSVGLAKI--RHNfpqAIAVEMEATAIAHVCHNFNVPFVVVRAISDvadqqsHLSFDEFLAVAAKQSS 219
Cdd:PRK05819 150 VGNVFSADLFYNPDPEMFDVleKYG---VLGVEMEAAALYGLAAKYGVKALTILTVSD------HIVTGEATTAEERQTT 220


                 ....*.
gi 16128152  220 L--MVE 223
Cdd:PRK05819 221 FndMIE 226
PRK08236 PRK08236
hypothetical protein; Provisional
 69-197 2.64e-03

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 37.73  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152   69 DVIINTGSAGGLAPTLKVGDIVVSDEARYHD--AD-------VTAFGYeygqlpGCPAgFKADDKLIAAAEACIAELNLN 139
Cdd:PRK08236  55 DLVVSAGIAGGFPGKAEVGSLVVADEIIAADlgAEtpdgflpVDELGF------GTTT-IQVDPALVRQLTEALLAAALG 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128152  140 AVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISD 197
Cdd:PRK08236 128 ATAGPVLTVSTVTGTAETAAALAARHPDAVAEAMEGFGVAEAAAAAGLPVLELRAISN 185
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 34-95 9.59e-03

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: 36.27  E-value: 9.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128152  34 YTGQLNGTEVALLKSGIG------KVaaalgatllLE--HCKPDVIINTGSAGGLAPTLKVGDIVVSDEA 95
Cdd:cd17767  45 YTGTYKGVPVSVCSTGIGgpsaaiAV---------EElaQLGAKTFIRVGTCGALQPDIKLGDLVIATGA 105
 
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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