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Conserved domains on  [gi|1264262913|ref|WP_097892211.1|]
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5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

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;
1-231 3.46e-114

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


:

Pssm-ID: 180148  Cd Length: 230  Bit Score: 325.92  E-value: 3.46e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   1 MRIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGF 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  81 HHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQVM 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAK-ELNLNVHRGLIASGDQFIAGAEKVA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264262913 161 AICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKELK 231
Cdd:PRK05584  160 AIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-231 3.46e-114

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 325.92  E-value: 3.46e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   1 MRIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGF 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  81 HHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQVM 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAK-ELNLNVHRGLIASGDQFIAGAEKVA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264262913 161 AICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKELK 231
Cdd:PRK05584  160 AIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-230 7.16e-106

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: 304.72  E-value: 7.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMSDPNQVMA 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACI-AELNLNAVRGLIVSGDAFINGSVGLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264262913 162 ICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:TIGR01704 160 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-231 4.60e-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: 279.87  E-value: 4.60e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   1 MRIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGF 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  81 HHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQAEnNVQVVKGMIATGDSFMSDPNQVM 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKES-GLKVVTGTIATGDRFVWSAEEKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 161 AICDKFEN----------LYavemeaaavaQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:COG0775   160 RLRERFPGalavdmegaaIA----------QVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229


                  .
gi 1264262913 231 K 231
Cdd:COG0775   230 R 230
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-226 1.82e-93

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: 273.22  E-value: 1.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   3 IAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHH 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  83 SLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQVMAI 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAK-ELGPKVHTGLIASGDQFVASSEKKEEL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 163 CDKFENL---------YavemeaaavaQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKV 226
Cdd:cd09008   160 RENFPALavemegaaiA----------QVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-228 1.20e-44

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: 149.03  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEqAETETI---ADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTI-LLERYKPKKIINTGSA 77
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLD-DETPVGppsRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  78 GGFHHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMSDPN 157
Cdd:pfam01048  80 GGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAA-ERLGIPVHRGVYATGDGFYFETP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264262913 158 QVMAIcdkFENLYAVEME--AAAVAQVCYQYKVPFVIIRALSDIAGKESNVT-----FDQFLDRAALHSTNFIIKVLK 228
Cdd:pfam01048 159 AEIRL---LRRLGADAVEmeTAAEAQVAREAGIPFAAIRVVSDLAAGGADGEltheeVEEFAERAAERAAALLLALLA 233
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
1-231 3.46e-114

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 325.92  E-value: 3.46e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   1 MRIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGF 80
Cdd:PRK05584    1 MKIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  81 HHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQVM 160
Cdd:PRK05584   81 APGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAK-ELNLNVHRGLIASGDQFIAGAEKVA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264262913 161 AICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKELK 231
Cdd:PRK05584  160 AIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKLA 230
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 2-230 7.16e-106

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: 304.72  E-value: 7.16e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:TIGR01704   1 KIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMSDPNQVMA 161
Cdd:TIGR01704  81 PTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACI-AELNLNAVRGLIVSGDAFINGSVGLAK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264262913 162 ICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:TIGR01704 160 IRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 1-231 4.60e-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: 279.87  E-value: 4.60e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   1 MRIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGF 80
Cdd:COG0775     1 MTIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  81 HHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQAEnNVQVVKGMIATGDSFMSDPNQVM 160
Cdd:COG0775    81 DPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKES-GLKVVTGTIATGDRFVWSAEEKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 161 AICDKFEN----------LYavemeaaavaQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:COG0775   160 RLRERFPGalavdmegaaIA----------QVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229


                  .
gi 1264262913 231 K 231
Cdd:COG0775   230 R 230
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 3-226 1.82e-93

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: 273.22  E-value: 1.82e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   3 IAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHH 82
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  83 SLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQVMAI 162
Cdd:cd09008    81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAK-ELGPKVHTGLIASGDQFVASSEKKEEL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 163 CDKFENL---------YavemeaaavaQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKV 226
Cdd:cd09008   160 RENFPALavemegaaiA----------QVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-226 4.15e-52

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: 167.47  E-value: 4.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   3 IAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHH 82
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  83 SLNVGDIVISTEVRYHDVDVtafnyehgqipgmPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMSDPNQVMAI 162
Cdd:cd17877    81 GLAVGDLVIADRVLYHDGDV-------------PAGLEADEKLVALAEELA-AGLNLKVHRGTIITVDAIVRKSAEKAAL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264262913 163 CDKFENLyAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLD-RAALHSTNFIIKV 226
Cdd:cd17877   147 AARFPAL-AVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFLDeEGAVRPGAVLLTL 210
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 2-228 1.20e-44

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: 149.03  E-value: 1.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEqAETETI---ADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTI-LLERYKPKKIINTGSA 77
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLD-DETPVGppsRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  78 GGFHHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIPGMPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMSDPN 157
Cdd:pfam01048  80 GGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAA-ERLGIPVHRGVYATGDGFYFETP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264262913 158 QVMAIcdkFENLYAVEME--AAAVAQVCYQYKVPFVIIRALSDIAGKESNVT-----FDQFLDRAALHSTNFIIKVLK 228
Cdd:pfam01048 159 AEIRL---LRRLGADAVEmeTAAEAQVAREAGIPFAAIRVVSDLAAGGADGEltheeVEEFAERAAERAAALLLALLA 233
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 2-230 3.63e-44

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 147.85  E-value: 3.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:PRK14697    3 RIGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTafnyehgQIPGMPP---GFRADEALVALAEK-CMQAENNVQVVKGMIATGDSFMSDPN 157
Cdd:PRK14697   83 PDVKVGDIVISTNVTHHDVSKT-------QMKNLFPfqeEFIASKELVELARKaCNSSSLHIEIHEGRIVSGECFVEDSK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 158 QVMAICDKFENlYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:PRK14697  156 LKAKLIDEYAP-HCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKNI 227
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 2-230 5.62e-37

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 134.75  E-value: 5.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:PRK06698    3 RIGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTafnyehgQIPGMPP---GFRADEALVALAEK-CMQAENNVQVVKGMIATGDSFMSDPN 157
Cdd:PRK06698   83 PDVKVGDIVISTNVTHHDVSKT-------QMKNLFPfqeEFIASKELVELARKaCNSSSLHMEIHEGRIVSGECFVEDSK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 158 QVMAICDKFENlYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAALHSTNFIIKVLKEL 230
Cdd:PRK06698  156 LKAKLIDEYAP-HCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKTI 227
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 2-201 2.34e-26

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: 101.46  E-value: 2.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIyilRNKLEQAETETIadcefTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:cd17766     1 MILIVTAVPLET---NLERVEAEREAV-----LRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HS-LNVGDIVISTEVRY-----------HDVDVTAFnyehGQIPGMPPGFRADEALVALAekcmqAENNVQVVKGMI--- 146
Cdd:cd17766    73 GSgLSVGDLVVASEEIAadlgvetpegfLSLDELGF----GLLRIGTDPYLNRFPLSALL-----LAAGLQVKTGPFltv 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264262913 147 --ATGDSFMSD------PnqvmAICdkfENL--YavemeaaAVAQVCYQYKVPFVIIRALSDIAG 201
Cdd:cd17766   144 stVTGTAERAAelqrrfP----AIA---ENMegA-------AVAHAALLYGVPFLEIRGISNPVG 194
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 3-216 1.06e-22

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: 91.58  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   3 IAVIGAMEEEIYILRNKLEQAET-ETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLErYKPKKIINTGSAGGFH 81
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKvSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCA-LGVDTIIRVGSCGALR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTAFNyehgqiPGMPPGFRADEALVALAEKCMqAENNVQVVKGMIATGDSFMsdpNQVMA 161
Cdd:cd09005    80 EDIKVGDLVIADGAIRGDGVTPYYV------VGPPFAPEADPELTAALEEAA-KELGLTVHVGTVWTTDAFY---RETRE 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264262913 162 ICDKFENLYAVEM--EAAAVAQVCYQYKVPFVIIRALSDIAGKESNVTFDQFLDRAA 216
Cdd:cd09005   150 ESEKLRKLGALAVemETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAE 206
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 43-230 6.61e-15

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 70.97  E-value: 6.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  43 VILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGfHHSLNVGDIVISTEVRYHDVdVTAFnYEHGQIPGMPPGFRAD 122
Cdd:PRK07164   47 ILYINTGIGLINAALATQKLIEKYQIEIIINYGAVGS-NINIDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYENN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 123 ealvalaekcmQAENNVQvvKGMIATGDSFMSDPNQVMAIcDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIAGK 202
Cdd:PRK07164  124 -----------KINKNFN--KIHLGSSNSFIFDLDKLKII-KDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIEN 189

                         170       180
                  ....*....|....*....|....*....
gi 1264262913 203 ESNVTF-DQFLDRAALHSTNFIIKVLKEL 230
Cdd:PRK07164  190 NSDIEIvNNNIKKGSKKALEFIFELLENI 218
fut_nucase TIGR03664
futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine ...
 34-201 1.53e-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: 70.03  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  34 TRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHHSLNVGDIVISTEV-----------RYHDVDV 102
Cdd:TIGR03664  22 YAGSVGGAGFDVLVTGVGPVNAAAATARLLARAPYELVINAGIAGGFPGKAAVGDLVVADSEiaadlgaetpeGFLPLEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 103 TAFNYEHGQIPGMPPGFRADEALVALAEKCMQAEnNVQVVKGMIATGDSFMSDPNQVMAICDKF----ENLyavemEAAA 178
Cdd:TIGR03664 102 LGFPQLPGGGRSYFNRIPLDPDLVERAVQLARAL-GLPVARGPFLTVSTVSGTAARAEALARRFgavaENM-----EGAA 175

                         170       180
                  ....*....|....*....|...
gi 1264262913 179 VAQVCYQYKVPFVIIRALSDIAG 201
Cdd:TIGR03664 176 VALAALRYGVPFLELRGISNLVG 198
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 2-200 3.46e-11

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 61.09  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFTRGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFH 81
Cdd:PRK06714    3 RIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  82 HSLNVGDIVISTEVRYHDVDVTA-----FNYEHGQIPGMppgfRADEALVALAEKcMQAENNVQVvkGMIATGDSFMSDP 156
Cdd:PRK06714   83 NKVKNGHIVVALNAIQHDVTAAGsgedvFNLYNGRTAPI----ETTKSLVRRIKK-IRSYDPIHF--GTFLSGDQRIRSS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1264262913 157 nQVMAICDKFENLYAVEMEAAAVAQVCYQYKVPFVIIRALSDIA 200
Cdd:PRK06714  156 -EMRYLLHTVYGALAVDQEVAAFAYVCQINKKPFLCLKAASDQA 198
PRK05634 PRK05634
nucleosidase; Provisional
 45-216 2.57e-10

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 57.77  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  45 LLKSGIGKVNAAMSTTILL--ERYKPKKIINTGSAGGFHHSLNvGDIVIStEVRYHDVDVTAFNyehgQIPGMPPGfrad 122
Cdd:PRK05634   25 LLITGIGKVAAAVALTRALarRGVLPPRVVNIGTAGALRDGLS-GVFEPS-HVINHDFSSDLIR----ALTGHPVA---- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 123 eALVALAEkcmqaennvqVVKGMIATGDSFMSDPN------QVMAICDkfenlyaveMEAAAVAQVCYQYKVPFVIIRAL 196
Cdd:PRK05634   95 -NRLELPT----------GDGAVLATGDAFISDTAtrdrlaQRADLVD---------MEGYAVAAVAAEFGVPCRLVKHV 154

                         170       180
                  ....*....|....*....|
gi 1264262913 197 SDIAGKESNVTFDQFLDRAA 216
Cdd:PRK05634  155 SDSADESALGSWPEAVDASA 174
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 2-199 8.75e-09

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 54.24  E-value: 8.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETI-----ADCEFTRGLLAGHEVILLKSG---------IGKVNAAMSTTILLERYK 67
Cdd:PLN02584   10 TVLIVIAMQAEAMPLVNALGLVEDVDSpfpkgVPWVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQALK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  68 PKKIINTGSAGGFH-HSLNVGDIVISTEVRYHDvdvtafnyehGQIPgmPPGFraDEALVALAEKC----MQAENNVQVv 142
Cdd:PLN02584   90 PDLIINAGTAGGFKaKGAAIGDVFLATAVANHD----------RRIP--IPVF--DKYGVGTRDAFptpnLIKALGLKE- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1264262913 143 kGMIATGDSF-MSDpnQVMAICDKFEnLYAVEMEAAAVAQVCYQYKVPFVIIRALSDI 199
Cdd:PLN02584  155 -GVLSTGNSLdMTE--QDEESIKAND-ATVKDMEGAAVAYVADLLKVPAIFVKAVTDI 208
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 32-152 2.32e-07

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: 49.75  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  32 EFT--RGLLAGHEVILLKSGIGkvnaAMSTTILLE---RYKPKKIINTGSAGGFHHSLNVGDIVISTE-VRYhdvDVTAF 105
Cdd:cd17767    41 EYRtyTGTYKGVPVSVCSTGIG----GPSAAIAVEelaQLGAKTFIRVGTCGALQPDIKLGDLVIATGaVRD---EGTSK 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1264262913 106 NYehgqipgMPPGFRA---DEALVALAEKCmqAENNVQVVKGMIATGDSF 152
Cdd:cd17767   114 HY-------VPPEYPAvadPEVVLALVEAA--EELGVPYHVGITASKDSF 154
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 32-152 3.41e-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: 49.40  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  32 EFT--RGLLAGHEVILLKSGIGKVNAAmsttILLE---RYKPKKIINTGSAGGFHHSLNVGDIVISTE-VRYhdvDVTAF 105
Cdd:COG2820    52 EFRtyTGTYKGKRITVISTGIGGPSAA----IAVEelaALGAKTFIRVGTSGALQPDIPVGDLVIATGaVRL---DGTSN 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1264262913 106 NYehgqipgMPPGF--RADEALV-ALAEKCmqAENNVQVVKGMIATGDSF 152
Cdd:COG2820   125 FY-------APAEYpaVADFELTrALVEAA--EELGVDYHVGITASTDGF 165
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 37-201 1.25e-06

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: 47.72  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  37 LLAGHEVILLK-SGIGKVNAAMSTTILLERyKPKKIINTGSAGGFHHSLNVGDIVISTEVRYHDvdvtafnyehgqipgm 115
Cdd:TIGR03468  15 RIAAGPGLLVClSGGGPERARAAAARLMAA-GAAGLVSFGTAGALDPALQPGDLVVPEEVRADG---------------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913 116 pPGFRADEALVALAEKCMQAENNVqvVKGMIATGDSFMSDPNQVMAICDK-------FENlyavemeaAAVAQVCYQYKV 188
Cdd:TIGR03468  78 -DRFPTDPAWRRRLLEALPAGLRV--HRGVLAASDTVVSTAAAKAALARAtgaaavdMES--------GAVAAVAAAAGL 146

                         170
                  ....*....|...
gi 1264262913 189 PFVIIRALSDIAG 201
Cdd:TIGR03468 147 PFAVIRVISDPAD 159
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 35-159 2.42e-06

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: 47.01  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  35 RGLLA------GHEVILLKSGIGkvNAAMS--TTILLERYKPKKIINTGSAGGFHHSLNVGDIVISTEVryhdvdVTAFN 106
Cdd:cd09006    40 RNMLGytgtykGKRVSVMGSGMG--MPSIGiyAYELFKFYGVKNIIRIGTCGAYQPDLKLRDVVLAMGA------STDSN 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 107 YEHGQIPGMPPGFRADEALVALAEKCMQaENNVQVVKGMIATGDSFMSDPNQV 159
Cdd:cd09006   112 YNRLRFGGGDFAPIADFELLRKAVETAK-ELGIPVHVGNVFSSDVFYDDDPEL 163
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 2-152 4.69e-06

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: 45.94  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913   2 RIAVIGAMEEEIYILRNKLEQAETETIADCEFT---RGLLAGHEVILLKSGIGkvnAAMsTTILLER---YKPKKIINTG 75
Cdd:cd09007     3 EKCVLVFSGDLLEYLLEEYGAEKIGELSSAGHTplyRLEYDGEEVGVVGPPVG---APA-AVLVLEEliaLGAKKFIVVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  76 SAGGFHHSLNVGDIVISTE-VR-----YHdvdvtafnYehgqipgMPPG--FRADEALVALAEKCMQaENNVQVVKGMIA 147
Cdd:cd09007    79 SCGSLDPDLAVGDIILPTSaLRdegtsYH--------Y-------LPPSryIEPDPELLDALEEALE-KAGIPYVRGKTW 142


                  ....*
gi 1264262913 148 TGDSF 152
Cdd:cd09007   143 TTDAP 147
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 33-166 1.41e-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: 44.72  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  33 FTrGLLAGHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHHSLNVGDIVI----STEVRYHDVdvtaFNYE 108
Cdd:COG0813    49 YT-GTYKGKRVSVMGSGMGIPSISIYAYELITEYGVKNIIRVGTCGALQEDVKVRDVVIamgaSTDSNVNRQ----RFGG 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1264262913 109 HGQIPGmpPGFRADEALVALAEkcmqaENNVQVVKGMIATGDSFMSDPNQVMAICDKF 166
Cdd:COG0813   124 GDFAPI--ADFELLRKAVEAAK-----ELGIKVHVGNVFSSDLFYREDPDLLEKLAKY 174
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 35-152 1.03e-04

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: 41.83  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  35 RGLLA------GHEVILLKSGIGkvnaAMSTTILLE---RYKPKKIINTGSAGGFHHSLNVGDIVIstevryhdvdVTAF 105
Cdd:cd17764    29 RGLLVytgkykGEEVTIATHGIG----GPSAAIVFEeliMLGAKVIIRLGTAGGLVPELRVGDIVV----------ATGA 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1264262913 106 NYEHGQI-----PGMPPGFRADEALV-ALAEKCmqAENNVQVVKGMIATGDSF 152
Cdd:cd17764    95 SYYPGGGlgqyfPDVCPPASPDPELTlELVESL--SKRGLKYYVGPVFSSDAF 145
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 46-113 1.04e-04

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 41.96  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264262913  46 LKSGIGKVNAAMSTTILLERYK-----PKKIINTGSAGGfhHSLNVGDIVISTEVRYHDVDVTAFNYEHGQIP 113
Cdd:PRK06026   34 LMTGVGPVEAAVNLTAALARLKaagdlPDLVVSLGSAGS--AKLEQTEVYQVSSVSYRDMDASPLGFEKGVTP 104
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
14-161 2.44e-04

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 41.00  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  14 YILRNKLEQAEtetiadcEFT--RGLLA------GHEVILLKSGIGKVNAAMSTTILLERYKPKKIINTGSAGGFHHSLN 85
Cdd:PRK05819   27 YIAETFLEDVV-------CVNevRGMLGftgtykGKRVSVMGTGMGIPSISIYANELITDYGVKKLIRVGSCGALQEDVK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  86 VGDIVI----STE-----VRYHDVDVTAFnyehgqipgmppgfrADEALVALAEKCMQaENNVQVVKGMIATGDSFMSD- 155
Cdd:PRK05819  100 VRDVVIamgaSTDsnvnrIRFKGHDFAPI---------------ADFDLLRKAYDAAK-EKGITVHVGNVFSADLFYNPd 163


                  ....*...
gi 1264262913 156 --PNQVMA 161
Cdd:PRK05819  164 peMFDVLE 171
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 23-230 9.69e-04

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


Pssm-ID: 350168  Cd Length: 188  Bit Score: 38.68  E-value: 9.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  23 AETETIADCEFTRG--LLAGHEVILLKSGIGKVNAAMSTTILLERyKPKKIINTGSAGGFHHSLNVGDIVISTEV----R 96
Cdd:cd17768     1 AEARCLTVTGLKFEarIAIGDGLLVILSGAGPERARRAAERLLAA-GARALISFGVAGGLDPALKPGDLVLPEAVvadgE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  97 YHDVDVTAFNYEHGQIPGMPPGFRA-----DEALVALAEKCMQAEnnvqvvkgmiATG----DsfM-SdpnQVMAicdkf 166
Cdd:cd17768    80 RYPTDPAWRRRLLRALPAGLRVVAGplagsDAPVLSVADKAALHA----------ATGavavD--MeS---GAVA----- 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264262913 167 enlyavemeaaavaQVCYQYKVPFVIIRALSDIAgkesnvtfDQFLDRAALHSTN-----FIIKVLKEL 230
Cdd:cd17768   140 --------------AVAAEAGLPFAAIRAIADPA--------DRSLPPAALKALDpdgsvDLLALLRAL 186
PRK08236 PRK08236
hypothetical protein; Provisional
 22-148 1.49e-03

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 38.50  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264262913  22 QAETETIadcefTRGLLAGHEVILLKSGIGKVNAAMST-TILLERYKPKK-IINTGSAGGFHHSLNVGDIVISTEVRYHD 99
Cdd:PRK08236   11 PAERDAV-----LRGLGNDSRFDVLAAGVGPAAAAASTaRALAAAAAPYDlVVSAGIAGGFPGKAEVGSLVVADEIIAAD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1264262913 100 VDVTAfnyEHGQIPGMPPGF-----RADEALVALAEKCMQAEnNVQVVKGMIAT 148
Cdd:PRK08236   86 LGAET---PDGFLPVDELGFgtttiQVDPALVRQLTEALLAA-ALGATAGPVLT 135
 
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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