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Conserved domains on  [gi|490412629|ref|WP_004285268|]
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5'-methylthioadenosine/adenosylhomocysteine nucleosidase [Neisseria weaveri]

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;
11-239 1.26e-108

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


:

Pssm-ID: 180148  Cd Length: 230  Bit Score: 312.06  E-value: 1.26e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  11 TVAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC 90
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAA 170
Cdd:PRK05584  82 PGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKEL-NLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 171 IRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKL 229
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
11-239 1.26e-108

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 312.06  E-value: 1.26e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  11 TVAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC 90
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAA 170
Cdd:PRK05584  82 PGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKEL-NLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 171 IRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKL 229
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 12-235 2.64e-101

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: 293.25  E-value: 2.64e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:cd09008    1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAAI 171
Cdd:cd09008   81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKEL-GPKVHTGLIASGDQFVASSEKKEEL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490412629 172 RKLFeDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRI 235
Cdd:cd09008  160 RENF-PALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 11-239 1.60e-99

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: 289.12  E-value: 1.60e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  11 TVAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC 90
Cdd:COG0775    2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAfDGAAVHRGLIVSGDQFVHSSEKTAA 170
Cdd:COG0775   82 PDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKE-SGLKVVTGTIATGDRFVWSAEEKRR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 171 IRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:COG0775  161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 12-239 4.40e-68

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: 209.19  E-value: 4.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:TIGR01704   2 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   92 GLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFDGaAVHRGLIVSGDQFVHSSEKTAAI 171
Cdd:TIGR01704  82 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNL-NAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490412629  172 RKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 11-237 3.02e-51

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: 166.37  E-value: 3.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   11 TVAVVGAMEQEIELLKNSLGNL--EEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTAL-LVGKFNPDCVINTGSAG 87
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDEtpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   88 GLCSGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSsek 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERL-GIPVHRGVYATGDGFYFE--- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490412629  168 TAAIRKLFED--VRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKAD-----ISFEEFLETASVHSADMVKRIVA 237
Cdd:pfam01048 157 TPAEIRLLRRlgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADgelthEEVEEFAERAAERAAALLLALLA 233
 
Name Accession Description Interval E-value
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
11-239 1.26e-108

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 312.06  E-value: 1.26e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  11 TVAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC 90
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLHGHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGVAGGLA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAA 170
Cdd:PRK05584  82 PGLKVGDVVVADELVQHDVDVTAFGYPYGQVPGLPAAFKADEKLVALAEKAAKEL-NLNVHRGLIASGDQFIAGAEKVAA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 171 IRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:PRK05584 161 IRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSFDEFLAVAAKYSANILKRMLEKL 229
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 12-235 2.64e-101

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: 293.25  E-value: 2.64e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:cd09008    1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLGGKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAAI 171
Cdd:cd09008   81 DLKIGDVVIATKVVYHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAAKEL-GPKVHTGLIASGDQFVASSEKKEEL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490412629 172 RKLFeDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRI 235
Cdd:cd09008  160 RENF-PALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEVVLEL 222
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 11-239 1.60e-99

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: 289.12  E-value: 1.60e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  11 TVAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC 90
Cdd:COG0775    2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAfDGAAVHRGLIVSGDQFVHSSEKTAA 170
Cdd:COG0775   82 PDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPALFEADPALLEAAKEAAKE-SGLKVVTGTIATGDRFVWSAEEKRR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 171 IRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:COG0775  161 LRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAAKNAAELLRALLRKL 229
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 12-239 4.40e-68

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: 209.19  E-value: 4.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:TIGR01704   2 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   92 GLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFDGaAVHRGLIVSGDQFVHSSEKTAAI 171
Cdd:TIGR01704  82 TLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNL-NAVRGLIVSGDAFINGSVGLAKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490412629  172 RKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:TIGR01704 161 RHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKL 228
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 12-232 8.34e-55

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: 174.79  E-value: 8.34e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:cd17877    1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHDVDVTafgyapgqvprlaARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSSEKTAAI 171
Cdd:cd17877   81 GLAVGDLVIADRVLYHDGDVP-------------AGLEADEKLVALAEELAAGL-NLKVHRGTIITVDAIVRKSAEKAAL 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490412629 172 RKLFeDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFL-ETASVHSADMV 232
Cdd:cd17877  147 AARF-PALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEEFLdEEGAVRPGAVL 207
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 11-237 3.02e-51

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: 166.37  E-value: 3.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   11 TVAVVGAMEQEIELLKNSLGNL--EEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTAL-LVGKFNPDCVINTGSAG 87
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDEtpVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAILAAIrLLKEFGVDAIIRTGTAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   88 GLCSGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLAARFDSDERLVAAAEKASAAFdGAAVHRGLIVSGDQFVHSsek 167
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPYFPDMAPAPADPELRALAKEAAERL-GIPVHRGVYATGDGFYFE--- 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490412629  168 TAAIRKLFED--VRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKAD-----ISFEEFLETASVHSADMVKRIVA 237
Cdd:pfam01048 157 TPAEIRLLRRlgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADgelthEEVEEFAERAAERAAALLLALLA 233
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 12-239 2.96e-43

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 145.92  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:PRK14697   4 IGIIGAMQIEIDLLLEKLVVQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHDVDVTAFgyaPGQVPRLAARFDSDERLVAAAEKASAAFDGAAVHRGLIVSGDQFVHSSEKTAai 171
Cdd:PRK14697  84 DVKVGDIVISTNVTHHDVSKTQM---KNLFPFQEEFIASKELVELARKACNSSSLHIEIHEGRIVSGECFVEDSKLKA-- 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 172 rKLFEDV--RVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMVKRIVAEL 239
Cdd:PRK14697 159 -KLIDEYapHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEIIVEMLKNI 227
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 12-232 8.58e-38

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 137.07  E-value: 8.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:PRK06698   4 IGIIGAMQIEIDLLLEKLIMQEEQIIAGMPFYVGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHDVDVTAFgyapGQVPRLAARFDSDERLVAAAEKASAAFD-GAAVHRGLIVSGDQFVHSSEKTAa 170
Cdd:PRK06698  84 DVKVGDIVISTNVTHHDVSKTQM----KNLFPFQEEFIASKELVELARKACNSSSlHMEIHEGRIVSGECFVEDSKLKA- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490412629 171 irKLFEDV--RVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETASVHSADMV 232
Cdd:PRK06698 159 --KLIDEYapHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTAANYCSEII 220
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 12-209 2.60e-28

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: 106.85  E-value: 2.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIellknslgNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLC- 90
Cdd:cd17766    2 ILIVTAVPLET--------NLERVEAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFPg 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQI--AH---------HDVDVTAFGYAPGQVPRLAARFDSDERLVAAaekasaafdGAAVHRGLI---- 155
Cdd:cd17766   74 SGLSVGDLVVASEEiaADlgvetpegfLSLDELGFGLLRIGTDPYLNRFPLSALLLAA---------GLQVKTGPFltvs 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 156 -VSGdqfvhSSEKTAAIRKLF----EDvrvveMEAAAIAQTCVQLDVPFVVIRAVSDLA 209
Cdd:cd17766  145 tVTG-----TAERAAELQRRFpaiaEN-----MEGAAVAHAALLYGVPFLEIRGISNPV 193
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 12-224 2.81e-26

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: 101.21  E-value: 2.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGN-FTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFnPDCVINTGSAGGLC 90
Cdd:cd09005    1 YAIIPGDPERVDVIDSKLENPQKVSSFRgYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCALG-VDTIIRVGSCGALR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  91 SGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPrlAARFDSDERLVAAAEKAsaafdGAAVHRGLIVSGDQFV-HSSEKTA 169
Cdd:cd09005   80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAP--EADPELTAALEEAAKEL-----GLTVHVGTVWTTDAFYrETREESE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490412629 170 AIRKLFedVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADISFEEFLETA 224
Cdd:cd09005  153 KLRKLG--ALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEA 205
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 48-211 1.28e-19

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: 83.54  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   48 GGKQVVLALSGIGKVNAAVSTALLVgKFNPDCVINTGSAGGLCSGLKVGDVVVGTQIAhhdVDVTAFGYAPGQVPRLAAR 127
Cdd:TIGR03468  18 AGPGLLVCLSGGGPERARAAAARLM-AAGAAGLVSFGTAGALDPALQPGDLVVPEEVR---ADGDRFPTDPAWRRRLLEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  128 FDsderlvaaaekasaafDGAAVHRGLIVSGDQFVHSSEKTAAIRKLfEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSD 207
Cdd:TIGR03468  94 LP----------------AGLRVHRGVLAASDTVVSTAAAKAALARA-TGAAAVDMESGAVAAVAAAAGLPFAVIRVISD 156


                  ....
gi 490412629  208 LADE 211
Cdd:TIGR03468 157 PADR 160
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 12-213 1.48e-19

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 84.20  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCS 91
Cdd:PRK06714   4 IAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTINDLEIISVITGVGKVSCASCVQLLISEFQPDELFMTGICGSLSN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  92 GLKVGDVVVGTQIAHHdvDVTAFGYAPGQVPRLAAR---FDSDERLVAAAEKASAAfdgAAVHRGLIVSGDQFVHSSEkt 168
Cdd:PRK06714  84 KVKNGHIVVALNAIQH--DVTAAGSGEDVFNLYNGRtapIETTKSLVRRIKKIRSY---DPIHFGTFLSGDQRIRSSE-- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 490412629 169 aaIRKLFEDVR---VVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKA 213
Cdd:PRK06714 157 --MRYLLHTVYgalAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKT 202
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 9-222 3.14e-19

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 83.52  E-value: 3.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   9 IETVAVVGAMEQEIELLKNSLGnLEEKRFGNF------TFYCGMLGGKQVVLALSG---------IGKVNAAVSTALLVG 73
Cdd:PLN02584   8 ISTVLIVIAMQAEAMPLVNALG-LVEDVDSPFpkgvpwVRYSGTHKGLRVHVVCPGkdkalgvdsVGTVPASLVTYAAIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  74 KFNPDCVINTGSAGGL-CSGLKVGDVVVGTQIAHHD--VDVTAFG-YAPGQ-----VPRLAARFDSDErlvaaaekasaa 144
Cdd:PLN02584  87 ALKPDLIINAGTAGGFkAKGAAIGDVFLATAVANHDrrIPIPVFDkYGVGTrdafpTPNLIKALGLKE------------ 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490412629 145 fdgaavhrGLIVSGDQFVHSSEKTAAIRKlfEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLAD-EKAdiSFEEFLE 222
Cdd:PLN02584 155 --------GVLSTGNSLDMTEQDEESIKA--NDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDgDKP--TAEEFLE 221
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 40-210 1.93e-17

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: 77.20  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  40 FTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKfNPDCVINTGSAGGLCSGLKVGDVVVGTQIahHDVDvtafgyapg 119
Cdd:cd17768   11 LKFEARIAIGDGLLVILSGAGPERARRAAERLLAA-GARALISFGVAGGLDPALKPGDLVLPEAV--VADG--------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 120 qvprlaARFDSDERLVAAAEKASAafDGAAVHRGLIVSGDQFVHSSEKTAAIRKLFEDVrVVEMEAAAIAQTCVQLDVPF 199
Cdd:cd17768   79 ------ERYPTDPAWRRRLLRALP--AGLRVVAGPLAGSDAPVLSVADKAALHAATGAV-AVDMESGAVAAVAAEAGLPF 149

                        170
                 ....*....|.
gi 490412629 200 VVIRAVSDLAD 210
Cdd:cd17768  150 AAIRAIADPAD 160
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 8-215 1.99e-15

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 72.51  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   8 KIETVAVVGAMEQEIELLKN-SLGNLEEKRFGNFTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSA 86
Cdd:PRK07164   2 NEKIIAIIYADNNEFVNLENfEFILLKNIESFQKKIAIFRYKNYNILYINTGIGLINAALATQKLIEKYQIEIIINYGAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  87 GGLCSgLKVGDVVVGTQIAHHDVdVTAFgYAPGQVPRLAARFDSDerlvaaaekasaaFDGAAVHRGLIVSGDQFVHSSE 166
Cdd:PRK07164  82 GSNIN-IDLGQVVYPEKFYLLDA-ITPW-YPPGQTPGEKEFYENN-------------KINKNFNKIHLGSSNSFIFDLD 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 490412629 167 KTAAIrKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLADEKADI 215
Cdd:PRK07164 146 KLKII-KDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDFIENNSDI 193
PRK05634 PRK05634
nucleosidase; Provisional
 54-236 1.57e-11

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 61.24  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  54 LALSGIGKVNAAVST--ALLVGKFNPDCVINTGSAGGL---CSGLKVGDVVVgtqiaHHDVDVTAFgyapgqvpRLAARF 128
Cdd:PRK05634  25 LLITGIGKVAAAVALtrALARRGVLPPRVVNIGTAGALrdgLSGVFEPSHVI-----NHDFSSDLI--------RALTGH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 129 DSDERLVAAAEkasaafDGAAvhrglIVSGDQFVhssEKTAAIRKLFEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDL 208
Cdd:PRK05634  92 PVANRLELPTG------DGAV-----LATGDAFI---SDTATRDRLAQRADLVDMEGYAVAAVAAEFGVPCRLVKHVSDS 157

                        170       180
                 ....*....|....*....|....*...
gi 490412629 209 ADEKADISFEEFLETASVHSADMVKRIV 236
Cdd:PRK05634 158 ADESALGSWPEAVDASARELGEWLAEHV 185
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 56-239 2.62e-09

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 55.44  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  56 LSGIGKVNAAVSTALLVGKFN-----PDCVINTGSAGGlcSGLKVGDVVVGTQIAHHDVDVTAFGYAPGQVPRLaarfds 130
Cdd:PRK06026  35 MTGVGPVEAAVNLTAALARLKaagdlPDLVVSLGSAGS--AKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPFL------ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 131 DERLVAAAEKASAAFDGAAVHRGL-IVSGDQFvhssektAAIrklfeDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSDLA 209
Cdd:PRK06026 107 DLPATVELPLRIPGIPEASLSTGGnIVSGAAY-------DAI-----DADMVDMETYAVLRACQAFGVPLIGLRGISDGA 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490412629 210 DEKADIS-FEEFLETASVHSADMVKRIVAEL 239
Cdd:PRK06026 175 AELKHVGdWTEYLHVIDEKLAGAVDRLERAL 205
PRK08236 PRK08236
hypothetical protein; Provisional
 45-208 7.79e-08

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 51.21  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  45 GMLGGKQVVLALSGIGKVNAAVSTA-LLVGKFNP-DCVINTGSAGGLCSGLKVGDVVVGTQIAHHDVDV-TAFGYAPgqV 121
Cdd:PRK08236  20 GLGNDSRFDVLAAGVGPAAAAASTArALAAAAAPyDLVVSAGIAGGFPGKAEVGSLVVADEIIAADLGAeTPDGFLP--V 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 122 PRL---AARFDSDERLVAAAEKASAAfDGAAVHRGLIVSGDQFVHSSEKTAAIRKLFEDVRVVEMEAAAIAQTCVQLDVP 198
Cdd:PRK08236  98 DELgfgTTTIQVDPALVRQLTEALLA-AALGATAGPVLTVSTVTGTAETAAALAARHPDAVAEAMEGFGVAEAAAAAGLP 176

                        170
                 ....*....|
gi 490412629 199 FVVIRAVSDL 208
Cdd:PRK08236 177 VLELRAISNP 186
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 40-220 1.48e-07

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: 50.77  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  40 FTFYCGMLG------GKQVVLALSGIGKVNAAVSTA----LLVGKFnpdcvINTGSAGGLCSGLKVGDVVVGTqiAHHDV 109
Cdd:cd17765   39 YNDHRGLLGytgtykGKPVSVQTTGMGCPSAAIVVEelaqLGVKRL-----IRVGTCGGLSSGLQLGDLIVAT--AAVPA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 110 DVTAFGYAPGQVPRLAARFDSDERLVAAAEKAsaafdGAAVHRGLIVSGDQFVhssEKTAAIRKLFED--VRVVEMEAAA 187
Cdd:cd17765  112 DGTTRALLGGEPYAPAADFELVEALYRAARAA-----GMPVHVGPVATSDLFY---DPTPDGVKRWRRrgVLAVEMEASA 183

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490412629 188 IAQTCVQLDVPFVVIRAVSDL-ADEKADISFEEF 220
Cdd:cd17765  184 LFTLAALRGLRAGCILTVSDLiGDPERRIDDEEL 217
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
 40-188 5.62e-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: 49.01  E-value: 5.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  40 FTFYCGMLGGKQVVLALSGIGKVNAAVSTALLVgKFNPDCVINTGSAGGLCSGLKVGDVVV--------GTqiAHHdvdv 111
Cdd:COG2820   53 FRTYTGTYKGKRITVISTGIGGPSAAIAVEELA-ALGAKTFIRVGTSGALQPDIPVGDLVIatgavrldGT--SNF---- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 112 tafgYAPGQVPRLAarfdsDERLVAAAEKASAAfDGAAVHRGLIVSGDQFVHSSEKTAAIR-------KLFEDVRV--VE 182
Cdd:COG2820  126 ----YAPAEYPAVA-----DFELTRALVEAAEE-LGVDYHVGITASTDGFYAEQGRELRVDpdldeklEAWRKLGVlnVE 195


                 ....*.
gi 490412629 183 MEAAAI 188
Cdd:COG2820  196 METAAL 201
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
 10-188 4.94e-06

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: 46.06  E-value: 4.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  10 ETVAVVGAmEQEIELLKNSLGNLE---EKRfgNFTFYCGMLGGKQVVLALSGIGKVNAAV---STALLVGKFnpdcVINT 83
Cdd:cd17764    1 ERVIAVGD-PGRVELLSTLLEDPRlvnENR--GLLVYTGKYKGEEVTIATHGIGGPSAAIvfeELIMLGAKV----IIRL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  84 GSAGGLCSGLKVGDVVVGTQIAHHdvDVTAFG-YAPGQVPRLAARFDSDERLVAAAEKAsaafdGAAVHRGLIVSGDQFv 162
Cdd:cd17764   74 GTAGGLVPELRVGDIVVATGASYY--PGGGLGqYFPDVCPPASPDPELTLELVESLSKR-----GLKYYVGPVFSSDAF- 145

                        170       180
                 ....*....|....*....|....*.
gi 490412629 163 HSSEKTAAIRKLFEDVRVVEMEAAAI 188
Cdd:cd17764  146 YAEDEEFAERWSSLGFIAVEMECATL 171
PRK07077 PRK07077
phosphorylase;
80-210 3.25e-05

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 43.87  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  80 VINTGSAGGLCSGLKVGDVVVGTQIahhdvdVTAFGYAPGQvPRLAARFDSDERLVAAaekasaafdGAAVHRGLIVSGD 159
Cdd:PRK07077  57 IVSFGVAGGLDPDLAPGDLVVATAV------DAPFGRVDTD-ARWSARLAAALELTPV---------ARRVVRGGLAGVE 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490412629 160 QFVHSSEKTAAIRKLfEDVRVVEME---AAAIAQTCvqlDVPFVVIRAVSDLAD 210
Cdd:PRK07077 121 APVVGAAAKAALHRA-TGALAVDMEshiAAAFAAAR---GLPFAACRVIVDPAW 170
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 80-188 7.93e-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: 42.41  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  80 VINTGSAGGLCSGLKVGDVVVGtQIAHHDVDVTAF-----GYAPGqvprlaARFDSDERLVAAAEKAsaafdGAAVHRGL 154
Cdd:COG0813   86 IIRVGTCGALQEDVKVRDVVIA-MGASTDSNVNRQrfgggDFAPI------ADFELLRKAVEAAKEL-----GIKVHVGN 153

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490412629 155 IVSGDQFVHS-SEKTAAIRKLfeDVRVVEMEAAAI 188
Cdd:COG0813  154 VFSSDLFYREdPDLLEKLAKY--GVLAVEMEAAAL 186
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
45-207 6.44e-04

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 39.84  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  45 GMLG------GKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCSGLKVGDVVVGtQIAHHDVDVTAFGYAP 118
Cdd:PRK05819  44 GMLGftgtykGKRVSVMGTGMGIPSISIYANELITDYGVKKLIRVGSCGALQEDVKVRDVVIA-MGASTDSNVNRIRFKG 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 119 GQVPRLAarfdsDERLVAAAEKASAAfDGAAVHRGLIVSGDQFvHSSEKTAaiRKLFEDVRV--VEMEAAAIAQTCVQLD 196
Cdd:PRK05819 123 HDFAPIA-----DFDLLRKAYDAAKE-KGITVHVGNVFSADLF-YNPDPEM--FDVLEKYGVlgVEMEAAALYGLAAKYG 193

                        170
                 ....*....|.
gi 490412629 197 VPFVVIRAVSD 207
Cdd:PRK05819 194 VKALTILTVSD 204
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 40-188 1.37e-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: 38.96  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  40 FTFYCGMLGGKQVVLALSGIGkvnaAVSTALLV------GKfnpDCVINTGSAGGLCSGLKVGDVVV--------GTQ-- 103
Cdd:cd17767   42 YRTYTGTYKGVPVSVCSTGIG----GPSAAIAVeelaqlGA---KTFIRVGTCGALQPDIKLGDLVIatgavrdeGTSkh 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 104 --------IAHHDVdVTAFgyapgqvpRLAArfdsdERLvaaaekasaafdGAAVHRGLIVSGD-----QFVHSSEKTAA 170
Cdd:cd17767  115 yvppeypaVADPEV-VLAL--------VEAA-----EEL------------GVPYHVGITASKDsfyggQGRPGPGLPPE 168

                        170       180
                 ....*....|....*....|...
gi 490412629 171 IRKLFED-----VRVVEMEAAAI 188
Cdd:cd17767  169 LPELLEEwqragVLNSEMESAAL 191
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
 45-223 1.68e-03

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


Pssm-ID: 188024  Cd Length: 232  Bit Score: 38.60  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629   45 GMLG------GKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCSGLKVGDVVVGT---------QIAHHDV 109
Cdd:TIGR00107  41 GMLGftgtykGKKISVMGHGMGIPSISIYVYELIKFYEVKTIIRVGSCGAIRPDVKLRDVIIAMgastdskynRVRFVEV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  110 DVTAFgyapgqvprlaARFDSDERLVAAAEKAsaafdGAAVHRGLIVSGDQFvHSSEKTAAIRKLFEDVRVVEMEAAAIA 189
Cdd:TIGR00107 121 DFAAI-----------ADFELVENAYDAAKAK-----GVDVHVGNVFSADAF-YQPDKDVFDLMAKYGILGVEMEAAALY 183

                         170       180       190
                  ....*....|....*....|....*....|....
gi 490412629  190 QTCVQLDVPFVVIRAVSDLADEKADISFEEFLET 223
Cdd:TIGR00107 184 ANAAELGAKALTILTVSDHLVTHEATTAEERQTT 217
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
45-224 4.02e-03

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 37.39  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  45 GMLG------GKQVVLALSGIGKVNAAVSTALLVGKFNPDCVINTGSAGGLCSGLKVGDVVVGtQIAHHDVDVTAFGYAP 118
Cdd:PRK13374  45 NMFGftgtykGKKVSVMGHGMGIPSMVIYVHELIATFGVKNIIRVGSCGATQDDVKLMDVIIA-QGASTDSKTNRIRFSG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 119 GQVPRLAArFDSDERLVAAAEKAsaafdGAAVHRGLIVSGDQFVHSSEKT-AAIRKLfeDVRVVEMEAAAIAQTCVQLDV 197
Cdd:PRK13374 124 HDFAAIAD-YQLLEKAVETAREK-----GVPVKVGNVFSSDLFYDPDEDAiEAMERF--GILGVDMEVAGLYGLAAYLGA 195

                        170       180       190
                 ....*....|....*....|....*....|....
gi 490412629 198 PFVVIRAVSD-------LADEKADISFEEFLETA 224
Cdd:PRK13374 196 EALAILTVSDhiitgeeTTAEERQLSFNDMIEVA 229
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 12-235 5.43e-03

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: 37.08  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  12 VAVVGAMEQEIELLKNSLGNLEEKRF---GNFTFYCGMLGGKQVVLALSGIGkvnAAVSTALL-------VGKFnpdcvI 81
Cdd:cd09007    4 KCVLVFSGDLLEYLLEEYGAEKIGELssaGHTPLYRLEYDGEEVGVVGPPVG---APAAVLVLeelialgAKKF-----I 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629  82 NTGSAGGLCSGLKVGDVVV--------GTqiAHHdvdvtafgYAPgqvprlAARF-DSDERLVaaaEKASAAFD--GAAV 150
Cdd:cd09007   76 VVGSCGSLDPDLAVGDIILptsalrdeGT--SYH--------YLP------PSRYiEPDPELL---DALEEALEkaGIPY 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490412629 151 HRGLIVSGDQF----VhssEKTAAIRKlfEDVRVVEMEAAAIAQTCVQLDVPFVVIRAVSD-LADEKADISFEEFLETAS 225
Cdd:cd09007  137 VRGKTWTTDAPyretR---AKVARRRA--EGCLAVEMEAAALFAVAQFRGVELAQLLYVSDsLAGEEWDPRGRDEGKDAR 211

                        250
                 ....*....|
gi 490412629 226 VHSADMVKRI 235
Cdd:cd09007  212 EKALELALEA 221
 
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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