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Conserved domains on  [gi|1372234963|ref|WP_107005130|]
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MULTISPECIES: purine-nucleoside phosphorylase [Shewanella]

Protein Classification

purine-nucleoside phosphorylase( domain architecture ID 10014215)

purine-nucleoside phosphorylase catalyzes the phosphorolysis of purine nucleoside to form the corresponding free purine base and pentose-1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-232 2.36e-155

DeoD-type purine-nucleoside phosphorylase;


:

Pssm-ID: 237368  Cd Length: 233  Bit Score: 430.29  E-value: 2.36e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:PRK13374    2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:PRK13374   82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:PRK13374  162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
 
Name Accession Description Interval E-value
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-232 2.36e-155

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 430.29  E-value: 2.36e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:PRK13374    2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:PRK13374   82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:PRK13374  162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
1-232 1.31e-144

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: 402.96  E-value: 1.31e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:COG0813     2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:COG0813    82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:COG0813   162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAA 233
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
4-231 9.79e-137

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: 382.91  E-value: 9.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVE 83
Cdd:cd09006     1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPD 163
Cdd:cd09006    81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372234963 164 EDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAV 231
Cdd:cd09006   161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
4-229 2.32e-103

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: 298.61  E-value: 2.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVE 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPD 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372234963 164 EDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLAL 229
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILAL 226
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
14-232 9.66e-31

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: 113.21  E-value: 9.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  14 KTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSM-VLYGHELINDFGVERIIRVGSLG 92
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAaILAAIRLLKEFGVDAIIRTGTAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  93 ATQRQVQMRDVILAQAA----GTDSVTNAKRSAGY--HMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPDEDL 166
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAinhdGRSPLFGPEGGPYFpdMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372234963 167 IPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHC--LTGEETSAEERQLSFNQMISLALAVA 232
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAagGADGELTHEEVEEFAERAAERAAALL 228
 
Name Accession Description Interval E-value
PRK13374 PRK13374
DeoD-type purine-nucleoside phosphorylase;
1-232 2.36e-155

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 237368  Cd Length: 233  Bit Score: 430.29  E-value: 2.36e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:PRK13374    2 STPHINAQPGDFAETVLMPGDPLRAKYIAETYLEDVVQVTDVRNMFGFTGTYKGKKVSVMGHGMGIPSMVIYVHELIATF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:PRK13374   82 GVKNIIRVGSCGATQDDVKLMDVIIAQGASTDSKTNRIRFSGHDFAAIADYQLLEKAVETAREKGVPVKVGNVFSSDLFY 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:PRK13374  162 DPDEDAIEAMERFGILGVDMEVAGLYGLAAYLGAEALAILTVSDHIITGEETTAEERQLSFNDMIEVALETA 233
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
1-232 1.31e-144

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: 402.96  E-value: 1.31e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:COG0813     2 MTPHIGAKKGDIAETVLLPGDPLRAKYIAETFLEDAVLVNEVRGMLGYTGTYKGKRVSVMGSGMGIPSISIYAYELITEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:COG0813    82 GVKNIIRVGTCGALQEDVKVRDVVIAMGASTDSNVNRQRFGGGDFAPIADFELLRKAVEAAKELGIKVHVGNVFSSDLFY 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:COG0813   162 REDPDLLEKLAKYGVLAVEMEAAALYTLAAKYGKRALAILTVSDHLVTGEETTAEERQTTFNDMMEIALEAA 233
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
4-231 9.79e-137

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: 382.91  E-value: 9.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVE 83
Cdd:cd09006     1 HIEAKKGDIAKTVLMPGDPLRAKYIAETFLEDAKLVNSVRNMLGYTGTYKGKRVSVMGSGMGMPSIGIYAYELFKFYGVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPD 163
Cdd:cd09006    81 NIIRIGTCGAYQPDLKLRDVVLAMGASTDSNYNRLRFGGGDFAPIADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372234963 164 EDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAV 231
Cdd:cd09006   161 PELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTVSDSLVTGEELSAEERETSFTNMIELALET 228
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
1-232 6.59e-131

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 368.42  E-value: 6.59e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDF 80
Cdd:PRK05819    1 MTPHINAKKGDIADTVLMPGDPLRAKYIAETFLEDVVCVNEVRGMLGFTGTYKGKRVSVMGTGMGIPSISIYANELITDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:PRK05819   81 GVKKLIRVGSCGALQEDVKVRDVVIAMGASTDSNVNRIRFKGHDFAPIADFDLLRKAYDAAKEKGITVHVGNVFSADLFY 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLALAVA 232
Cdd:PRK05819  161 NPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTILTVSDHIVTGEATTAEERQTTFNDMIEIALESA 232
deoD TIGR00107
purine-nucleoside phosphorylase, family 1 (deoD); Purine nucleoside phosphorylase (also called ...
4-229 2.32e-103

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: 298.61  E-value: 2.32e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVE 83
Cdd:TIGR00107   1 HINAKKGDIADVVLMPGDPLRAKYIAETFLEDVREVNEVRGMLGFTGTYKGKKISVMGHGMGIPSISIYVYELIKFYEVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPD 163
Cdd:TIGR00107  81 TIIRVGSCGAIRPDVKLRDVIIAMGASTDSKYNRVRFVEVDFAAIADFELVENAYDAAKAKGVDVHVGNVFSADAFYQPD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1372234963 164 EDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLAL 229
Cdd:TIGR00107 161 KDVFDLMAKYGILGVEMEAAALYANAAELGAKALTILTVSDHLVTHEATTAEERQTTFKDMIILAL 226
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
1-232 1.63e-71

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: 217.94  E-value: 1.63e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   1 MTAHINAAKGDFAKTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELInDF 80
Cdd:cd17765     1 MPIHIRAEPGDVAEAVLLPGDPGRATYIAETFFDGPRLYNDHRGLLGYTGTYKGKPVSVQTTGMGCPSAAIVVEELA-QL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  81 GVERIIRVGSLGATQRQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:cd17765    80 GVKRLIRVGTCGGLSSGLQLGDLIVATAAVPADGTTRALLGGEPYAPAADFELVEALYRAARAAGMPVHVGPVATSDLFY 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1372234963 161 DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEET-SAEERQLSFNQMISLALAVA 232
Cdd:cd17765   160 DPTPDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCILTVSDLIGDPERRiDDEELRAGVDRMTEVALEAV 232
Udp COG2820
Uridine phosphorylase [Nucleotide transport and metabolism]; Uridine phosphorylase is part of ...
4-229 4.01e-56

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


Pssm-ID: 442068  Cd Length: 251  Bit Score: 179.21  E-value: 4.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHFlEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINdFGVE 83
Cdd:COG2820    13 HLGLKPGDVADYVILPGDPGRVELIASYL-DDVELVAENREFRTYTGTYKGKRITVISTGIGGPSAAIAVEELAA-LGAK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAA-GTDSVTNAKRSAGYhmPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDP 162
Cdd:COG2820    91 TFIRVGTSGALQPDIPVGDLVIATGAvRLDGTSNFYAPAEY--PAVADFELTRALVEAAEELGVDYHVGITASTDGFYAE 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234963 163 DE----------DLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERqlSFNQMISLAL 229
Cdd:COG2820   169 QGrelrvdpdldEKLEAWRKLGVLNVEMETAALFTLARLRGHRAGSVLAVSANRVTGEFSKDPEE--AVERAIKVAL 243
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
4-229 1.26e-52

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: 169.93  E-value: 1.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDFAKTVIMPGDPLRAKYIAEHfLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINdFGVE 83
Cdd:cd17767     2 HIGLKPGDVAPYVLLPGDPGRVERIAEL-LDDAEEVADNREYRTYTGTYKGVPVSVCSTGIGGPSAAIAVEELAQ-LGAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  84 RIIRVGSLGATQRQVQMRDVILAQAA-GTDSVTNAKRSAGYhmPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY-- 160
Cdd:cd17767    80 TFIRVGTCGALQPDIKLGDLVIATGAvRDEGTSKHYVPPEY--PAVADPEVVLALVEAAEELGVPYHVGITASKDSFYgg 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372234963 161 ---------DPDEDLIPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQLSFNQMISLAL 229
Cdd:cd17767   158 qgrpgpglpPELPELLEEWQRAGVLNSEMESAALFTLASLRGVRAGAVLAVVGNRVTDEAPDEEDVAAGEERAIRVAL 235
MTAP_SsMTAPI_like cd17764
5'-deoxy-5'-methylthioadenosine phosphorylases similar to Sulfolobus solfataricus MTAPI; 5 ...
14-219 2.63e-45

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: 150.45  E-value: 2.63e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  14 KTVIMPGDPLRAKYIAEHfLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINdFGVERIIRVGSLGA 93
Cdd:cd17764     1 ERVIAVGDPGRVELLSTL-LEDPRLVNENRGLLVYTGKYKGEEVTIATHGIGGPSAAIVFEELIM-LGAKVIIRLGTAGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  94 TQRQVQMRDVILAQAAG-TDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPDEDLIPALER 172
Cdd:cd17764    79 LVPELRVGDIVVATGASyYPGGGLGQYFPDVCPPASPDPELTLELVESLSKRGLKYYVGPVFSSDAFYAEDEEFAERWSS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1372234963 173 FGILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEERQL 219
Cdd:cd17764   159 LGFIAVEMECATLFTLGWLRGVKAGAVLVVSDNLVKGGKLMLTKEEL 205
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
16-230 3.27e-44

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: 147.44  E-value: 3.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  16 VIMPGDPLRAKYIAEHfLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINdFGVERIIRVGSLGATQ 95
Cdd:cd09005     2 AIIPGDPERVDVIDSK-LENPQKVSSFRGYTMYTGKYNGKRVTVVNGGMGSPSAAIVVEELCA-LGVDTIIRVGSCGALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  96 RQVQMRDVILAQAAGTDSVTNAKRSAGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPDEDLIPALERFGI 175
Cdd:cd09005    80 EDIKVGDLVIADGAIRGDGVTPYYVVGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRETREESEKLRKLGA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1372234963 176 LGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGE-ETSAEERQLSFNQMISLALA 230
Cdd:cd09005   160 LAVEMETSALATLAHLRGVKAASILAVSDNLITGEiGFVDEFLSEAEKKAIEIALD 215
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
14-232 9.66e-31

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: 113.21  E-value: 9.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  14 KTVIMPGDPLRAKYIAEHFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSM-VLYGHELINDFGVERIIRVGSLG 92
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAaILAAIRLLKEFGVDAIIRTGTAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  93 ATQRQVQMRDVILAQAA----GTDSVTNAKRSAGY--HMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYDPDEDL 166
Cdd:pfam01048  81 GLNPDLKVGDVVIPTDAinhdGRSPLFGPEGGPYFpdMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFETPAE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372234963 167 IPALERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHC--LTGEETSAEERQLSFNQMISLALAVA 232
Cdd:pfam01048 161 IRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAagGADGELTHEEVEEFAERAAERAAALL 228
NP_TgUP-like cd17769
nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily ...
15-192 1.06e-15

nucleoside phosphorylases similar to Toxoplasma gondii uridine phosphorylase; This subfamily is composed of mostly uncharacterized proteins with similarity to Toxoplasma gondii uridine phosphorylase (TgUPase). Toxoplasma gondii appears to have a single non-specific uridine phosphorylase which catalyzes the reversible phosphorolysis of uridine, deoxyuridine and thymidine, rather than the two distinct enzymes of mammalian cells: uridine phosphorylase (nucleoside phosphorylase-I family) and thymidine phosphorylase (nucleoside phosphorylase-II family). TgUPase is a potential target for intervention against toxoplasmosis. It belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350169  Cd Length: 255  Bit Score: 73.77  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  15 TVimpGDPLRAKYIAEHFLEDA--RVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMvlyghelinDFGVeR-------- 84
Cdd:cd17769     5 TV---GDPARARLIAKLLDKEPkvFELTSERGFLTITGRYKGVPVSIVAIGMGAPMM---------DFFV-Rearavvdg 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  85 ---IIRVGSLGATQRQVQMRDVILAQAA---------GTDSVTNAKRSAGYHM--PTSASFPL--LLKAWEQAKAQGLSV 148
Cdd:cd17769    72 pmaIIRLGSCGSLDPDVPVGSVVVPSASvavtrnyddDDFAGPSTSSEKPYLIskPVPADPELseLLESELKASLGGEVV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234963 149 RVGNVFSGDLYY-----------DPDEDLIP-ALERF-GILGIDMEVAGLYGLAQQF 192
Cdd:cd17769   152 VEGLNASADSFYssqgrqdpnfpDHNENLIDkLLKRYpGAASLEMETFHLFHLARCS 208
PRK11178 PRK11178
uridine phosphorylase; Provisional
4-196 3.67e-13

uridine phosphorylase; Provisional


Pssm-ID: 183018  Cd Length: 251  Bit Score: 66.60  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963   4 HINAAKGDF--AKTVIMPGDPLRAKYIAEhFLEDARVVTSVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELiNDFG 81
Cdd:PRK11178    6 HLGLTKADLqgATLAIVPGDPERVEKIAA-LMDNPVFLASHREFTSWRAELDGKPVIVCSTGIGGPSTSIAVEEL-AQLG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  82 VERIIRVGSLGATQRQVQMRDVILAQAAgtDSVTNAKRS-AGYHMPTSASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYY 160
Cdd:PRK11178   84 VRTFLRIGTTGAIQPHINVGDVLVTTAS--VRLDGASLHfAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFY 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234963 161 dpdedliPALERF---------------------GILGIDMEVAGLYGLAQQFGIEA 196
Cdd:PRK11178  162 -------PGQERYdtysgrvvrrfkgsmeewqamGVMNYEMESATLLTMCASQGLRA 211
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
12-231 5.91e-11

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: 59.80  E-value: 5.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  12 FAKTVIMP--GDPLRakYIAEHFleDARVVTSVRNMLG---YTGSWQGKPVSVMGHGMGIPSMVLYGHELInDFGVERII 86
Cdd:cd09007     1 LPEKCVLVfsGDLLE--YLLEEY--GAEKIGELSSAGHtplYRLEYDGEEVGVVGPPVGAPAAVLVLEELI-ALGAKKFI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  87 RVGSLGATQRQVQMRDVILaqaagtdsVTNAKRSAG--YH-MPTS----ASFPLLLKAWEQAKAQGLSVRVGNVFSGDLY 159
Cdd:cd09007    76 VVGSCGSLDPDLAVGDIIL--------PTSALRDEGtsYHyLPPSryiePDPELLDALEEALEKAGIPYVRGKTWTTDAP 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234963 160 YDPDEDLIpalERF---GILGIDMEVAGLYGLAQQFGIEALAILTVSD--HCLTGEETSAEERQLSFNQMISLALAV 231
Cdd:cd09007   148 YRETRAKV---ARRraeGCLAVEMEAAALFAVAQFRGVELAQLLYVSDslAGEEWDPRGRDEGKDAREKALELALEA 221
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
25-216 3.12e-09

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: 55.20  E-value: 3.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  25 AKYIAEHfLEDARVVTsVRNMLGYTGSWQGKPVSVMGHGMGipsMV---LYGHELINDFGVERIIRVGSLGATQRQVQMR 101
Cdd:cd09008    11 IAPLLEL-LENVEEET-IAGRTFYEGTLGGKEVVLVQSGIG---KVnaaIATQLLIDRFKPDAIINTGVAGGLDPDLKIG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963 102 DVILA-QAAGTDSVTNAKRSAGYHMPT-SASFP----LLLKAWEQAKAQGLSVRVGNVFSGDLYYDpDEDLIPAL-ERFG 174
Cdd:cd09008    86 DVVIAtKVVYHDVDATAFGYEGGQPPGmPAYFPadpeLLELAKKAAKELGPKVHTGLIASGDQFVA-SSEKKEELrENFP 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1372234963 175 ILGIDMEVAGLYGLAQQFGIEALAILTVSDHCLTGEETSAEE 216
Cdd:cd09008   165 ALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEE 206
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
25-232 1.15e-08

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: 53.76  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  25 AKYIAEHfLEDARVVTsVRNMLGYTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVERIIRVGSLGATQRQVQMRDVI 104
Cdd:COG0775    13 VAALLEA-LEDKKEVQ-IAGFTFYLGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGGLDPDLKIGDVV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963 105 LAQAA---GTDsVTNAKRSAGYHMPTSASFP----LLLKAWEQAKAQGLSVRVGNVFSGDLYYDPDEDLIPALERF-GIL 176
Cdd:COG0775    91 LATEVvqhDVD-VTAFGYPRGQVPGMPALFEadpaLLEAAKEAAKESGLKVVTGTIATGDRFVWSAEEKRRLRERFpGAL 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1372234963 177 GIDMEVAGLYGLAQQFGIEALAILTVSDHCltGEETSAEerqlsFNQMISLALAVA 232
Cdd:COG0775   170 AVDMEGAAIAQVCYRFGVPFLVIRAISDLA--GEKAPND-----FDEFLEEAAKNA 218
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
48-216 1.51e-06

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: 47.29  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  48 YTGSWQGKPVSVMGHGMGIPSMVLYGHELINDFGVERIIRVGSLGATQRQVQMRDVILAqaagtDSVTNAkrSAGYHMPT 127
Cdd:cd17877    32 YRGTLGGHPVVLVESGMGKANAARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIA-----DRVLYH--DGDVPAGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963 128 SASFPLLLKAWEQAKAQGLSVRVGNVFSGDLYYdPDEDLIPAL-ERFGILGIDMEVAGLYGLAQQFGIEALAILTVSDHC 206
Cdd:cd17877   105 EADEKLVALAEELAAGLNLKVHRGTIITVDAIV-RKSAEKAALaARFPALAVDMESAAIAQVAAARGIPFLAIRAISDPA 183
                         170
                  ....*....|
gi 1372234963 207 LTGEETSAEE 216
Cdd:cd17877   184 DEELPFSIEE 193
euk_UDPppase TIGR01719
uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine ...
10-92 3.02e-03

uridine phosphorylase; This model represents a clade of mainly eucaryotic uridine phosphorylases. Genes from human and mouse have been characterized. This enzyme is a member of the PHP/UDP subfamily (pfam01048) and is closely related to the bacterial uridine (TIGR01718) and inosine (TIGR00107) phosphorylase equivalogs. In addition to the eukaryotes, a gene from Mycobacterium leprae is included in this equivalog and may have resulted from lateral gene transfer. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130780 [Multi-domain]  Cd Length: 287  Bit Score: 37.82  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234963  10 GDfAKTVIMPGDPLRAKYIAEHFLEDARV--VTSVRNM--------LGYTGswqgkPVSVMGHGMGIPSMVLYGHELIND 79
Cdd:TIGR01719  29 GD-VKFVCMGGTPSRMKAFARYVGAELGLscGRDYPNIsergdrfaMYKVG-----PVLCVSHGMGIPSISIMLHELIKL 102
                          90
                  ....*....|....*...
gi 1372234963  80 FGVER-----IIRVGSLG 92
Cdd:TIGR01719 103 LYYARcknptFIRIGTSG 120
 
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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