NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1470777144|gb|RHB80845|]
View 

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [Bifidobacterium pseudocatenulatum]

Protein Classification

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase( domain architecture ID 12963595)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 4-235 8.29e-71

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: 215.82  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLG-----GKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDTDMRLVGQwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:cd09008    76 GGLDPDLKIGDVVIATKVVYHDVDATAFGY-EGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470777144 164 KVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:cd09008   155 KKEELRENFPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGE----ADEDFEEFLELAAKNSAEVVLEL 222
 
Name Accession Description Interval E-value
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 4-235 8.29e-71

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: 215.82  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLG-----GKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDTDMRLVGQwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:cd09008    76 GGLDPDLKIGDVVIATKVVYHDVDATAFGY-EGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470777144 164 KVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:cd09008   155 KKEELRENFPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGE----ADEDFEEFLELAAKNSAEVVLEL 222
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-235 3.90e-62

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: 193.97  E-value: 3.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIETNkgtrvNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGI 82
Cdd:COG0775     2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGK-----EVVLVNSGIGKVNAATATTLLIARFRPDAVINTGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  83 AGNLNTHLHINDVVLGGTLRYLDTDMRLVGQWKPGTADQPVEeFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDP 162
Cdd:COG0775    77 AGGLDPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPAL-FEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1470777144 163 KKVEQVIRET-GADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDY-VEFKEFdISEYADTAAKIAVNIVKRM 235
Cdd:COG0775   156 EEKRRLRERFpGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKApNDFDEF-LEEAAKNAAELLRALLRKL 229
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
3-235 4.27e-53

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 170.69  E-value: 4.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGI 82
Cdd:PRK05584    2 KIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLH-----GHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  83 AGNLNTHLHINDVVLGGTLRYLDTDMRLVGqWKPG-TADQPVEeFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDD 161
Cdd:PRK05584   77 AGGLAPGLKVGDVVVADELVQHDVDVTAFG-YPYGqVPGLPAA-FKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1470777144 162 PKKVEQvIRET--GADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:PRK05584  155 AEKVAA-IRAEfpDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDE----AHVSFDEFLAVAAKYSANILKRM 225
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 3-233 7.50e-41

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: 139.40  E-value: 7.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITvteEAGVSVTRGTIETNKGTRVNVAATVGGMGTVNIA-ATTQHLIDADQPDAVIFSG 81
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET---PVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  82 IAGNLNTHLHINDVVLGGTLRYLDTDMRLVGQwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDD 161
Cdd:pfam01048  78 TAGGLNPDLKVGDVVIPTDAINHDGRSPLFGP-EGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1470777144 162 PKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDY-----VEFKEFDISEYADTAAKIAVNIVK 233
Cdd:pfam01048 157 TPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGAdgeltHEEVEEFAERAAERAAALLLALLA 233
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 4-235 4.45e-28

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: 106.34  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:TIGR01704   2 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLN---GTEVALLKS--GIGKVAAALGATLLLEHCKPDVIINTGSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDTDMRLVgQWKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:TIGR01704  77 GGLAPTLKVGDIVVSDEARYHDADVTAF-GYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1470777144 164 KVEQV-IRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTD-YVEFKEFdISEYADTAAKIAVNIVKRM 235
Cdd:TIGR01704 156 GLAKIrHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQsHLSFDEF-LAVAAKQSSLMVESLVQKL 228
 
Name Accession Description Interval E-value
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 4-235 8.29e-71

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: 215.82  E-value: 8.29e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAGRTFYEGTLG-----GKEVVLVQSGIGKVNAAIATQLLIDRFKPDAIINTGVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDTDMRLVGQwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:cd09008    76 GGLDPDLKIGDVVIATKVVYHDVDATAFGY-EGGQPPGMPAYFPADPELLELAKKAAKELGPKVHTGLIASGDQFVASSE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470777144 164 KVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:cd09008   155 KKEELRENFPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGE----ADEDFEEFLELAAKNSAEVVLEL 222
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 3-235 3.90e-62

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: 193.97  E-value: 3.90e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIETNkgtrvNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGI 82
Cdd:COG0775     2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFTFYLGTLGGK-----EVVLVNSGIGKVNAATATTLLIARFRPDAVINTGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  83 AGNLNTHLHINDVVLGGTLRYLDTDMRLVGQWKPGTADQPVEeFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDP 162
Cdd:COG0775    77 AGGLDPDLKIGDVVLATEVVQHDVDVTAFGYPRGQVPGMPAL-FEADPALLEAAKEAAKESGLKVVTGTIATGDRFVWSA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1470777144 163 KKVEQVIRET-GADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDY-VEFKEFdISEYADTAAKIAVNIVKRM 235
Cdd:COG0775   156 EEKRRLRERFpGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKApNDFDEF-LEEAAKNAAELLRALLRKL 229
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
3-235 4.27e-53

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 170.69  E-value: 4.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFSGI 82
Cdd:PRK05584    2 KIGIIGAMEEEVTLLLDKLENAQTITLAGREFYTGTLH-----GHEVVLVLSGIGKVAAALTATILIEHFKVDAVINTGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  83 AGNLNTHLHINDVVLGGTLRYLDTDMRLVGqWKPG-TADQPVEeFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDD 161
Cdd:PRK05584   77 AGGLAPGLKVGDVVVADELVQHDVDVTAFG-YPYGqVPGLPAA-FKADEKLVALAEKAAKELNLNVHRGLIASGDQFIAG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1470777144 162 PKKVEQvIRET--GADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:PRK05584  155 AEKVAA-IRAEfpDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDE----AHVSFDEFLAVAAKYSANILKRM 225
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 3-233 7.50e-41

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: 139.40  E-value: 7.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   3 TIAIIGAMDEEVANIASALSDITvteEAGVSVTRGTIETNKGTRVNVAATVGGMGTVNIA-ATTQHLIDADQPDAVIFSG 81
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDET---PVGPPSRGGKFYTGTLGGVPVVLVRHGIGPPNAAiLAAIRLLKEFGVDAIIRTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  82 IAGNLNTHLHINDVVLGGTLRYLDTDMRLVGQwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDD 161
Cdd:pfam01048  78 TAGGLNPDLKVGDVVIPTDAINHDGRSPLFGP-EGGPYFPDMAPAPADPELRALAKEAAERLGIPVHRGVYATGDGFYFE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1470777144 162 PKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDY-----VEFKEFDISEYADTAAKIAVNIVK 233
Cdd:pfam01048 157 TPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGAdgeltHEEVEEFAERAAERAAALLLALLA 233
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 4-228 1.95e-34

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: 122.40  E-value: 1.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGGFRFYRGTLG---GHPVVLVES--GMGKANAARAAQLLLEHFQPDLIISTGFA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDtdmrlvgqwkpGTADQPVEEfhsDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:cd17877    76 GGLDPGLAVGDLVIADRVLYHD-----------GDVPAGLEA---DEKLVALAEELAAGLNLKVHRGTIITVDAIVRKSA 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1470777144 164 KVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDY-VEFKEFDISEYADTAAKIA 228
Cdd:cd17877   142 EKAALAARFPALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELpFSIEEFLDEEGAVRPGAVL 207
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 1-235 4.72e-29

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 108.94  E-value: 4.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   1 MSTIAIIGAMDEEvanIASALSDITVTEE---AGVSVTRGTIetnKGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAV 77
Cdd:PRK14697    1 MNRIGIIGAMQIE---IDLLLEKLVVQEEqiiAGMPFYVGEF---MGTEVIVTRC--GVGKVNAAACTQTLIHKFDVDAI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  78 IFSGIAGNLNTHLHINDVVLGGTLRYLDTDMRLVGQWKPGTadqpvEEFHSDDRLIEVADKVLTDLSVHhIT---GIIAT 154
Cdd:PRK14697   73 INTGVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNLFPFQ-----EEFIASKELVELARKACNSSSLH-IEiheGRIVS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 155 GNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKR 234
Cdd:PRK14697  147 GECFVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDE----AQISYDDFAKTAANYCSEIIVE 222


                  .
gi 1470777144 235 M 235
Cdd:PRK14697  223 M 223
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 4-235 4.45e-28

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: 106.34  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:TIGR01704   2 IGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLN---GTEVALLKS--GIGKVAAALGATLLLEHCKPDVIINTGSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLNTHLHINDVVLGGTLRYLDTDMRLVgQWKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPK 163
Cdd:TIGR01704  77 GGLAPTLKVGDIVVSDEARYHDADVTAF-GYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1470777144 164 KVEQV-IRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTD-YVEFKEFdISEYADTAAKIAVNIVKRM 235
Cdd:TIGR01704 156 GLAKIrHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQsHLSFDEF-LAVAAKQSSLMVESLVQKL 228
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
 1-235 4.78e-25

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 102.01  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   1 MSTIAIIGAMDEEVANIasaLSDITVTEEAGVSVTRGTIETNKGTRVNVaaTVGGMGTVNIAATTQHLIDADQPDAVIFS 80
Cdd:PRK06698    1 MNRIGIIGAMQIEIDLL---LEKLIMQEEQIIAGMPFYVGEFMGTEVIV--TRCGVGKVNAAACTQTLIHKFDVDAIINT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  81 GIAGNLNTHLHINDVVLGGTLRYLDTDMRLVGQWKPGTadqpvEEFHSDDRLIEVADKVLTDLSVHHIT--GIIATGNYF 158
Cdd:PRK06698   76 GVAGGLHPDVKVGDIVISTNVTHHDVSKTQMKNLFPFQ-----EEFIASKELVELARKACNSSSLHMEIheGRIVSGECF 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1470777144 159 VDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDyvefKEFDISEYADTAAKIAVNIVKRM 235
Cdd:PRK06698  151 VEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDE----AQISYDDFAKTAANYCSEIIVEM 223
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 4-230 1.83e-20

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: 85.80  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEVANIASALSDITVTEE-AGVSVTRGTIetnKGTRVNVAAtvGGMGTVNIAATTQHLIDAdQPDAVIFSGI 82
Cdd:cd09005     1 YAIIPGDPERVDVIDSKLENPQKVSSfRGYTMYTGKY---NGKRVTVVN--GGMGSPSAAIVVEELCAL-GVDTIIRVGS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  83 AGNLNTHLHINDVVLGGTLRYLDTDMRLVGqwkpgtaDQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDP 162
Cdd:cd09005    75 CGALREDIKVGDLVIADGAIRGDGVTPYYV-------VGPPFAPEADPELTAALEEAAKELGLTVHVGTVWTTDAFYRET 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1470777144 163 KKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDYVEFKEFDISEYADTAAKIAVN 230
Cdd:cd09005   148 REESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGFVDEFLSEAEKKAIEIALD 215
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 48-208 2.18e-15

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: 71.80  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  48 NVAATVGGMGTVNIAATTQHLIDADqPDAVIFSGIAGNLNTHLHINDVVLGGTL----RYLDTDMRLVGqwkpgtadqpv 123
Cdd:cd17768    22 GLLVILSGAGPERARRAAERLLAAG-ARALISFGVAGGLDPALKPGDLVLPEAVvadgERYPTDPAWRR----------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 124 eefhsddRLIEVADKVLTdlsVHhiTGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSD 203
Cdd:cd17768    90 -------RLLRALPAGLR---VV--AGPLAGSDAPVLSVADKAALHAATGAVAVDMESGAVAAVAAEAGLPFAAIRAIAD 157


                  ....*
gi 1470777144 204 NADTD 208
Cdd:cd17768   158 PADRS 162
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 4-202 1.22e-14

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: 70.26  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   4 IAIIGAMDEEvaniasalSDITVTEEAGVSVTRGTIEtnkGTRVNVAatVGGMGTVNIAATTQHLIDADQPDAVIFSGIA 83
Cdd:cd17766     2 ILIVTAVPLE--------TNLERVEAEREAVLRGLLG---DQRVDVL--VAGVGPVNAAAATALLLERHPPDLVINAGIA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  84 GNLN-THLHINDVVLGGTLRYLDTDMRLVGQWKP------GTADQPVEEFHSDdrliEVADKVLTDLSVHHITGIIATGN 156
Cdd:cd17766    69 GAFPgSGLSVGDLVVASEEIAADLGVETPEGFLSldelgfGLLRIGTDPYLNR----FPLSALLLAAGLQVKTGPFLTVS 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1470777144 157 YFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALS 202
Cdd:cd17766   145 TVTGTAERAAELQRRFPAIAENMEGAAVAHAALLYGVPFLEIRGIS 190
HpnG TIGR03468
hopanoid-associated phosphorylase; The sequences in this family are members of the pfam01048 ...
 46-208 4.51e-13

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: 65.82  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  46 RVNVAATV----GGMGTVNIAATTQHLIDADQpDAVIFSGIAGNLNTHLHINDVVLGGTLRYldtdmrlvgqwkpgtadq 121
Cdd:TIGR03468  15 RIAAGPGLlvclSGGGPERARAAAARLMAAGA-AGLVSFGTAGALDPALQPGDLVVPEEVRA------------------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 122 PVEEFHSDDRLIEVADKVLTDLSVHHiTGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRAL 201
Cdd:TIGR03468  76 DGDRFPTDPAWRRRLLEALPAGLRVH-RGVLAASDTVVSTAAAKAALARATGAAAVDMESGAVAAVAAAAGLPFAVIRVI 154


                  ....*..
gi 1470777144 202 SDNADTD 208
Cdd:TIGR03468 155 SDPADRA 161
PNP_EcPNPI-like cd09006
purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas ...
 43-208 1.60e-09

purine nucleoside phosphorylases similar to Escherichia coli PNP-I (DeoD) and Trichomonas vaginalis PNP; Escherichia coli purine nucleoside phosphorylase (PNP)-I (or DeoD) accepts both 6-oxo and 6-amino purine nucleosides as substrates. Trichomonas vaginalis PNP has broad substrate specificity, having phosphorolytic catalytic activity with adenosine, inosine, and guanosine (with adenosine as the preferred substrate). This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350157  Cd Length: 228  Bit Score: 56.26  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  43 KGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIAGNLNTHLHINDVVLG-GTlrylDTDMRLVGQWKPGTADQ 121
Cdd:cd09006    50 KGKRVSVMGS--GMGMPSIGIYAYELFKFYGVKNIIRIGTCGAYQPDLKLRDVVLAmGA----STDSNYNRLRFGGGDFA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 122 PVeefhSDDRLIEVADKVLTDLSVHHITGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRAL 201
Cdd:cd09006   124 PI----ADFELLRKAVETAKELGIPVHVGNVFSSDVFYDDDPELWKKLKKYGVLAVEMEAAALYTNAARLGKKALAILTV 199


                  ....*..
gi 1470777144 202 SDNADTD 208
Cdd:cd09006   200 SDSLVTG 206
PRK05634 PRK05634
nucleosidase; Provisional
 55-206 5.36e-09

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 53.92  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  55 GMGTVNIA-ATTQHLIDADQ-PDAVIFSGIAGNLNTHLhindvvlggtlryldtdmrlVGQWKPGTADQpvEEFHSDdRL 132
Cdd:PRK05634   29 GIGKVAAAvALTRALARRGVlPPRVVNIGTAGALRDGL--------------------SGVFEPSHVIN--HDFSSD-LI 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1470777144 133 IEVADKVLTDLSVHHITG--IIATGNYFVDDPKKVEQVIRetGADAVEMEGAAVAHVAARNGLPVLVIRALSDNAD 206
Cdd:PRK05634   86 RALTGHPVANRLELPTGDgaVLATGDAFISDTATRDRLAQ--RADLVDMEGYAVAAVAAEFGVPCRLVKHVSDSAD 159
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 55-230 1.64e-08

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 53.25  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  55 GMGTVNIAATTQHLIDADQPDAVIFSGIAGNLNtHLHINDVVLGGTLRYLDTdmrlVGQWKPgTADQPVEEFHSDDRLIE 134
Cdd:PRK07164   53 GIGLINAALATQKLIEKYQIEIIINYGAVGSNI-NIDLGQVVYPEKFYLLDA----ITPWYP-PGQTPGEKEFYENNKIN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 135 VADKvltdlsvhhiTGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSD--NADTDYVef 212
Cdd:PRK07164  127 KNFN----------KIHLGSSNSFIFDLDKLKIIKDFIFVSFFDMEAFALAQVCFKNKVKFYCIKYVSDfiENNSDIE-- 194

                         170
                  ....*....|....*...
gi 1470777144 213 kefDISEYADTAAKIAVN 230
Cdd:PRK07164  195 ---IVNNNIKKGSKKALE 209
PRK06714 PRK06714
S-adenosylhomocysteine nucleosidase; Validated
 1-211 1.82e-08

S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 168652  Cd Length: 236  Bit Score: 53.39  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   1 MSTIAIIGAMDEEVANIASALSDITVTEEAGVSVTRGTIEtnkgtRVNVAATVGGMGTVNIAATTQHLIDADQPDAVIFS 80
Cdd:PRK06714    1 MKRIAIVAAWEPELTYLHQSYPSERIEKRAAWEFHFHTIN-----DLEIISVITGVGKVSCASCVQLLISEFQPDELFMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  81 GIAGNLNTHLHINDVVLGgtLRYLDTDMRlvgqwKPGTADQPVEEFHSDDRLIEVADKVLTDLSVHHITGIIATGNYFVD 160
Cdd:PRK06714   76 GICGSLSNKVKNGHIVVA--LNAIQHDVT-----AAGSGEDVFNLYNGRTAPIETTKSLVRRIKKIRSYDPIHFGTFLSG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1470777144 161 DPKKVEQVIRET-----GADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDYVE 211
Cdd:PRK06714  149 DQRIRSSEMRYLlhtvyGALAVDQEVAAFAYVCQINKKPFLCLKAASDQANDKTKE 204
PNP_ThPNP_like cd17765
purine nucleoside phosphorylases similar to Thermus thermophiles PNP; Purine nucleoside ...
 41-203 2.53e-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: 50.00  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  41 TNKGTRVNVAATvgGMGTVNIAATTQHLID--ADQpdaVIFSGIAGNLNTHLHINDVVLGGTLRYLDTDMRlvgQWKPGT 118
Cdd:cd17765    51 TYKGKPVSVQTT--GMGCPSAAIVVEELAQlgVKR---LIRVGTCGGLSSGLQLGDLIVATAAVPADGTTR---ALLGGE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 119 ADQPVEEFhsddRLIEVADKVLTDLSVHHITGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVI 198
Cdd:cd17765   123 PYAPAADF----ELVEALYRAARAAGMPVHVGPVATSDLFYDPTPDGVKRWRRRGVLAVEMEASALFTLAALRGLRAGCI 198


                  ....*
gi 1470777144 199 RALSD 203
Cdd:cd17765   199 LTVSD 203
DeoD COG0813
Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside ...
 43-202 2.68e-07

Purine-nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine-nucleoside phosphorylase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440575  Cd Length: 236  Bit Score: 49.73  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  43 KGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIAGNLNTHLHINDVVLGgtlRYLDTDMRLVGQWKPGTADQP 122
Cdd:COG0813    54 KGKRVSVMGS--GMGIPSISIYAYELITEYGVKNIIRVGTCGALQEDVKVRDVVIA---MGASTDSNVNRQRFGGGDFAP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 123 VEEFHSDDRLIEVADKvlTDLSVHhiTGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGlpvlvIRALS 202
Cdd:COG0813   129 IADFELLRKAVEAAKE--LGIKVH--VGNVFSSDLFYREDPDLLEKLAKYGVLAVEMEAAALYTLAAKYG-----KRALA 199
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 2-215 5.86e-07

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 48.85  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144   2 STIAIIGAMDEEVANIASALsDITVTEEA----GVS--VTRGTIetnKGTRVNV-------AATVGGMGTVNIAATTQHL 68
Cdd:PLN02584    9 STVLIVIAMQAEAMPLVNAL-GLVEDVDSpfpkGVPwvRYSGTH---KGLRVHVvcpgkdkALGVDSVGTVPASLVTYAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  69 IDADQPDAVIFSGIAGNLNTH-LHINDVVLGGTLRYldTDMRLvgqwkpgtadqPVEEFhsDDRLIEVADKVLTDLSVHH 147
Cdd:PLN02584   85 IQALKPDLIINAGTAGGFKAKgAAIGDVFLATAVAN--HDRRI-----------PIPVF--DKYGVGTRDAFPTPNLIKA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1470777144 148 I---TGIIATGNYfVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNADTDYVEFKEF 215
Cdd:PLN02584  150 LglkEGVLSTGNS-LDMTEQDEESIKANDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDGDKPTAEEF 219
AMN cd17762
AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate ...
 55-194 2.81e-06

AMP nucleosidase; AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to ribose 5-phosphate and adenine. It is a prokaryotic enzyme which plays a role in purine nucleoside salvage and intracellular AMP level regulation. AMN is active as a homohexamer; each monomer is comprised of a catalytic domain and a putative regulatory domain. This model represents the catalytic domain. AMN 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: 350162  Cd Length: 242  Bit Score: 46.78  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  55 GMGTVNiAATTQHLIDADQPDAVIFSGIAGNLNTHLHINDVVLG-------GTLR-YLDtdmrlvgQWKPGTADQPVEEF 126
Cdd:cd17762    67 GVGSPN-AATITDLLAVLRPKAVLMLGHCGGLRNSQEIGDFVLPiaairgeGTSDdYLP-------PEVPALPSFELQRA 138

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1470777144 127 HSDdrlievadkVLTDLSVHHITGIIATGNY----FVDDPKKveqVIRETGADAVEMEGAAVAHVAARNGLP 194
Cdd:cd17762   139 LSD---------ALREVGLDYRTGTVYTTDRrnweFDEAFKE---YLRESRAIAIDMESATIFAVGFANRVP 198
deoD PRK05819
DeoD-type purine-nucleoside phosphorylase;
41-204 2.03e-05

DeoD-type purine-nucleoside phosphorylase;


Pssm-ID: 180275  Cd Length: 235  Bit Score: 44.08  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  41 TNKGTRVNVAATvgGMGTVNIAATTQHLIDADQPDAVIFSGIAGNLNTHLHINDVVLGGTLrylDTDMRLV-GQWKPGTA 119
Cdd:PRK05819   51 TYKGKRVSVMGT--GMGIPSISIYANELITDYGVKKLIRVGSCGALQEDVKVRDVVIAMGA---STDSNVNrIRFKGHDF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 120 dQPVEEFHSDDRLIEVADKVltDLSVHhiTGIIATGNYFVDDPKKVEQVIRETGADAVEMEGAAVAHVAARNGLPVLVIR 199
Cdd:PRK05819  126 -APIADFDLLRKAYDAAKEK--GITVH--VGNVFSADLFYNPDPEMFDVLEKYGVLGVEMEAAALYGLAAKYGVKALTIL 200


                  ....*
gi 1470777144 200 ALSDN 204
Cdd:PRK05819  201 TVSDH 205
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 77-231 1.21e-04

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


Pssm-ID: 350158 [Multi-domain]  Cd Length: 221  Bit Score: 41.70  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144  77 VIFSGIAGNLNTHLHINDVVL-GGTLR-------YLDtdmrlvgqwkpgtadqPVEEFHSDDRLIEVADKVLTDLSVHHI 148
Cdd:cd09007    74 FIVVGSCGSLDPDLAVGDIILpTSALRdegtsyhYLP----------------PSRYIEPDPELLDALEEALEKAGIPYV 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1470777144 149 TGIIATgnyfvDD------PKKVEQVIREtGADAVEMEGAAVAHVAARNGLPVLVIRALSDN-ADTDYVEFKEFDISEYA 221
Cdd:cd09007   138 RGKTWT-----TDapyretRAKVARRRAE-GCLAVEMEAAALFAVAQFRGVELAQLLYVSDSlAGEEWDPRGRDEGKDAR 211

                         170
                  ....*....|
gi 1470777144 222 DTAAKIAVNI 231
Cdd:cd09007   212 EKALELALEA 221
PRK07077 PRK07077
phosphorylase;
170-206 1.59e-03

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 38.48  E-value: 1.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1470777144 170 RETGADAVEMEGAAVAHVAARNGLPVLVIRALSDNAD 206
Cdd:PRK07077  134 RATGALAVDMESHIAAAFAAARGLPFAACRVIVDPAW 170
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH