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Conserved domains on  [gi|1063726842|ref|NP_001329683|]
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Phosphorylase superfamily protein [Arabidopsis thaliana]

Protein Classification

nucleoside phosphorylase-I family protein( domain architecture ID 762)

nucleoside phosphorylase-I family protein

CATH:  3.40.50.1580
PubMed:  11743878
SCOP:  4000573

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NP-I super family cl00303
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 6-189 4.68e-121

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.


The actual alignment was detected with superfamily member PLN02584:

Pssm-ID: 444819  Cd Length: 249  Bit Score: 342.37  E-value: 4.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842   6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584    1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584   81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160

                         170       180
                  ....*....|....*....|....
gi 1063726842 166 DSMDMSPHDEESITANDATVKDME 189
Cdd:PLN02584  161 NSLDMTEQDEESIKANDATVKDME 184
 
Name Accession Description Interval E-value
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 6-189 4.68e-121

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 342.37  E-value: 4.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842   6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584    1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584   81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160

                         170       180
                  ....*....|....*....|....
gi 1063726842 166 DSMDMSPHDEESITANDATVKDME 189
Cdd:PLN02584  161 NSLDMTEQDEESIKANDATVKDME 184
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 16-189 4.49e-23

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: 91.79  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQP 95
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAG-----RTFYEGTLGGKEVVLVQSG---------IGKVNAAIATQLLIDRFKP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  96 DLIINAGTAGGFKaKGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLST 164
Cdd:cd09008    67 DAIINTGVAGGLD-PDLKIGDVVIATKVVYHDVDATAFGYEGGQPpGMPAYFPAdPELLElakkaakelGPKVHTGLIAS 145

                         170       180
                  ....*....|....*....|....*.
gi 1063726842 165 GDSMDMSPHDEESITAN-DATVKDME 189
Cdd:cd09008   146 GDQFVASSEKKEELRENfPALAVEME 171
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 15-189 2.51e-17

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: 76.49  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  15 TIVFIVAMQKEAQPLINRLRLVEEVNTPFPKevtwiMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQ 94
Cdd:COG0775     2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFT-----FYLGTLGGKEVVLVNSG---------IGKVNAATATTLLIARFR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  95 PDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLS 163
Cdd:COG0775    68 PDAVINTGVAGGLDP-DLKIGDVVLATEVVQHDVDVTAFGYPRGQVpGMPALFEAdPALLEaakeaakesGLKVVTGTIA 146

                         170       180
                  ....*....|....*....|....*...
gi 1063726842 164 TGDSMDMSPHDEESI--TANDATVKDME 189
Cdd:COG0775   147 TGDRFVWSAEEKRRLreRFPGALAVDME 174
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 15-190 9.39e-15

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: 69.68  E-value: 9.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  15 TIVFIVAMQKEAQPLINRLRLVEEVntpFPKEVTWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLV-TYASILAI 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPV---GPPSRGGKFYTGTLGGVPVVLVRHG---------IGPPNAAILaAIRLLKEF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  94 QPDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIP--VPVLDIYGVGMRNTFPTPNLIKEL---------NLKVGRL 162
Cdd:pfam01048  69 GVDAIIRTGTAGGLNP-DLKVGDVVIPTDAINHDGRSPlfGPEGGPYFPDMAPAPADPELRALAkeaaerlgiPVHRGVY 147

                         170       180
                  ....*....|....*....|....*....
gi 1063726842 163 STGDSMDMSPHDEESITAND-ATVKDMEV 190
Cdd:pfam01048 148 ATGDGFYFETPAEIRLLRRLgADAVEMET 176
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 67-189 6.93e-04

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: 39.32  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  67 GKDSTLGVESVGTVPASLVTYASILAIQPDLIINAGTAGGFKaKGACISDVYVVSTVAFHDrrIPVPVLDiYGVGMRNTF 146
Cdd:TIGR01704  39 GTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA-PTLKVGDIVVSDEARYHD--ADVTAFG-YEYGQLPGC 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063726842 147 P------------TPNLIKELNLKV--GRLSTGDSMDMSPHDEESITA--NDATVKDME 189
Cdd:TIGR01704 115 PagfkaddkliaaAEACIAELNLNAvrGLIVSGDAFINGSVGLAKIRHnfPQAIAVEME 173
 
Name Accession Description Interval E-value
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 6-189 4.68e-121

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 342.37  E-value: 4.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842   6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584    1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584   81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160

                         170       180
                  ....*....|....*....|....
gi 1063726842 166 DSMDMSPHDEESITANDATVKDME 189
Cdd:PLN02584  161 NSLDMTEQDEESIKANDATVKDME 184
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 16-189 4.49e-23

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: 91.79  E-value: 4.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQP 95
Cdd:cd09008     1 IGIIGAMEEEIAPLLELLENVEEETIAG-----RTFYEGTLGGKEVVLVQSG---------IGKVNAAIATQLLIDRFKP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  96 DLIINAGTAGGFKaKGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLST 164
Cdd:cd09008    67 DAIINTGVAGGLD-PDLKIGDVVIATKVVYHDVDATAFGYEGGQPpGMPAYFPAdPELLElakkaakelGPKVHTGLIAS 145

                         170       180
                  ....*....|....*....|....*.
gi 1063726842 165 GDSMDMSPHDEESITAN-DATVKDME 189
Cdd:cd09008   146 GDQFVASSEKKEELRENfPALAVEME 171
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 15-189 2.51e-17

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: 76.49  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  15 TIVFIVAMQKEAQPLINRLRLVEEVNTPFPKevtwiMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQ 94
Cdd:COG0775     2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFT-----FYLGTLGGKEVVLVNSG---------IGKVNAATATTLLIARFR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  95 PDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLS 163
Cdd:COG0775    68 PDAVINTGVAGGLDP-DLKIGDVVLATEVVQHDVDVTAFGYPRGQVpGMPALFEAdPALLEaakeaakesGLKVVTGTIA 146

                         170       180
                  ....*....|....*....|....*...
gi 1063726842 164 TGDSMDMSPHDEESI--TANDATVKDME 189
Cdd:COG0775   147 TGDRFVWSAEEKRRLreRFPGALAVDME 174
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 15-190 9.39e-15

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: 69.68  E-value: 9.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  15 TIVFIVAMQKEAQPLINRLRLVEEVntpFPKEVTWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLV-TYASILAI 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPV---GPPSRGGKFYTGTLGGVPVVLVRHG---------IGPPNAAILaAIRLLKEF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  94 QPDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIP--VPVLDIYGVGMRNTFPTPNLIKEL---------NLKVGRL 162
Cdd:pfam01048  69 GVDAIIRTGTAGGLNP-DLKVGDVVIPTDAINHDGRSPlfGPEGGPYFPDMAPAPADPELRALAkeaaerlgiPVHRGVY 147

                         170       180
                  ....*....|....*....|....*....
gi 1063726842 163 STGDSMDMSPHDEESITAND-ATVKDMEV 190
Cdd:pfam01048 148 ATGDGFYFETPAEIRLLRRLgADAVEMET 176
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 16-189 4.41e-08

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: 51.14  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKdlninivcpGKDSTLGVESVGTVPASLVTYASILAIQP 95
Cdd:cd17877     1 IGIIAAMPEEISPLLRRIEVLQKVRLGG-----FRFYRGTLG---------GHPVVLVESGMGKANAARAAQLLLEHFQP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  96 DLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLikELNLKVGRLSTGDSMDMSPHDE 175
Cdd:cd17877    67 DLIISTGFAGGLDP-GLAVGDLVIADRVLYHDGDVPAGLEADEKLVALAEELAAGL--NLKVHRGTIITVDAIVRKSAEK 143

                         170
                  ....*....|....*
gi 1063726842 176 ESITA-NDATVKDME 189
Cdd:cd17877   144 AALAArFPALAVDME 158
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
15-167 3.59e-06

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 45.88  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  15 TIVFIVAMQKEAQPLINRLRLVEEV---NTPFpkevtwimFKGMYKdlninivcpGKDSTLGVESVGTVPASLVTYASIL 91
Cdd:PRK05584    2 KIGIIGAMEEEVTLLLDKLENAQTItlaGREF--------YTGTLH---------GHEVVLVLSGIGKVAAALTATILIE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  92 AIQPDLIINAGTAGGFkAKGACISDVYVVSTVAFHD--------RRIPVPVLDIYgvgmrntFPT-PNLIK--------- 153
Cdd:PRK05584   65 HFKVDAVINTGVAGGL-APGLKVGDVVVADELVQHDvdvtafgyPYGQVPGLPAA-------FKAdEKLVAlaekaakel 136

                         170
                  ....*....|....
gi 1063726842 154 ELNLKVGRLSTGDS 167
Cdd:PRK05584  137 NLNVHRGLIASGDQ 150
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 52-164 5.23e-06

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: 45.22  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  52 FKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTV-------- 123
Cdd:cd17766    25 LRGLLGDQRVDVLVAG---------VGPVNAAAATALLLERHPPDLVINAGIAGAFPGSGLSVGDLVVASEEiaadlgve 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063726842 124 ---AFHD-RRIPVPVLDIYGVGMRNTFPT--PNLIKELNLKVGRLST 164
Cdd:cd17766    96 tpeGFLSlDELGFGLLRIGTDPYLNRFPLsaLLLAAGLQVKTGPFLT 142
PRK05634 PRK05634
nucleosidase; Provisional
 77-189 3.32e-04

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 39.67  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  77 VGTVPASlVTYASILA---IQPDLIINAGTAGGFKAKgacISDVYVVSTVAFHDrrIPVPVL-DIYGvgmrntFPTPNLI 152
Cdd:PRK05634   30 IGKVAAA-VALTRALArrgVLPPRVVNIGTAGALRDG---LSGVFEPSHVINHD--FSSDLIrALTG------HPVANRL 97

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063726842 153 kELNLKVG-RLSTGDSMDMSPHDEESItANDATVKDME 189
Cdd:PRK05634   98 -ELPTGDGaVLATGDAFISDTATRDRL-AQRADLVDME 133
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 67-189 6.93e-04

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: 39.32  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  67 GKDSTLGVESVGTVPASLVTYASILAIQPDLIINAGTAGGFKaKGACISDVYVVSTVAFHDrrIPVPVLDiYGVGMRNTF 146
Cdd:TIGR01704  39 GTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA-PTLKVGDIVVSDEARYHD--ADVTAFG-YEYGQLPGC 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063726842 147 P------------TPNLIKELNLKV--GRLSTGDSMDMSPHDEESITA--NDATVKDME 189
Cdd:TIGR01704 115 PagfkaddkliaaAEACIAELNLNAvrGLIVSGDAFINGSVGLAKIRHnfPQAIAVEME 173
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 13-147 3.46e-03

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 36.91  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063726842  13 ISTIVFIVAMQKEAQPLINRLRLVEE---VNTPFpkevtwimFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYAS 89
Cdd:PRK14697    1 MNRIGIIGAMQIEIDLLLEKLVVQEEqiiAGMPF--------YVGEFMGTEVIVTRCG---------VGKVNAAACTQTL 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063726842  90 ILAIQPDLIINAGTAGGFKAKgACISDVYVVSTVAFHdrripvpvlDIYGVGMRNTFP 147
Cdd:PRK14697   64 IHKFDVDAIINTGVAGGLHPD-VKVGDIVISTNVTHH---------DVSKTQMKNLFP 111
 
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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