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Conserved domains on  [gi|30690140|ref|NP_195210|]
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Phosphorylase superfamily protein [Arabidopsis thaliana]

Protein Classification

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase( domain architecture ID 10010832)

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase irreversibly cleaves the glycosidic bond in 5'-methylthioadenosine (MTA) to yield adenine and 5'-methylthioribose (MTAN1 and MTAN2); may be active towards S-adenosylhomocysteine (MTAN2)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
6-254 3.01e-165

5'-methylthioadenosine nucleosidase


:

Pssm-ID: 178196  Cd Length: 249  Bit Score: 456.78  E-value: 3.01e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584   1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584  81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  166 DSMDMSPHDEESITANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSEEFLENLAAVTAKLDESLTKVIDF 245
Cdd:PLN02584 161 NSLDMTEQDEESIKANDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDGDKPTAEEFLENLSAAAAALQGAVPKVLDF 240

                 ....*....
gi 30690140  246 ISGKCLSDL 254
Cdd:PLN02584 241 ISGKCLSEL 249
 
Name Accession Description Interval E-value
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
6-254 3.01e-165

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 456.78  E-value: 3.01e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584   1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584  81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  166 DSMDMSPHDEESITANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSEEFLENLAAVTAKLDESLTKVIDF 245
Cdd:PLN02584 161 NSLDMTEQDEESIKANDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDGDKPTAEEFLENLSAAAAALQGAVPKVLDF 240

                 ....*....
gi 30690140  246 ISGKCLSDL 254
Cdd:PLN02584 241 ISGKCLSEL 249
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
16-235 1.65e-37

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: 131.08  E-value: 1.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQP 95
Cdd:cd09008   1 IGIIGAMEEEIAPLLELLENVEEETIAG-----RTFYEGTLGGKEVVLVQSG---------IGKVNAAIATQLLIDRFKP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  96 DLIINAGTAGGFKaKGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLST 164
Cdd:cd09008  67 DAIINTGVAGGLD-PDLKIGDVVIATKVVYHDVDATAFGYEGGQPpGMPAYFPAdPELLElakkaakelGPKVHTGLIAS 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690140 165 GDSMDMSPHDEESITAN-DATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:cd09008 146 GDQFVASSEKKEELRENfPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDfEEFLELAAKNSAEV 218
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
15-235 3.93e-30

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: 112.31  E-value: 3.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  15 TIVFIVAMQKEAQPLINRLRLVEEVNTPFPKevtwiMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQ 94
Cdd:COG0775   2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFT-----FYLGTLGGKEVVLVNSG---------IGKVNAATATTLLIARFR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  95 PDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLS 163
Cdd:COG0775  68 PDAVINTGVAGGLDP-DLKIGDVVLATEVVQHDVDVTAFGYPRGQVpGMPALFEAdPALLEaakeaakesGLKVVTGTIA 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690140 164 TGDSMDMSPHDEESI--TANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:COG0775 147 TGDRFVWSAEEKRRLreRFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDfDEFLEEAAKNAAEL 221
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
15-244 1.74e-25

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: 100.11  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    15 TIVFIVAMQKEAQPLINRLRLVEEVntpFPKEVTWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLV-TYASILAI 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPV---GPPSRGGKFYTGTLGGVPVVLVRHG---------IGPPNAAILaAIRLLKEF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    94 QPDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIP--VPVLDIYGVGMRNTFPTPNLIKEL---------NLKVGRL 162
Cdd:pfam01048  69 GVDAIIRTGTAGGLNP-DLKVGDVVIPTDAINHDGRSPlfGPEGGPYFPDMAPAPADPELRALAkeaaerlgiPVHRGVY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   163 STGDSMDMSPHDEESITAND-ATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDG---NRPTSEEFLENLAAVTAKLDES 238
Cdd:pfam01048 148 ATGDGFYFETPAEIRLLRRLgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGgadGELTHEEVEEFAERAAERAAAL 227

                  ....*.
gi 30690140   239 LTKVID 244
Cdd:pfam01048 228 LLALLA 233
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
67-235 1.03e-11

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: 62.82  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    67 GKDSTLGVESVGTVPASLVTYASILAIQPDLIINAGTAGGFKaKGACISDVYVVSTVAFHDrrIPVPVLDiYGVGMRNTF 146
Cdd:TIGR01704  39 GTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA-PTLKVGDIVVSDEARYHD--ADVTAFG-YEYGQLPGC 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   147 P------------TPNLIKELNLKV--GRLSTGDSMDMSPHDEESITA--NDATVKDMEGAAVAYVADIFKVPTILIKGV 210
Cdd:TIGR01704 115 PagfkaddkliaaAEACIAELNLNAvrGLIVSGDAFINGSVGLAKIRHnfPQAIAVEMEATAIAHVCHNFNVPFVVVRAI 194
                         170       180
                  ....*....|....*....|....*.
gi 30690140   211 TDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:TIGR01704 195 SDVADQQSHLSfDEFLAVAAKQSSLM 220
 
Name Accession Description Interval E-value
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
6-254 3.01e-165

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 456.78  E-value: 3.01e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    6 GQVEKRPISTIVFIVAMQKEAQPLINRLRLVEEVNTPFPKEVTWIMFKGMYKDLNINIVCPGKDSTLGVESVGTVPASLV 85
Cdd:PLN02584   1 QQEEMRPISTVLIVIAMQAEAMPLVNALGLVEDVDSPFPKGVPWVRYSGTHKGLRVHVVCPGKDKALGVDSVGTVPASLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   86 TYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLIKELNLKVGRLSTG 165
Cdd:PLN02584  81 TYAAIQALKPDLIINAGTAGGFKAKGAAIGDVFLATAVANHDRRIPIPVFDKYGVGTRDAFPTPNLIKALGLKEGVLSTG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  166 DSMDMSPHDEESITANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSEEFLENLAAVTAKLDESLTKVIDF 245
Cdd:PLN02584 161 NSLDMTEQDEESIKANDATVKDMEGAAVAYVADLLKVPAIFVKAVTDIVDGDKPTAEEFLENLSAAAAALQGAVPKVLDF 240

                 ....*....
gi 30690140  246 ISGKCLSDL 254
Cdd:PLN02584 241 ISGKCLSEL 249
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
16-235 1.65e-37

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: 131.08  E-value: 1.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQP 95
Cdd:cd09008   1 IGIIGAMEEEIAPLLELLENVEEETIAG-----RTFYEGTLGGKEVVLVQSG---------IGKVNAAIATQLLIDRFKP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  96 DLIINAGTAGGFKaKGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLST 164
Cdd:cd09008  67 DAIINTGVAGGLD-PDLKIGDVVIATKVVYHDVDATAFGYEGGQPpGMPAYFPAdPELLElakkaakelGPKVHTGLIAS 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30690140 165 GDSMDMSPHDEESITAN-DATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:cd09008 146 GDQFVASSEKKEELRENfPALAVEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDfEEFLELAAKNSAEV 218
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
15-235 3.93e-30

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: 112.31  E-value: 3.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  15 TIVFIVAMQKEAQPLINRLRLVEEVNTPFPKevtwiMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQ 94
Cdd:COG0775   2 TIGIIGAMEEEVAALLEALEDKKEVQIAGFT-----FYLGTLGGKEVVLVNSG---------IGKVNAATATTLLIARFR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  95 PDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGV-GMRNTFPT-PNLIK---------ELNLKVGRLS 163
Cdd:COG0775  68 PDAVINTGVAGGLDP-DLKIGDVVLATEVVQHDVDVTAFGYPRGQVpGMPALFEAdPALLEaakeaakesGLKVVTGTIA 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30690140 164 TGDSMDMSPHDEESI--TANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:COG0775 147 TGDRFVWSAEEKRRLreRFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDfDEFLEEAAKNAAEL 221
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
15-244 1.74e-25

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: 100.11  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    15 TIVFIVAMQKEAQPLINRLRLVEEVntpFPKEVTWIMFKGMYKDLNINIVCPGkdstlgvesVGTVPASLV-TYASILAI 93
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDDETPV---GPPSRGGKFYTGTLGGVPVVLVRHG---------IGPPNAAILaAIRLLKEF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    94 QPDLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIP--VPVLDIYGVGMRNTFPTPNLIKEL---------NLKVGRL 162
Cdd:pfam01048  69 GVDAIIRTGTAGGLNP-DLKVGDVVIPTDAINHDGRSPlfGPEGGPYFPDMAPAPADPELRALAkeaaerlgiPVHRGVY 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   163 STGDSMDMSPHDEESITAND-ATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDG---NRPTSEEFLENLAAVTAKLDES 238
Cdd:pfam01048 148 ATGDGFYFETPAEIRLLRRLgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGgadGELTHEEVEEFAERAAERAAAL 227

                  ....*.
gi 30690140   239 LTKVID 244
Cdd:pfam01048 228 LLALLA 233
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
16-233 2.17e-15

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: 72.71  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  16 IVFIVAMQKEAQPLINRLRLVEEVNTPFpkevtWIMFKGMYKdlninivcpGKDSTLGVESVGTVPASLVTYASILAIQP 95
Cdd:cd17877   1 IGIIAAMPEEISPLLRRIEVLQKVRLGG-----FRFYRGTLG---------GHPVVLVESGMGKANAARAAQLLLEHFQP 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  96 DLIINAGTAGGFKAkGACISDVYVVSTVAFHDRRIPVPVLDIYGVGMRNTFPTPNLikELNLKVGRLSTGDSMDMSPHDE 175
Cdd:cd17877  67 DLIISTGFAGGLDP-GLAVGDLVIADRVLYHDGDVPAGLEADEKLVALAEELAAGL--NLKVHRGTIITVDAIVRKSAEK 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140 176 ESITAN-DATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLENLAAVTA 233
Cdd:cd17877 144 AALAARfPALAVDMESAAIAQVAAARGIPFLAIRAISDPADEELPFSiEEFLDEEGAVRP 203
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
15-226 4.85e-14

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 68.99  E-value: 4.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   15 TIVFIVAMQKEAQPLINRLRLVEEV---NTPFpkevtwimFKGMYKdlninivcpGKDSTLGVESVGTVPASLVTYASIL 91
Cdd:PRK05584   2 KIGIIGAMEEEVTLLLDKLENAQTItlaGREF--------YTGTLH---------GHEVVLVLSGIGKVAAALTATILIE 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   92 AIQPDLIINAGTAGGFkAKGACISDVYVVSTVAFHD--------RRIPVPVLDIYgvgmrntFPT-PNLIK--------- 153
Cdd:PRK05584  65 HFKVDAVINTGVAGGL-APGLKVGDVVVADELVQHDvdvtafgyPYGQVPGLPAA-------FKAdEKLVAlaekaakel 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30690140  154 ELNLKVGRLSTGDSMDMSPHDEESITAN--DATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTS-EEFLE 226
Cdd:PRK05584 137 NLNVHRGLIASGDQFIAGAEKVAAIRAEfpDALAVEMEGAAIAQVCHEFGVPFVVVRAISDTADDEAHVSfDEFLA 212
PRK05634 PRK05634
nucleosidase; Provisional
77-215 5.68e-13

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 65.47  E-value: 5.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   77 VGTVPASlVTYASILA---IQPDLIINAGTAGGFKAKgacISDVYVVSTVAFHDrrIPVPVL-DIYGvgmrntFPTPNLI 152
Cdd:PRK05634  30 IGKVAAA-VALTRALArrgVLPPRVVNIGTAGALRDG---LSGVFEPSHVINHD--FSSDLIrALTG------HPVANRL 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30690140  153 kELNLKVG-RLSTGDSMDMSPHDEESItANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVD 215
Cdd:PRK05634  98 -ELPTGDGaVLATGDAFISDTATRDRL-AQRADLVDMEGYAVAAVAAEFGVPCRLVKHVSDSAD 159
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
52-218 5.80e-13

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: 66.02  E-value: 5.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  52 FKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYASILAIQPDLIINAGTAGGFKAKGACISDVYVVSTV-------- 123
Cdd:cd17766  25 LRGLLGDQRVDVLVAG---------VGPVNAAAATALLLERHPPDLVINAGIAGAFPGSGLSVGDLVVASEEiaadlgve 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140 124 ---AFHD-RRIPVPVLDIYGVGMRNTFPT--PNLIKELNLKVGR---LSTgdsmdmsphdeesITANDATVK-------- 186
Cdd:cd17766  96 tpeGFLSlDELGFGLLRIGTDPYLNRFPLsaLLLAAGLQVKTGPfltVST-------------VTGTAERAAelqrrfpa 162
                       170       180       190
                ....*....|....*....|....*....|....*
gi 30690140 187 ---DMEGAAVAYVADIFKVPTILIKGVTDIVdGNR 218
Cdd:cd17766 163 iaeNMEGAAVAHAALLYGVPFLEIRGISNPV-GPR 196
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
67-235 1.03e-11

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: 62.82  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140    67 GKDSTLGVESVGTVPASLVTYASILAIQPDLIINAGTAGGFKaKGACISDVYVVSTVAFHDrrIPVPVLDiYGVGMRNTF 146
Cdd:TIGR01704  39 GTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLA-PTLKVGDIVVSDEARYHD--ADVTAFG-YEYGQLPGC 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   147 P------------TPNLIKELNLKV--GRLSTGDSMDMSPHDEESITA--NDATVKDMEGAAVAYVADIFKVPTILIKGV 210
Cdd:TIGR01704 115 PagfkaddkliaaAEACIAELNLNAvrGLIVSGDAFINGSVGLAKIRHnfPQAIAVEMEATAIAHVCHNFNVPFVVVRAI 194
                         170       180
                  ....*....|....*....|....*.
gi 30690140   211 TDIVDGNRPTS-EEFLENLAAVTAKL 235
Cdd:TIGR01704 195 SDVADQQSHLSfDEFLAVAAKQSSLM 220
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
13-251 1.04e-08

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 54.25  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   13 ISTIVFIVAMQKEAQPLINRLRLVEE---VNTPFpkevtwimFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYAS 89
Cdd:PRK14697   1 MNRIGIIGAMQIEIDLLLEKLVVQEEqiiAGMPF--------YVGEFMGTEVIVTRCG---------VGKVNAAACTQTL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   90 ILAIQPDLIINAGTAGGFKAKgACISDVYVVSTVAFHDrripvpvldIYGVGMRNTFP-------TPNLIK--------- 153
Cdd:PRK14697  64 IHKFDVDAIINTGVAGGLHPD-VKVGDIVISTNVTHHD---------VSKTQMKNLFPfqeefiaSKELVElarkacnss 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  154 ELNLKV--GRLSTGDS-MDMSPHDEESITANDATVKDMEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSeefLENLAA 230
Cdd:PRK14697 134 SLHIEIheGRIVSGECfVEDSKLKAKLIDEYAPHCTEMEGAAIGHVAYINEVPFLVIRCISDSADDEAQIS---YDDFAK 210
                        250       260
                 ....*....|....*....|..
gi 30690140  231 VTAKL-DESLTKVIDFISGKCL 251
Cdd:PRK14697 211 TAANYcSEIIVEMLKNISSKTV 232
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
77-212 1.21e-06

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 47.74  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   77 VGTVPASLVTYASI--LAIQ---PDLIINAGTAGGFKAKGAcisDVYVVSTVAFHD--------RRIPVPVLDiygvgMR 143
Cdd:PRK06026  38 VGPVEAAVNLTAALarLKAAgdlPDLVVSLGSAGSAKLEQT---EVYQVSSVSYRDmdasplgfEKGVTPFLD-----LP 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30690140  144 NTFPTPNLIKELnlKVGRLSTGDSMdMSPHDEESItanDATVKDMEGAAVAYVADIFKVPTILIKGVTD 212
Cdd:PRK06026 110 ATVELPLRIPGI--PEASLSTGGNI-VSGAAYDAI---DADMVDMETYAVLRACQAFGVPLIGLRGISD 172
PRK06698 PRK06698
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; Validated
13-230 4.07e-05

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


Pssm-ID: 136007 [Multi-domain]  Cd Length: 459  Bit Score: 44.23  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   13 ISTIVFIVAMQKEAQPLINRLRLVEE---VNTPFpkevtwimFKGMYKDLNINIVCPGkdstlgvesVGTVPASLVTYAS 89
Cdd:PRK06698   1 MNRIGIIGAMQIEIDLLLEKLIMQEEqiiAGMPF--------YVGEFMGTEVIVTRCG---------VGKVNAAACTQTL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   90 ILAIQPDLIINAGTAGGFKAKgACISDVYVVSTVAFHDrripvpvldIYGVGMRNTFPTPNLI---KELNLKVGRLSTGD 166
Cdd:PRK06698  64 IHKFDVDAIINTGVAGGLHPD-VKVGDIVISTNVTHHD---------VSKTQMKNLFPFQEEFiasKELVELARKACNSS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  167 SMDMSPHdEESITANDATVKD-----------------MEGAAVAYVADIFKVPTILIKGVTDIVDGNRPTSEEFLENLA 229
Cdd:PRK06698 134 SLHMEIH-EGRIVSGECFVEDsklkaklideyaphcteMEGAAIGHVAYINEVPFLVIRCISDSADDEAQISYDDFAKTA 212

                 .
gi 30690140  230 A 230
Cdd:PRK06698 213 A 213
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
56-217 6.55e-04

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 39.77  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140   56 YKDLNINIVCpgkdstlgVES-VGTVPASLVTYASILAIQPDLIINAGtaggfkAKGACISD----VYVVSTVAFHDRRI 130
Cdd:PRK07164  40 FRYKNYNILY--------INTgIGLINAALATQKLIEKYQIEIIINYG------AVGSNINIdlgqVVYPEKFYLLDAIT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30690140  131 PvpvldIYGVGMrntfpTP-------NLIKELNLKVGRLSTGDSMdMSPHDEESITANDATVK--DMEGAAVAYVADIFK 201
Cdd:PRK07164 106 P-----WYPPGQ-----TPgekefyeNNKINKNFNKIHLGSSNSF-IFDLDKLKIIKDFIFVSffDMEAFALAQVCFKNK 174
                        170
                 ....*....|....*.
gi 30690140  202 VPTILIKGVTDIVDGN 217
Cdd:PRK07164 175 VKFYCIKYVSDFIENN 190
 
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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