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Conserved domains on  [gi|1952676097|ref|XP_038517358|]
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S-methyl-5'-thioadenosine phosphorylase isoform X2 [Canis lupus familiaris]

Protein Classification

MTAP family purine nucleoside phosphorylase( domain architecture ID 12963734)

MTAP family purine nucleoside phosphorylase such as S-methyl-5'-thioadenosine phosphorylase, which catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
 12-255 6.87e-145

5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus MTAPII and Pseudomonas aeruginosa PAO1 5'-methylthioinosine phosphorylase (MTIP); MTAP catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. This subfamily includes human MTAP which is highly specific for MTA, and Sulfolobus solfataricus MTAPII which accepts adenosine in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAP1 belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family. This group also includes Pseudomonas aeruginosa PAO1 MTI phosphorylase (MTIP) which uses 5'-methylthioinosine (MTI) as a preferred substrate, and does not use MTA. 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 (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: 350161  Cd Length: 238  Bit Score: 406.04  E-value: 6.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:cd09010     1 IGIIGGSGLYDLDGLEDVEEVTVETPYGKPSGPVTIGELGGREVAFLPRHGRGHRIPPHRINYRANIWALKELGVTRIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMVT 171
Cdd:cd09010    81 VSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTFFDGG-----GVVHVDFAEPFCPELRELLIEAAKELGIPVHDGGTYVC 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSLL 251
Cdd:cd09010   156 TEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAGLEDEP-VTVEEVLEVLKENAEKVKRLL 234


                  ....
gi 1952676097 252 LTTI 255
Cdd:cd09010   235 LAAI 238
 
Name Accession Description Interval E-value
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
 12-255 6.87e-145

5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus MTAPII and Pseudomonas aeruginosa PAO1 5'-methylthioinosine phosphorylase (MTIP); MTAP catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. This subfamily includes human MTAP which is highly specific for MTA, and Sulfolobus solfataricus MTAPII which accepts adenosine in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAP1 belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family. This group also includes Pseudomonas aeruginosa PAO1 MTI phosphorylase (MTIP) which uses 5'-methylthioinosine (MTI) as a preferred substrate, and does not use MTA. 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 (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: 350161  Cd Length: 238  Bit Score: 406.04  E-value: 6.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:cd09010     1 IGIIGGSGLYDLDGLEDVEEVTVETPYGKPSGPVTIGELGGREVAFLPRHGRGHRIPPHRINYRANIWALKELGVTRIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMVT 171
Cdd:cd09010    81 VSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTFFDGG-----GVVHVDFAEPFCPELRELLIEAAKELGIPVHDGGTYVC 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSLL 251
Cdd:cd09010   156 TEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAGLEDEP-VTVEEVLEVLKENAEKVKRLL 234


                  ....
gi 1952676097 252 LTTI 255
Cdd:cd09010   235 LAAI 238
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
 12-259 2.18e-117

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


Pssm-ID: 439776  Cd Length: 241  Bit Score: 336.64  E-value: 2.18e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDpeILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:COG0005     1 IGIIGGSGLGD--LLEDIEEVAVETPYGEHSGELVIGTLGGKRVVFLPRHGRGHYYEPHMINYRANIRALKALGVKRLIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHsKGAMVT 171
Cdd:COG0005    79 TNAVGSLNPDLKPGDLVLIDDHIDLTGGRPLTGFNGG-----GVRFVDMTDPYDPELRELLLEAAKELGIPLD-EGVYVC 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSLL 251
Cdd:COG0005   153 TEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDEP-LTHEEVLEVAAAAAEKLRRLL 231


                  ....*...
gi 1952676097 252 LTTIPQIG 259
Cdd:COG0005   232 KELIARLP 239
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
10-273 1.51e-116

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 335.46  E-value: 1.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  10 VKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHV 89
Cdd:PRK08564    8 ASIGIIGGSGLYDPGIFENSKEVKVYTPYGEPSDNIIIGEIEGVEVAFLPRHGRGHRIPPHKINYRANIWALKELGVEWV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  90 IVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHacargVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAM 169
Cdd:PRK08564   88 IAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDGPV-----VAHVSMADPFCPELRKIIIETAKELGIRTHEKGTY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 170 VTIEGPRFSSRAESFMFR-TWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEevVSVDRVLKTLKENANKAK 248
Cdd:PRK08564  163 ICIEGPRFSTRAESRMWReVFKADIIGMTLVPEVNLACELGMCYATIAMVTDYDVWAEKP--VTAEEVTRVMAENTEKAK 240

                         250       260
                  ....*....|....*....|....*
gi 1952676097 249 SLLLTTIPQIGSMEWSETLHNLKNM 273
Cdd:PRK08564  241 KLLYEAIPRIPEERKCSCCDSLKTA 265
MTAP TIGR01694
5'-deoxy-5'-methylthioadenosine phosphorylase; This model represents the methylthioadenosine ...
 11-257 3.40e-116

5'-deoxy-5'-methylthioadenosine phosphorylase; This model represents the methylthioadenosine phosphorylase found in metazoa, cyanobacteria and a limited number of archaea such as Sulfolobus, Aeropyrum, Pyrobaculum, Pyrococcus, and Thermoplasma. This enzyme is responsible for the first step in the methionine salvage pathway after the transfer of the amino acid moiety from S-adenosylmethionine. The enzyme from human is well-characterized including a crystal structure. A misleading characterization is found for a Sulfolobus solfataricus enzyme, which is called a MTAP. In fact, as uncovered by the genome sequence of S. solfataricus, there are at least two nucleotide phosphorylases and the one found in the MTAP clade is not the one annotated as such. The sequence in this clade has not been isolated but is likely to be the authentic SsMTAP as it displays all of the conserved active site residues found in the human enzyme. This explains the finding that the characterized enzyme has greater efficiency towards the purines inosine, guanosine and adenosine over MTA. In fact, this mis-naming of this enzyme has been carried forward to several publications including a crystal stucture. In between the trusted and noise cutoffs are: 1) several archaeal sequences which appear to contain several residues characteristic of phosphorylases which act on guanosine or inosine (according to the crystal structure of MTAP and alignments). In any case, these residues are not conserved. 2) sequences from Mycobacterium tuberculosis and Streptomyces coelicolor which have better, although not perfect retention of the active site residues, but considering the general observation that bacteria utilize the MTA/SAH nucleotidase enzyme and a kinase to do this reaction, these have been excluded pending stronger evidence of their function, and 3) a sequence from Drosophila which appears to be a recent divergence (long branch in neighbor-joining trees) and lacks some of the conserved active site residues. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273762  Cd Length: 241  Bit Score: 333.54  E-value: 3.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVI 90
Cdd:TIGR01694   1 MIGVIGGSGLYDLEGLKDVEEVNVDTPYGNPSAPIVVGRVAGVDVAFLPRHGRGHDIPPHEVNYRANIWALKSLGVKYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  91 VTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHacargVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMV 170
Cdd:TIGR01694  81 SVNAVGSLREEYPPGDLVVPDQFIDRTSGRPSTFFDGGK-----VVHVDFGDPYCEDLRQRLIESLRRLGLTVHDGGTYV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 171 TIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSL 250
Cdd:TIGR01694 156 CTEGPRFSTRAESRMFKSWGADIVGMTGVPEAVLARELELCYATLALVTDYDCWISADH-VTAEEVEEVMGENVEKAKRI 234


                  ....*..
gi 1952676097 251 LLTTIPQ 257
Cdd:TIGR01694 235 LLEAIKK 241
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 11-255 3.41e-53

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: 172.91  E-value: 3.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGLDDPEILEGRTEkyvDTPFGKPSDA--LILGKIKNVDcVLLARHGrqhsIMPSNVNYQANIWALKEEGCTH 88
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDD---ETPVGPPSRGgkFYTGTLGGVP-VVLVRHG----IGPPNAAILAAIRLLKEFGVDA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  89 VIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHAcargvcHIPMAEP-FCPKTREVLIETAKKLGLRCHSkG 167
Cdd:pfam01048  73 IIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPY------FPDMAPApADPELRALAKEAAERLGIPVHR-G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 168 AMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCwKEHEEVVSVDRVLKTLKENANKA 247
Cdd:pfam01048 146 VYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAA-GGADGELTHEEVEEFAERAAERA 224


                  ....*...
gi 1952676097 248 KSLLLTTI 255
Cdd:pfam01048 225 AALLLALL 232
 
Name Accession Description Interval E-value
MTAP_SsMTAPII_like_MTIP cd09010
5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus ...
 12-255 6.87e-145

5'-deoxy-5'-methylthioadenosine phosphorylases (MTAP) similar to Sulfolobus solfataricus MTAPII and Pseudomonas aeruginosa PAO1 5'-methylthioinosine phosphorylase (MTIP); MTAP catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. This subfamily includes human MTAP which is highly specific for MTA, and Sulfolobus solfataricus MTAPII which accepts adenosine in addition to MTA. Two MTAPs have been isolated from S. solfataricus: SsMTAP1 and SsMTAPII, SsMTAP1 belongs to a different subfamily of the nucleoside phosphorylase-I (NP-I) family. This group also includes Pseudomonas aeruginosa PAO1 MTI phosphorylase (MTIP) which uses 5'-methylthioinosine (MTI) as a preferred substrate, and does not use MTA. 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 (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: 350161  Cd Length: 238  Bit Score: 406.04  E-value: 6.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:cd09010     1 IGIIGGSGLYDLDGLEDVEEVTVETPYGKPSGPVTIGELGGREVAFLPRHGRGHRIPPHRINYRANIWALKELGVTRIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMVT 171
Cdd:cd09010    81 VSAVGSLREEIKPGDLVIPDQFIDFTKGRPSTFFDGG-----GVVHVDFAEPFCPELRELLIEAAKELGIPVHDGGTYVC 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSLL 251
Cdd:cd09010   156 TEGPRFETRAEIRMFRRLGGDVVGMTGVPEAVLARELGICYASIALVTNYAAGLEDEP-VTVEEVLEVLKENAEKVKRLL 234


                  ....
gi 1952676097 252 LTTI 255
Cdd:cd09010   235 LAAI 238
XapA COG0005
Purine nucleoside phosphorylase [Nucleotide transport and metabolism]; Purine nucleoside ...
 12-259 2.18e-117

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


Pssm-ID: 439776  Cd Length: 241  Bit Score: 336.64  E-value: 2.18e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDpeILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:COG0005     1 IGIIGGSGLGD--LLEDIEEVAVETPYGEHSGELVIGTLGGKRVVFLPRHGRGHYYEPHMINYRANIRALKALGVKRLIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHsKGAMVT 171
Cdd:COG0005    79 TNAVGSLNPDLKPGDLVLIDDHIDLTGGRPLTGFNGG-----GVRFVDMTDPYDPELRELLLEAAKELGIPLD-EGVYVC 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSLL 251
Cdd:COG0005   153 TEGPRFETPAEIRMLRRLGADVVGMSTVPEAILAREAGLCYAGISLVTNYAAGISDEP-LTHEEVLEVAAAAAEKLRRLL 231


                  ....*...
gi 1952676097 252 LTTIPQIG 259
Cdd:COG0005   232 KELIARLP 239
PRK08564 PRK08564
S-methyl-5'-thioadenosine phosphorylase;
10-273 1.51e-116

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236290  Cd Length: 267  Bit Score: 335.46  E-value: 1.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  10 VKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHV 89
Cdd:PRK08564    8 ASIGIIGGSGLYDPGIFENSKEVKVYTPYGEPSDNIIIGEIEGVEVAFLPRHGRGHRIPPHKINYRANIWALKELGVEWV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  90 IVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHacargVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAM 169
Cdd:PRK08564   88 IAVSAVGSLREDYKPGDFVIPDQFIDMTKKREYTFYDGPV-----VAHVSMADPFCPELRKIIIETAKELGIRTHEKGTY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 170 VTIEGPRFSSRAESFMFR-TWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEevVSVDRVLKTLKENANKAK 248
Cdd:PRK08564  163 ICIEGPRFSTRAESRMWReVFKADIIGMTLVPEVNLACELGMCYATIAMVTDYDVWAEKP--VTAEEVTRVMAENTEKAK 240

                         250       260
                  ....*....|....*....|....*
gi 1952676097 249 SLLLTTIPQIGSMEWSETLHNLKNM 273
Cdd:PRK08564  241 KLLYEAIPRIPEERKCSCCDSLKTA 265
MTAP TIGR01694
5'-deoxy-5'-methylthioadenosine phosphorylase; This model represents the methylthioadenosine ...
 11-257 3.40e-116

5'-deoxy-5'-methylthioadenosine phosphorylase; This model represents the methylthioadenosine phosphorylase found in metazoa, cyanobacteria and a limited number of archaea such as Sulfolobus, Aeropyrum, Pyrobaculum, Pyrococcus, and Thermoplasma. This enzyme is responsible for the first step in the methionine salvage pathway after the transfer of the amino acid moiety from S-adenosylmethionine. The enzyme from human is well-characterized including a crystal structure. A misleading characterization is found for a Sulfolobus solfataricus enzyme, which is called a MTAP. In fact, as uncovered by the genome sequence of S. solfataricus, there are at least two nucleotide phosphorylases and the one found in the MTAP clade is not the one annotated as such. The sequence in this clade has not been isolated but is likely to be the authentic SsMTAP as it displays all of the conserved active site residues found in the human enzyme. This explains the finding that the characterized enzyme has greater efficiency towards the purines inosine, guanosine and adenosine over MTA. In fact, this mis-naming of this enzyme has been carried forward to several publications including a crystal stucture. In between the trusted and noise cutoffs are: 1) several archaeal sequences which appear to contain several residues characteristic of phosphorylases which act on guanosine or inosine (according to the crystal structure of MTAP and alignments). In any case, these residues are not conserved. 2) sequences from Mycobacterium tuberculosis and Streptomyces coelicolor which have better, although not perfect retention of the active site residues, but considering the general observation that bacteria utilize the MTA/SAH nucleotidase enzyme and a kinase to do this reaction, these have been excluded pending stronger evidence of their function, and 3) a sequence from Drosophila which appears to be a recent divergence (long branch in neighbor-joining trees) and lacks some of the conserved active site residues. [Central intermediary metabolism, Other, Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273762  Cd Length: 241  Bit Score: 333.54  E-value: 3.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVI 90
Cdd:TIGR01694   1 MIGVIGGSGLYDLEGLKDVEEVNVDTPYGNPSAPIVVGRVAGVDVAFLPRHGRGHDIPPHEVNYRANIWALKSLGVKYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  91 VTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHacargVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMV 170
Cdd:TIGR01694  81 SVNAVGSLREEYPPGDLVVPDQFIDRTSGRPSTFFDGGK-----VVHVDFGDPYCEDLRQRLIESLRRLGLTVHDGGTYV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 171 TIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvVSVDRVLKTLKENANKAKSL 250
Cdd:TIGR01694 156 CTEGPRFSTRAESRMFKSWGADIVGMTGVPEAVLARELELCYATLALVTDYDCWISADH-VTAEEVEEVMGENVEKAKRI 234


                  ....*..
gi 1952676097 251 LLTTIPQ 257
Cdd:TIGR01694 235 LLEAIKK 241
PRK08931 PRK08931
S-methyl-5'-thioadenosine phosphorylase;
7-260 3.74e-106

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 181584  Cd Length: 289  Bit Score: 310.02  E-value: 3.74e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097   7 PTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGC 86
Cdd:PRK08931    1 MTKAVLGIIGGSGVYDIDGLEDARWERVESPWGEPSDALLFGRLGGVPMVFLPRHGRGHRLSPSDINYRANIDALKRAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  87 THVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDgsHACargVCHIPMAEPFCPKTREVLIETAKKLGLRCHSK 166
Cdd:PRK08931   81 TDIVSLSACGSFREELPPGTFVIVDQFIDRTFAREKSFFG--TGC---VAHVSMAHPVCPRLGDRLAAAARAEGITVHRG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 167 GAMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEVVSVDRVLKTLKENANK 246
Cdd:PRK08931  156 GTYLCMEGPQFSTLAESKLYRSWGCDVIGMTNMPEAKLAREAEICYATVAMVTDYDCWHPDHDAVTVDAVIAVLLANADK 235

                         250
                  ....*....|....
gi 1952676097 247 AKSLLLTTIPQIGS 260
Cdd:PRK08931  236 ARALVARLAPDLGA 249
PRK08666 PRK08666
5'-methylthioadenosine phosphorylase; Validated
 10-258 2.94e-91

5'-methylthioadenosine phosphorylase; Validated


Pssm-ID: 169548  Cd Length: 261  Bit Score: 271.20  E-value: 2.94e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  10 VKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSdaLILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHV 89
Cdd:PRK08666    2 VRIAIIGGSGVYDPKILENIREETVETPYGEVK--VKIGTYAGEEVAFLARHGEGHSVPPHKINYRANIWALKELGVERI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  90 IVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHAcarGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAM 169
Cdd:PRK08666   80 LATSAVGSLNPNMKPGDFVILDQFLDFTKNRHYTFYDGGES---GVVHVDFTDPYCPELRKALITAARELGLTYHPGGTY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 170 VTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKE-----HEEVVSVdrvlktLKENA 244
Cdd:PRK08666  157 VCTEGPRFETAAEIRMFRILGGDLVGMTQVPEAVLARELEMCYATVAIVTNYAAGISptkltHSEVVEL------MAQNS 230

                         250
                  ....*....|....
gi 1952676097 245 NKAKSLLLTTIPQI 258
Cdd:PRK08666  231 ENIKKLIMKAIELI 244
PRK07432 PRK07432
S-methyl-5'-thioadenosine phosphorylase;
8-258 2.17e-85

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 180977  Cd Length: 290  Bit Score: 257.40  E-value: 2.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097   8 TAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCT 87
Cdd:PRK07432    2 TQAKIGIIGGSGLYKMEALKDVEEVQLETPFGSPSDALIVGTLDGTRVAFLARHGRNHTLLPTELPFRANIYAMKQLGVE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  88 HVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHacargVCHIPMAEPFCPKTREVLIETAKKLGL---RCH 164
Cdd:PRK07432   82 YLISASAVGSLKEEAKPLDMVVPDQFIDRTKNRISTFFGEGI-----VAHIGFGDPICPALAGVLADAIASLNLpdvTLH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 165 SKGAMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEVVSVDRVLKTLKENA 244
Cdd:PRK07432  157 RGGTYVCMEGPAFSTKAESNLYRSWGATVIGMTNLPEAKLAREAEIAYATLALVTDYDCWHPDHDSVTVEMVIGNLHKNA 236

                         250
                  ....*....|....
gi 1952676097 245 NKAKSLLLTTIPQI 258
Cdd:PRK07432  237 VNAQKVIQETVRRL 250
PRK07823 PRK07823
S-methyl-5'-thioadenosine phosphorylase;
5-258 8.60e-77

S-methyl-5'-thioadenosine phosphorylase;


Pssm-ID: 236107  Cd Length: 264  Bit Score: 234.21  E-value: 8.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097   5 AAPTAVKIGIIGGTGLddPEILE-GRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKE 83
Cdd:PRK07823    1 MHNNGAMLGVIGGSGF--YSFFGsDAREVNVDTPYGPPSAPITIGEVGGRRVAFLPRHGRDHEFSPHTVPYRANMWALRA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  84 EGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGshacarGVCHIPMAEPFCPKTREVLIETAkklglRC 163
Cdd:PRK07823   79 LGVRRVFAPCAVGSLRPELGPGTVVVPDQLVDRTSGRAQTYFDS------GGVHVSFADPYCPTLRAAALGLP-----GV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 164 HSKGAMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEVVSVDRVLKTLKEN 243
Cdd:PRK07823  148 VDGGTMVVVQGPRFSTRAESRWFAAQGWSLVNMTGYPEAVLARELELCYAAIALVTDLDAGVEAGEGVKAVDVFAEFGRN 227

                         250
                  ....*....|....*
gi 1952676097 244 ANKAKSLLLTTIPQI 258
Cdd:PRK07823  228 IERLKRLVRDAIAAV 242
PRK09136 PRK09136
S-methyl-5'-thioinosine phosphorylase;
12-251 1.62e-60

S-methyl-5'-thioinosine phosphorylase;


Pssm-ID: 236390  Cd Length: 245  Bit Score: 192.09  E-value: 1.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHSIMPSNVNYQANIWALKEEGCTHVIV 91
Cdd:PRK09136    2 LAIIGGTGLTQLAGLDIVQRQVVRTPYGAPSGPLTFGTLAGREVVFLARHGHGHTIPPHKVNYRANIWALKQAGATRVLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  92 TTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGShacARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGAMVT 171
Cdd:PRK09136   82 VNTVGGIHADMGPGTLVVPDQIIDYTWGRKSTFFEGD---GEEVTHIDFTHPYSPMLRQRLLAAARAAGVSLVDGGVYAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 172 IEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEVVSVDRVLKTLKENANKAKSLL 251
Cdd:PRK09136  159 TQGPRLETAAEIARLERDGCDLVGMTGMPEAALARELGLPYACLALVANWAAGRGDSAEITMAEIEAALDAAMGRVRELL 238
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 12-254 5.59e-57

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: 182.10  E-value: 5.59e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  12 IGIIGGTGLDDPEI---LEGRTEKYVDtpfgkPSDALILGKIKNVDCVLLARHgrqhsiMPSnVNYQANIWALKEEGCTH 88
Cdd:cd09005     1 YAIIPGDPERVDVIdskLENPQKVSSF-----RGYTMYTGKYNGKRVTVVNGG------MGS-PSAAIVVEELCALGVDT 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  89 VIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTfydgshacargVCHIPMAEPFCPKTREVLIETAKKLGLRCHsKGA 168
Cdd:cd09005    69 IIRVGSCGALREDIKVGDLVIADGAIRGDGVTPYY-----------VVGPPFAPEADPELTAALEEAAKELGLTVH-VGT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 169 MVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEvvsvdrVLKTLKENANKAK 248
Cdd:cd09005   137 VWTTDAFYRETREESEKLRKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITGEIGF------VDEFLSEAEKKAI 210


                  ....*.
gi 1952676097 249 SLLLTT 254
Cdd:cd09005   211 EIALDA 216
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 11-255 3.41e-53

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: 172.91  E-value: 3.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGLDDPEILEGRTEkyvDTPFGKPSDA--LILGKIKNVDcVLLARHGrqhsIMPSNVNYQANIWALKEEGCTH 88
Cdd:pfam01048   1 KIAIIGGSPEELALLAELLDD---ETPVGPPSRGgkFYTGTLGGVP-VVLVRHG----IGPPNAAILAAIRLLKEFGVDA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  89 VIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTFYDGSHAcargvcHIPMAEP-FCPKTREVLIETAKKLGLRCHSkG 167
Cdd:pfam01048  73 IIRTGTAGGLNPDLKVGDVVIPTDAINHDGRSPLFGPEGGPY------FPDMAPApADPELRALAKEAAERLGIPVHR-G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 168 AMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCwKEHEEVVSVDRVLKTLKENANKA 247
Cdd:pfam01048 146 VYATGDGFYFETPAEIRLLRRLGADAVEMETAAEAQVAREAGIPFAAIRVVSDLAA-GGADGELTHEEVEEFAERAAERA 224


                  ....*...
gi 1952676097 248 KSLLLTTI 255
Cdd:pfam01048 225 AALLLALL 232
PNP-EcPNPII_like cd09009
purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); ...
 7-255 4.14e-36

purine nucleoside phosphorylases similar to human PNP and Escherichia coli PNP-II (XapA); Human PNP catalyzes the reversible phosphorolysis of the purine nucleosides and deoxynucleosides inosine, guanosine, deoxyinosine, and deoxyguanosine. Patients with PNP deficiency typically present with severe immunodeficiency, neurological dysfunction, and autoimmunity. Escherichia coli PNPII, product of the xapA/pndA gene, catalyzes the phosphorolysis of xanthosine, inosine and guanosine with equal efficiency and has been referred to as xanthosine phosphorylase and inosine-guanosine phosphorylase. E. coli PNPII is also capable of converting nicotinamide to nicotinamide riboside, and may be involved in the NAD+ salvage pathway. It is one of two purine nucleoside phosphorylases found in E. coli, which also contains PNPI, which displays a different substrate specificity and belongs to a different subgroup of the nucleoside phosphorylase-I (NP-I) family than PNPII. 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 (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: 350160  Cd Length: 265  Bit Score: 129.82  E-value: 4.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097   7 PTAVKIGIIGGTGLDDP-EILEGRTE-KYVDTP-FGKPSDA-----LILGKIKNVDCVLLArhGRQHS---------IMP 69
Cdd:cd09009    15 GFKPKIGIILGSGLGGLaDEIEDPVEiPYSDIPgFPVSTVEghagrLVFGTLGGKPVLVMQ--GRFHYyegysmqevTFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  70 snvnyqanIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTfydGSHACARGVCHIPMAEPFCPKTR 149
Cdd:cd09009    93 --------VRVMKALGVKTLILTNAAGGLNPDFKPGDLMLITDHINLTGDNPLI---GPNDDEFGPRFPDMSDAYDPELR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 150 EVLIETAKKLGLRCHsKG--AMVTieGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYdCWKEH 227
Cdd:cd09009   162 ELAKEAAKELGIPLH-EGvyAGVS--GPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHLGMRVLGLSLITNL-AAGDS 237

                         250       260
                  ....*....|....*....|....*...
gi 1952676097 228 EEVVSVDRVLKTLKENANKAKSLLLTTI 255
Cdd:cd09009   238 DEPLSHEEVLEAAKKAAPKLSRLLREII 265
PRK08202 PRK08202
purine nucleoside phosphorylase; Provisional
 11-258 2.93e-33

purine nucleoside phosphorylase; Provisional


Pssm-ID: 236183  Cd Length: 272  Bit Score: 122.61  E-value: 2.93e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGL-------DDPEILEgrtekYVDTP-FGKPSDA-----LILGKIKNVDCVLLArhGRQHSimpsnvnYQAN 77
Cdd:PRK08202   23 EIGLILGSGLgaladeiENAVVIP-----YADIPgFPVSTVEghageLVLGRLGGKPVLAMQ--GRFHY-------YEGY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  78 --------IWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTfydGSHACARGVCHIPMAEPFCPKTR 149
Cdd:PRK08202   89 smeavtfpVRVMKALGVETLIVTNAAGGLNPDFGPGDLMLISDHINLTGRNPLI---GPNDDEFGPRFPDMSDAYDPELR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 150 EVLIETAKKLGLRCHsKGAMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDY---DCWKE 226
Cdd:PRK08202  166 ALAKKVAKELGIPLQ-EGVYVGVSGPSYETPAEIRMLRTLGADAVGMSTVPEVIVARHCGLKVLGISCITNLaagISDEP 244

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1952676097 227 --HEEVVsvdrvlktlkENANKAKSLLLTTIPQI 258
Cdd:PRK08202  245 lsHEEVL----------EVAERAAPKFGRLVKAI 268
PNPH-PUNA-XAPA TIGR01697
inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily ...
 11-255 2.05e-22

inosine/guanosine/xanthosine phosphorylase family; This model is a subset of the subfamily represented by pfam00896 (phosphorylase family 2). This model excludes the methylthioadenosine phosphorylases (MTAP, TIGR01684) which are believed toplay a specific role in the recycling of methionine from methylthioadenosine. In this subfamily is found three clades of purine phosphorylases based on a neighbor-joining tree using the MTAP family as an outgroup. The highest-branching clade (TIGR01698) consists of a group of sequences from both gram positive and gram negative bacteria which have been annotated as purine nucleotide phosphorylases but have not been further characterized as to substrate specificity. Of the two remaining clades, one is xanthosine phosphorylase (XAPA, TIGR01699), is limited to certain gamma proteobacteria and constitutes a special purine phosphorylase found in a specialized operon for xanthosine catabolism. The enzyme also acts on the same purines (inosine and guanosine) as the other characterized members of this subfamily, but is only induced when xanthosine must be degraded. The remaining and largest clade consists of purine nucleotide phosphorylases (PNPH, TIGR01700) from metazoa and bacteria which act primarily on guanosine and inosine (and do not act on adenosine). Sequences from Clostridium (GP:15025051) and Thermotoga (OMNI:TM1596) fall between these last two clades and are uncharacterized with respect to substrate range and operon.


Pssm-ID: 130758  Cd Length: 248  Bit Score: 93.18  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  11 KIGIIGGTGL-------DDPEILEgrtekYVDTP-FGKPSDA-----LILGKIKNVDCVLLArhGRQHSIMP-SNVNYQA 76
Cdd:TIGR01697   1 DVAIILGSGLgaladqvEDAVIIP-----YEKIPgFPVSTVVghageLVFGRLGGKPVVCMQ--GRFHYYEGyDMATVTF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  77 NIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTKRPQTfydGSHACARGVCHIPMAEPFCPKTREVLIETA 156
Cdd:TIGR01697  74 PVRVMKLLGVEILVVTNAAGGLNPDFKPGDLMIIKDHINLPGLNPLV---GPNDDRFGTRFPDLSNAYDRELRKLAQDVA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097 157 KKLGLRCHsKGAMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDY-----DCWKEHEEvv 231
Cdd:TIGR01697 151 KELGFPLT-EGVYVMVSGPSYETPAEIRMLRILGADAVGMSTVPEVIVARHCGIKVLAVSLITNMaagitDVPLSHEE-- 227

                         250       260
                  ....*....|....*....|....
gi 1952676097 232 svdrVLKTLKENANKAKSLLLTTI 255
Cdd:TIGR01697 228 ----VLAAAAAAAERFISLLEDII 247
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 85-196 1.20e-04

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: 42.48  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  85 GCTHVIVTTACGSLREEIQPGDIVIIDQFIdrttkrpqtFYDGSHACARGVCHIPMAEPFCPKTREVLIETAKKL----G 160
Cdd:cd09008    65 KPDAIINTGVAGGLDPDLKIGDVVIATKVV---------YHDVDATAFGYEGGQPPGMPAYFPADPELLELAKKAakelG 135

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952676097 161 LRCHsKGAMVTieGPRFSSRAE--SFMFRTWGADVINM 196
Cdd:cd09008   136 PKVH-TGLIAS--GDQFVASSEkkEELRENFPALAVEM 170
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 79-196 2.78e-04

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: 41.43  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952676097  79 WALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDrttkrpqtfYDGShACARG-----VCHIPMAEPFCPKTREVLI 153
Cdd:COG0775    61 LLIARFRPDAVINTGVAGGLDPDLKIGDVVLATEVVQ---------HDVD-VTAFGyprgqVPGMPALFEADPALLEAAK 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1952676097 154 ETAKKLGLRCHsKGAMVTieGPRFSSRAESFMF---RTWGADVINM 196
Cdd:COG0775   131 EAAKESGLKVV-TGTIAT--GDRFVWSAEEKRRlreRFPGALAVDM 173
NP-I_spr0068 cd09007
uncharacterized subfamily of the nucleoside phosphorylase-I family; This subfamily is composed ...
 85-114 8.07e-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: 39.77  E-value: 8.07e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1952676097  85 GCTHVIVTTACGSLREEIQPGDIVIIDQFI 114
Cdd:cd09007    70 GAKKFIVVGSCGSLDPDLAVGDIILPTSAL 99
UP_EcUdp-like cd17767
uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine ...
 95-164 2.66e-03

uridine phosphorylases similar to Escherichia coli Udp and related phosphorylases; Uridine phosphorylase (UP) is specific for pyrimidines, and is involved in pyrimidine salvage and in the maintenance of uridine homeostasis. In addition to E. coli Udp, this subfamily includes Shewanella oneidensis MR-1 UP and Plasmodium falciparum purine nucleoside phosphorylase (PfPNP). PfPNP is an outlier in terms of genetic distance from the other families of PNPs. PfPNP is catalytically active for inosine and guanosine, and in addition, has a weak UP activity. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.


Pssm-ID: 350167  Cd Length: 239  Bit Score: 38.19  E-value: 2.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952676097  95 CGSLREEIQPGDIVIidqfidrttkrpqtfydgSHACAR--GVCH--IPMAEPFCPkTREV---LIETAKKLGLRCH 164
Cdd:cd17767    87 CGALQPDIKLGDLVI------------------ATGAVRdeGTSKhyVPPEYPAVA-DPEVvlaLVEAAEELGVPYH 144
 
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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