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Conserved domains on  [gi|1778564609|ref|WP_154773096|]
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MULTISPECIES: 5'-nucleosidase [Acinetobacter]

Protein Classification

Pfs family protein( domain architecture ID 10002400)

Pfs family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 16-183 5.15e-27

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: 101.91  E-value: 5.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  16 KGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVT 91
Cdd:COG0775    35 LGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGG--LDPDlkigDVVLATEVVQHDVDVTAFGYPRGQV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  92 PV-DTDYPAEINL--------DGFFAHLNKGTCGTGDNF----------ETGTPKVACnlVDMEGYALAKVCKKLGVRLI 152
Cdd:COG0775   113 PGmPALFEADPALleaakeaaKESGLKVVTGTIATGDRFvwsaeekrrlRERFPGALA--VDMEGAAIAQVCYRFGVPFL 190

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLEL 183
Cdd:COG0775   191 VIRAISDLAGEKAPNDFDEFLEEAAKNAAEL 221
 
Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 16-183 5.15e-27

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: 101.91  E-value: 5.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  16 KGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVT 91
Cdd:COG0775    35 LGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGG--LDPDlkigDVVLATEVVQHDVDVTAFGYPRGQV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  92 PV-DTDYPAEINL--------DGFFAHLNKGTCGTGDNF----------ETGTPKVACnlVDMEGYALAKVCKKLGVRLI 152
Cdd:COG0775   113 PGmPALFEADPALleaakeaaKESGLKVVTGTIATGDRFvwsaeekrrlRERFPGALA--VDMEGAAIAQVCYRFGVPFL 190

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLEL 183
Cdd:COG0775   191 VIRAISDLAGEKAPNDFDEFLEEAAKNAAEL 221
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 29-180 1.26e-23

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 92.80  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  29 SGIGKVNAAFKAFEVIQKTGCKTLL-----NLGTAGSSYFDAHELVEVTQYVQRDMDVSPLGFDVGVTPVdTDYPAEINL 103
Cdd:PRK06026   36 TGVGPVEAAVNLTAALARLKAAGDLpdlvvSLGSAGSAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPF-LDLPATVEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609 104 DGFFAHLNKGTCGTGDNFETGTP--KVACNLVDMEGYALAKVCKKLGVRLISVKYITDGANDTAHL-DWEENLLLGAKKL 180
Cdd:PRK06026  115 PLRIPGIPEASLSTGGNIVSGAAydAIDADMVDMETYAVLRACQAFGVPLIGLRGISDGAAELKHVgDWTEYLHVIDEKL 194
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 5-183 1.28e-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: 92.95  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609   5 LALIMALPNESKGLFEQ---------AGVEVH------------YSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyF 63
Cdd:cd09008     1 IGIIGAMEEEIAPLLELlenveeetiAGRTFYegtlggkevvlvQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGG--L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  64 DAH----ELVEVTQYVQRDMDVSPLGFDVGVTPVDTD-YPAEINL--------DGFFAHLNKGTCGTGDNFETGTPKVA- 129
Cdd:cd09008    79 DPDlkigDVVIATKVVYHDVDATAFGYEGGQPPGMPAyFPADPELlelakkaaKELGPKVHTGLIASGDQFVASSEKKEe 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1778564609 130 --------CnlVDMEGYALAKVCKKLGVRLISVKYITDGANDTAHLDWEENLLLGAKKLLEL 183
Cdd:cd09008   159 lrenfpalA--VEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEV 218
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-183 3.02e-16

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: 73.53  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  23 GVEVH--YSGIGKVNAAFKA-FEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVTPVD- 94
Cdd:pfam01048  41 GVPVVlvRHGIGPPNAAILAaIRLLKEFGVDAIIRTGTAGG--LNPDlkvgDVVIPTDAINHDGRSPLFGPEGGPYFPDm 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  95 TDYPAEINL-DGFFAHLNK-------GTCGTGDNFETGTP-------KVACNLVDMEGYALAKVCKKLGVRLISVKYITD 159
Cdd:pfam01048 119 APAPADPELrALAKEAAERlgipvhrGVYATGDGFYFETPaeirllrRLGADAVEMETAAEAQVAREAGIPFAAIRVVSD 198

                         170       180
                  ....*....|....*....|....*....
gi 1778564609 160 GANDTA-----HLDWEENLLLGAKKLLEL 183
Cdd:pfam01048 199 LAAGGAdgeltHEEVEEFAERAAERAAAL 227
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 15-188 8.94e-10

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: 55.88  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  15 SKGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSSY--FDAHELVEVTQYVQRDMDVSPLGFDVGVTP 92
Cdd:TIGR01704  33 YTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAptLKVGDIVVSDEARYHDADVTAFGYEYGQLP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  93 ------------VDTDYPAEINLDGFFAhlnKGTCGTGDNFETGTPKVA--------CNLVDMEGYALAKVCKKLGVRLI 152
Cdd:TIGR01704 113 gcpagfkaddklIAAAEACIAELNLNAV---RGLIVSGDAFINGSVGLAkirhnfpqAIAVEMEATAIAHVCHNFNVPFV 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLEL-YKTIK 188
Cdd:TIGR01704 190 VVRAISDVADQQSHLSFDEFLAVAAKQSSLMvESLVQ 226
 
Name Accession Description Interval E-value
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 16-183 5.15e-27

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: 101.91  E-value: 5.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  16 KGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVT 91
Cdd:COG0775    35 LGTLGGKEVVLVNSGIGKVNAATATTLLIARFRPDAVINTGVAGG--LDPDlkigDVVLATEVVQHDVDVTAFGYPRGQV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  92 PV-DTDYPAEINL--------DGFFAHLNKGTCGTGDNF----------ETGTPKVACnlVDMEGYALAKVCKKLGVRLI 152
Cdd:COG0775   113 PGmPALFEADPALleaakeaaKESGLKVVTGTIATGDRFvwsaeekrrlRERFPGALA--VDMEGAAIAQVCYRFGVPFL 190

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLEL 183
Cdd:COG0775   191 VIRAISDLAGEKAPNDFDEFLEEAAKNAAEL 221
PRK06026 PRK06026
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated
 29-180 1.26e-23

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Validated


Pssm-ID: 180353  Cd Length: 212  Bit Score: 92.80  E-value: 1.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  29 SGIGKVNAAFKAFEVIQKTGCKTLL-----NLGTAGSSYFDAHELVEVTQYVQRDMDVSPLGFDVGVTPVdTDYPAEINL 103
Cdd:PRK06026   36 TGVGPVEAAVNLTAALARLKAAGDLpdlvvSLGSAGSAKLEQTEVYQVSSVSYRDMDASPLGFEKGVTPF-LDLPATVEL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609 104 DGFFAHLNKGTCGTGDNFETGTP--KVACNLVDMEGYALAKVCKKLGVRLISVKYITDGANDTAHL-DWEENLLLGAKKL 180
Cdd:PRK06026  115 PLRIPGIPEASLSTGGNIVSGAAydAIDADMVDMETYAVLRACQAFGVPLIGLRGISDGAAELKHVgDWTEYLHVIDEKL 194
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 5-183 1.28e-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: 92.95  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609   5 LALIMALPNESKGLFEQ---------AGVEVH------------YSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyF 63
Cdd:cd09008     1 IGIIGAMEEEIAPLLELlenveeetiAGRTFYegtlggkevvlvQSGIGKVNAAIATQLLIDRFKPDAIINTGVAGG--L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  64 DAH----ELVEVTQYVQRDMDVSPLGFDVGVTPVDTD-YPAEINL--------DGFFAHLNKGTCGTGDNFETGTPKVA- 129
Cdd:cd09008    79 DPDlkigDVVIATKVVYHDVDATAFGYEGGQPPGMPAyFPADPELlelakkaaKELGPKVHTGLIASGDQFVASSEKKEe 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1778564609 130 --------CnlVDMEGYALAKVCKKLGVRLISVKYITDGANDTAHLDWEENLLLGAKKLLEL 183
Cdd:cd09008   159 lrenfpalA--VEMEGAAIAQVCYLNGVPFLVIRSISDLADGEADEDFEEFLELAAKNSAEV 218
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
23-178 4.72e-20

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 83.63  E-value: 4.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  23 GVEV--HYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVTP---- 92
Cdd:PRK05584   40 GHEVvlVLSGIGKVAAALTATILIEHFKVDAVINTGVAGG--LAPGlkvgDVVVADELVQHDVDVTAFGYPYGQVPglpa 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  93 -VDTDyPAEINL-----DGFFAHLNKGTCGTGDNFETGTPKVA------CNL--VDMEGYALAKVCKKLGVRLISVKYIT 158
Cdd:PRK05584  118 aFKAD-EKLVALaekaaKELNLNVHRGLIASGDQFIAGAEKVAairaefPDAlaVEMEGAAIAQVCHEFGVPFVVVRAIS 196

                         170       180
                  ....*....|....*....|
gi 1778564609 159 DGANDTAHLDWEENLLLGAK 178
Cdd:PRK05584  197 DTADDEAHVSFDEFLAVAAK 216
PRK05634 PRK05634
nucleosidase; Provisional
 1-188 6.62e-20

nucleosidase; Provisional


Pssm-ID: 235538  Cd Length: 185  Bit Score: 82.42  E-value: 6.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609   1 MSSDLALIM-ALPNESKGLfeQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLL--NLGTAGSSYFDAHELVEVTQYVQR 77
Cdd:PRK05634    1 MSMTRVLVVsATKEEAVYV--PAGLPLLITGIGKVAAAVALTRALARRGVLPPRvvNIGTAGALRDGLSGVFEPSHVINH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  78 DMDVSPLGFDVGvtpvdTDYPAEINLDGffahLNKGTCGTGDNFETGTP-----KVACNLVDMEGYALAKVCKKLGVRLI 152
Cdd:PRK05634   79 DFSSDLIRALTG-----HPVANRLELPT----GDGAVLATGDAFISDTAtrdrlAQRADLVDMEGYAVAAVAAEFGVPCR 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLELYKTIK 188
Cdd:PRK05634  150 LVKHVSDSADESALGSWPEAVDASARELGEWLAEHV 185
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 23-183 3.02e-16

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: 73.53  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  23 GVEVH--YSGIGKVNAAFKA-FEVIQKTGCKTLLNLGTAGSsyFDAH----ELVEVTQYVQRDMDVSPLGFDVGVTPVD- 94
Cdd:pfam01048  41 GVPVVlvRHGIGPPNAAILAaIRLLKEFGVDAIIRTGTAGG--LNPDlkvgDVVIPTDAINHDGRSPLFGPEGGPYFPDm 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  95 TDYPAEINL-DGFFAHLNK-------GTCGTGDNFETGTP-------KVACNLVDMEGYALAKVCKKLGVRLISVKYITD 159
Cdd:pfam01048 119 APAPADPELrALAKEAAERlgipvhrGVYATGDGFYFETPaeirllrRLGADAVEMETAAEAQVAREAGIPFAAIRVVSD 198

                         170       180
                  ....*....|....*....|....*....
gi 1778564609 160 GANDTA-----HLDWEENLLLGAKKLLEL 183
Cdd:pfam01048 199 LAAGGAdgeltHEEVEEFAERAAERAAAL 227
PRK07164 PRK07164
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional
 19-182 2.11e-10

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; Provisional


Pssm-ID: 235950  Cd Length: 218  Bit Score: 57.49  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  19 FEQAGVEVHY--SGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSS-YFDAHELVEVTQYVQrdMDVSPLGFDVGVTPVDT 95
Cdd:PRK07164   40 FRYKNYNILYinTGIGLINAALATQKLIEKYQIEIIINYGAVGSNiNIDLGQVVYPEKFYL--LDAITPWYPPGQTPGEK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  96 DYpaeINLDGFFAHLNKGTCGTGDNFETGTPKVAC-------NLVDMEGYALAKVCKKLGVRLISVKYITDG-ANDTAHL 167
Cdd:PRK07164  118 EF---YENNKINKNFNKIHLGSSNSFIFDLDKLKIikdfifvSFFDMEAFALAQVCFKNKVKFYCIKYVSDFiENNSDIE 194

                         170
                  ....*....|....*
gi 1778564609 168 DWEENLLLGAKKLLE 182
Cdd:PRK07164  195 IVNNNIKKGSKKALE 209
MTA/SAH-Nsdase TIGR01704
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; This model represents the enzyme ...
 15-188 8.94e-10

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: 55.88  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  15 SKGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSSY--FDAHELVEVTQYVQRDMDVSPLGFDVGVTP 92
Cdd:TIGR01704  33 YTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAptLKVGDIVVSDEARYHDADVTAFGYEYGQLP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  93 ------------VDTDYPAEINLDGFFAhlnKGTCGTGDNFETGTPKVA--------CNLVDMEGYALAKVCKKLGVRLI 152
Cdd:TIGR01704 113 gcpagfkaddklIAAAEACIAELNLNAV---RGLIVSGDAFINGSVGLAkirhnfpqAIAVEMEATAIAHVCHNFNVPFV 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1778564609 153 SVKYITDGANDTAHLDWEENLLLGAKKLLEL-YKTIK 188
Cdd:TIGR01704 190 VVRAISDVADQQSHLSFDEFLAVAAKQSSLMvESLVQ 226
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 5-171 2.92e-07

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: 48.44  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609   5 LALIMALPNESKGL-------------------FEQAGVEVH--YSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGS--S 61
Cdd:cd17877     1 IGIIAAMPEEISPLlrrievlqkvrlggfrfyrGTLGGHPVVlvESGMGKANAARAAQLLLEHFQPDLIISTGFAGGldP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  62 YFDAHELVEVTQYVQRDMDVsPLGFDVGVTPVDTdypAEINLDGFFAHLNKGTCGTGDNFeTGTPKVACNL--------V 133
Cdd:cd17877    81 GLAVGDLVIADRVLYHDGDV-PAGLEADEKLVAL---AEELAAGLNLKVHRGTIITVDAI-VRKSAEKAALaarfpalaV 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1778564609 134 DMEGYALAKVCKKLGVRLISVKYITDGANDTAHLDWEE 171
Cdd:cd17877   156 DMESAAIAQVAAARGIPFLAIRAISDPADEELPFSIEE 193
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 16-152 6.80e-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: 44.83  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  16 KGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH-----ELVEVTQYVQRDM---------DV 81
Cdd:cd17766    26 RGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGA--FPGSglsvgDLVVASEEIAADLgvetpegflSL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  82 SPLGFDVGVTPVD---TDYPAEINLDGFFAHLNKG---TCGTGdnfeTGTPKVACNLV--------DMEGYALAKVCKKL 147
Cdd:cd17766   104 DELGFGLLRIGTDpylNRFPLSALLLAAGLQVKTGpflTVSTV----TGTAERAAELQrrfpaiaeNMEGAAVAHAALLY 179


                  ....*
gi 1778564609 148 GVRLI 152
Cdd:cd17766   180 GVPFL 184
NP-I cd09005
nucleoside phosphorylase-I family; The nucleoside phosphorylase-I family members accept a ...
 29-183 2.88e-05

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: 43.05  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  29 SGIGKVNAAFKAFEVIQkTGCKTLLNLGTAGS--SYFDAHELVEVTQYVQRDmdvsplgfdvGVTP---VDTDYPAEINL 103
Cdd:cd09005    47 GGMGSPSAAIVVEELCA-LGVDTIIRVGSCGAlrEDIKVGDLVIADGAIRGD----------GVTPyyvVGPPFAPEADP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609 104 D------------GFFAHlnKGTCGTGDNFETGTP-------KVACNLVDMEGYALAKVCKKLGVRLISVKYITDGANDT 164
Cdd:cd09005   116 EltaaleeaakelGLTVH--VGTVWTTDAFYRETReeseklrKLGALAVEMETSALATLAHLRGVKAASILAVSDNLITG 193

                         170
                  ....*....|....*....
gi 1778564609 165 AHLDWEENLLLGAKKLLEL 183
Cdd:cd09005   194 EIGFVDEFLSEAEKKAIEI 212
PLN02584 PLN02584
5'-methylthioadenosine nucleosidase
 31-182 6.03e-05

5'-methylthioadenosine nucleosidase


Pssm-ID: 178196  Cd Length: 249  Bit Score: 42.30  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  31 IGKVNAAFKAFEVIQKTGCKTLLNLGTAGSsyFDAH-----ELVEVTQYVQRDMDVSPLGFDV-GVTPVDTdYPAEiNLd 104
Cdd:PLN02584   72 VGTVPASLVTYAAIQALKPDLIINAGTAGG--FKAKgaaigDVFLATAVANHDRRIPIPVFDKyGVGTRDA-FPTP-NL- 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609 105 gfFAHLN--KGTCGTGDNFETGTPKVA------CNLVDMEGYALAKVCKKLGVRLISVKYIT---DGANDTAHlDWEENL 173
Cdd:PLN02584  147 --IKALGlkEGVLSTGNSLDMTEQDEEsikandATVKDMEGAAVAYVADLLKVPAIFVKAVTdivDGDKPTAE-EFLENL 223


                  ....*....
gi 1778564609 174 LLGAKKLLE 182
Cdd:PLN02584  224 SAAAAALQG 232
PRK14697 PRK14697
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/phosphatase; ...
 16-171 4.50e-04

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


Pssm-ID: 184794  Cd Length: 233  Bit Score: 39.61  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  16 KGLFEQAGVEVHYSGIGKVNAAFKAFEVIQKTGCKTLLNLGTAGSSYFDAH--ELVEVTQYVQRDMDVSPLGfdvGVTPV 93
Cdd:PRK14697   36 VGEFMGTEVIVTRCGVGKVNAAACTQTLIHKFDVDAIINTGVAGGLHPDVKvgDIVISTNVTHHDVSKTQMK---NLFPF 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564609  94 DTDYPAE----------INLDGFFAHLNKGTCGTGDNFETGTpKVACNLVD--------MEGYALAKVCKKLGVRLISVK 155
Cdd:PRK14697  113 QEEFIASkelvelarkaCNSSSLHIEIHEGRIVSGECFVEDS-KLKAKLIDeyaphcteMEGAAIGHVAYINEVPFLVIR 191

                         170
                  ....*....|....*.
gi 1778564609 156 YITDGANDTAHLDWEE 171
Cdd:PRK14697  192 CISDSADDEAQISYDD 207
 
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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