NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2769574458|ref|WP_366496789|]
View 

futalosine hydrolase [Streptomyces sp. NPDC051572]

Protein Classification

futalosine hydrolase( domain architecture ID 10013027)

futalosine hydrolase converts futalosine into dehypoxanthinyl futalosine in the biosynthesis of menaquinone

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK08236 PRK08236
hypothetical protein; Provisional
 21-221 3.53e-79

hypothetical protein; Provisional


:

Pssm-ID: 236194  Cd Length: 212  Bit Score: 236.88  E-value: 3.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  21 RVLVATAVPAERDAVARAFTNDSWVDVIAAGV--GPAAAAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIADEIT 98
Cdd:PRK08236    3 RVLVVTAVPAERDAVLRGLGNDSRFDVLAAGVgpAAAAASTARALAAAAAPYDLVVSAGIAGGFPGKAEVGSLVVADEII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  99 AADLGAETPDGFVPVTELGFGTVTHRPPSALVRDL-----AAASGARTGAVLTVSTVTGTAARAAELRARHPRALAEAME 173
Cdd:PRK08236   83 AADLGAETPDGFLPVDELGFGTTTIQVDPALVRQLteallAAALGATAGPVLTVSTVTGTAETAAALAARHPDAVAEAME 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2769574458 174 GFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:PRK08236  163 GFGVAEAAAAAGLPVLELRAISNPVGPRDRAAWRIKEALAALTAASSV 210
 
Name Accession Description Interval E-value
PRK08236 PRK08236
hypothetical protein; Provisional
 21-221 3.53e-79

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 236.88  E-value: 3.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  21 RVLVATAVPAERDAVARAFTNDSWVDVIAAGV--GPAAAAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIADEIT 98
Cdd:PRK08236    3 RVLVVTAVPAERDAVLRGLGNDSRFDVLAAGVgpAAAAASTARALAAAAAPYDLVVSAGIAGGFPGKAEVGSLVVADEII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  99 AADLGAETPDGFVPVTELGFGTVTHRPPSALVRDL-----AAASGARTGAVLTVSTVTGTAARAAELRARHPRALAEAME 173
Cdd:PRK08236   83 AADLGAETPDGFLPVDELGFGTTTIQVDPALVRQLteallAAALGATAGPVLTVSTVTGTAETAAALAARHPDAVAEAME 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2769574458 174 GFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:PRK08236  163 GFGVAEAAAAAGLPVLELRAISNPVGPRDRAAWRIKEALAALTAASSV 210
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 21-221 2.43e-62

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: 193.91  E-value: 2.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  21 RVLVATAVP---------AERDAVARAFTNDSWVDVIAAGVGPAAAAAATATALAGTPYALVVSAGIAGGFQP-EAPVGS 90
Cdd:cd17766     1 MILIVTAVPletnlerveAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFPGsGLSVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  91 LVIADEITAADLGAETPDGFVPVTELGFGTVTHRPPSALVRDLAAAS------GARTGAVLTVSTVTGTAARAAELRARH 164
Cdd:cd17766    81 LVVASEEIAADLGVETPEGFLSLDELGFGLLRIGTDPYLNRFPLSALllaaglQVKTGPFLTVSTVTGTAERAAELQRRF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2769574458 165 PrALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:cd17766   161 P-AIAENMEGAAVAHAALLYGVPFLEIRGISNPVGPRDRSAWDIPEALEALQRAVLA 216
fut_nucase TIGR03664
futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine ...
 22-221 3.09e-49

futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine futalosine in a pathway for the biosynthesis of menaquinone distinct from the pathway observed in E. coli.


Pssm-ID: 274710  Cd Length: 222  Bit Score: 160.93  E-value: 3.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  22 VLVATAVPAERDAVARAFTNDSW-------VDVIAAGVGPAAAAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIA 94
Cdd:TIGR03664   1 ILIVTAVTAEASALLRGLGGRYAgsvggagFDVLVTGVGPVNAAAATARLLARAPYELVINAGIAGGFPGKAAVGDLVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  95 DEITAADLGAETPDGFVPVTELGF-------GTVTHRPP--SALVRDLAAASGA-----RTGAVLTVSTVTGTAARAAEL 160
Cdd:TIGR03664  81 DSEIAADLGAETPEGFLPLEALGFpqlpgggRSYFNRIPldPDLVERAVQLARAlglpvARGPFLTVSTVSGTAARAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769574458 161 RARHpRALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:TIGR03664 161 ARRF-GAVAENMEGAAVALAALRYGVPFLELRGISNLVGPRDRSRWRIKEALAALQRAAAK 220
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 72-214 4.57e-20

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: 85.35  E-value: 4.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  72 LVVSAGIAGGFQPEAPVGSLVIADEITAADLGAET---PDGFVPVTELGFgtVTHRPPSALVRDLAAASG--ARTGAVLT 146
Cdd:COG0775    70 AVINTGVAGGLDPDLKIGDVVLATEVVQHDVDVTAfgyPRGQVPGMPALF--EADPALLEAAKEAAKESGlkVVTGTIAT 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2769574458 147 VSTVTGTAARAAELRARHPRALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAA 214
Cdd:COG0775   148 GDRFVWSAEEKRRLRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAA 215
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 72-218 4.53e-08

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: 51.96  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  72 LVVSAGIAGGFQPEAPVGSLVIADEITAADLGAetpDGFVPVTELGFGTVTHRPPSALVRDLAAASGARTGAVL---TVS 148
Cdd:pfam01048  72 AIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRS---PLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVhrgVYA 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769574458 149 TVTGTAARAAELRARHPR--ALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEG 218
Cdd:pfam01048 149 TGDGFYFETPAEIRLLRRlgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERA 220
 
Name Accession Description Interval E-value
PRK08236 PRK08236
hypothetical protein; Provisional
 21-221 3.53e-79

hypothetical protein; Provisional


Pssm-ID: 236194  Cd Length: 212  Bit Score: 236.88  E-value: 3.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  21 RVLVATAVPAERDAVARAFTNDSWVDVIAAGV--GPAAAAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIADEIT 98
Cdd:PRK08236    3 RVLVVTAVPAERDAVLRGLGNDSRFDVLAAGVgpAAAAASTARALAAAAAPYDLVVSAGIAGGFPGKAEVGSLVVADEII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  99 AADLGAETPDGFVPVTELGFGTVTHRPPSALVRDL-----AAASGARTGAVLTVSTVTGTAARAAELRARHPRALAEAME 173
Cdd:PRK08236   83 AADLGAETPDGFLPVDELGFGTTTIQVDPALVRQLteallAAALGATAGPVLTVSTVTGTAETAAALAARHPDAVAEAME 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2769574458 174 GFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:PRK08236  163 GFGVAEAAAAAGLPVLELRAISNPVGPRDRAAWRIKEALAALTAASSV 210
futalosine_nucleosidase_MqnB cd17766
futalosine nucleosidase which catalyzes the hydrolysis of futalosine to ...
 21-221 2.43e-62

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: 193.91  E-value: 2.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  21 RVLVATAVP---------AERDAVARAFTNDSWVDVIAAGVGPAAAAAATATALAGTPYALVVSAGIAGGFQP-EAPVGS 90
Cdd:cd17766     1 MILIVTAVPletnlerveAEREAVLRGLLGDQRVDVLVAGVGPVNAAAATALLLERHPPDLVINAGIAGAFPGsGLSVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  91 LVIADEITAADLGAETPDGFVPVTELGFGTVTHRPPSALVRDLAAAS------GARTGAVLTVSTVTGTAARAAELRARH 164
Cdd:cd17766    81 LVVASEEIAADLGVETPEGFLSLDELGFGLLRIGTDPYLNRFPLSALllaaglQVKTGPFLTVSTVTGTAERAAELQRRF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2769574458 165 PrALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:cd17766   161 P-AIAENMEGAAVAHAALLYGVPFLEIRGISNPVGPRDRSAWDIPEALEALQRAVLA 216
fut_nucase TIGR03664
futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine ...
 22-221 3.09e-49

futalosine hydrolase; This enzyme catalyzes the conversion of futalosine to de-hypoxanthine futalosine in a pathway for the biosynthesis of menaquinone distinct from the pathway observed in E. coli.


Pssm-ID: 274710  Cd Length: 222  Bit Score: 160.93  E-value: 3.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  22 VLVATAVPAERDAVARAFTNDSW-------VDVIAAGVGPAAAAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIA 94
Cdd:TIGR03664   1 ILIVTAVTAEASALLRGLGGRYAgsvggagFDVLVTGVGPVNAAAATARLLARAPYELVINAGIAGGFPGKAAVGDLVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  95 DEITAADLGAETPDGFVPVTELGF-------GTVTHRPP--SALVRDLAAASGA-----RTGAVLTVSTVTGTAARAAEL 160
Cdd:TIGR03664  81 DSEIAADLGAETPEGFLPLEALGFpqlpgggRSYFNRIPldPDLVERAVQLARAlglpvARGPFLTVSTVSGTAARAEAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769574458 161 RARHpRALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEGFGK 221
Cdd:TIGR03664 161 ARRF-GAVAENMEGAAVALAALRYGVPFLELRGISNLVGPRDRSRWRIKEALAALQRAAAK 220
MtnN COG0775
Nucleoside phosphorylase/nucleosidase, includes 5'-methylthioadenosine/S-adenosylhomocysteine ...
 72-214 4.57e-20

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: 85.35  E-value: 4.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  72 LVVSAGIAGGFQPEAPVGSLVIADEITAADLGAET---PDGFVPVTELGFgtVTHRPPSALVRDLAAASG--ARTGAVLT 146
Cdd:COG0775    70 AVINTGVAGGLDPDLKIGDVVLATEVVQHDVDVTAfgyPRGQVPGMPALF--EADPALLEAAKEAAKESGlkVVTGTIAT 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2769574458 147 VSTVTGTAARAAELRARHPRALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAA 214
Cdd:COG0775   148 GDRFVWSAEEKRRLRERFPGALAVDMEGAAIAQVCYRFGVPFLVIRAISDLAGEKAPNDFDEFLEEAA 215
NP_MTAN-like cd17877
nucleoside phosphorylases similar to 5'-methylthioadenosine/S-adenosylhomocysteine ...
 57-197 8.82e-11

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: 59.61  E-value: 8.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  57 AAAATATALAGTPYALVVSAGIAGGFQPEAPVGSLVIADEITAADlgaetpdgfvpvTELGFGTVTHRPPSALVRDLAAA 136
Cdd:cd17877    53 AARAAQLLLEHFQPDLIISTGFAGGLDPGLAVGDLVIADRVLYHD------------GDVPAGLEADEKLVALAEELAAG 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2769574458 137 SG--ARTGAVLTVSTVTGTAARAAELRARHPrALAEAMEGFGVAEAAAAHGIPVLELRAVSNP 197
Cdd:cd17877   121 LNlkVHRGTIITVDAIVRKSAEKAALAARFP-ALAVDMESAAIAQVAAARGIPFLAIRAISDP 182
MTAN cd09008
5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases; This subfamily includes both ...
 72-196 1.44e-08

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: 53.27  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  72 LVVSAGIAGGFQPEAPVGSLVIADEITAADLGAeTPDGFVPVTELGfGTVTHRPPSALVRDLAAASGARTGAVLTVSTVT 151
Cdd:cd09008    68 AIINTGVAGGLDPDLKIGDVVIATKVVYHDVDA-TAFGYEGGQPPG-MPAYFPADPELLELAKKAAKELGPKVHTGLIAS 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2769574458 152 G----TAARAAELRARHPRALAEAMEGFGVAEAAAAHGIPVLELRAVSN 196
Cdd:cd09008   146 GdqfvASSEKKEELRENFPALAVEMEGAAIAQVCYLNGVPFLVIRSISD 194
PNP_UDP_1 pfam01048
Phosphorylase superfamily; Members of this family include: purine nucleoside phosphorylase ...
 72-218 4.53e-08

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: 51.96  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  72 LVVSAGIAGGFQPEAPVGSLVIADEITAADLGAetpDGFVPVTELGFGTVTHRPPSALVRDLAAASGARTGAVL---TVS 148
Cdd:pfam01048  72 AIIRTGTAGGLNPDLKVGDVVIPTDAINHDGRS---PLFGPEGGPYFPDMAPAPADPELRALAKEAAERLGIPVhrgVYA 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769574458 149 TVTGTAARAAELRARHPR--ALAEAMEGFGVAEAAAAHGIPVLELRAVSNPVGPRDRAAWRIGDALAALTEG 218
Cdd:pfam01048 149 TGDGFYFETPAEIRLLRRlgADAVEMETAAEAQVAREAGIPFAAIRVVSDLAAGGADGELTHEEVEEFAERA 220
adenosylhopane_nucleosidase_HpnG-like cd17768
adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; ...
 73-199 1.06e-04

adenosylhopane nucleosidase which cleaves adenine from adenosylhopane to form ribosyl hopane; similar to Burkholderia cenocepacia HpnG; adenosylhopane nucleosidase HpnG, catalyzes the second step in hopanoid side-chain biosynthesis. Hopanoids are bacterial membrane lipids. This CD belongs to the PNP_UDP_1 superfamily which includes members which accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. PNP_UDP_1 includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Superfamily members have different physiologically relevant quaternary structures: hexameric such as the trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP, homotrimeric such as human PNP and Escherichia coli PNPII (XapA), homohexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD), or homodimeric such as human and Trypanosoma brucei UP. The PNP_UDP_2 (nucleoside phosphorylase-II family) is a different structural family.


Pssm-ID: 350168  Cd Length: 188  Bit Score: 41.76  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  73 VVSAGIAGGFQPEAPVGSLVIADEITAADLGAETPDGFVpvtelgfgtvthrppSALVRDLAAASGARTGAVLTVSTVTG 152
Cdd:cd17768    50 LISFGVAGGLDPALKPGDLVLPEAVVADGERYPTDPAWR---------------RRLLRALPAGLRVVAGPLAGSDAPVL 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2769574458 153 TaaraaelrARHPRALAEA-------MEGFGVAEAAAAHGIPVLELRAVSNPVG 199
Cdd:cd17768   115 S--------VADKAALHAAtgavavdMESGAVAAVAAEAGLPFAAIRAIADPAD 160
PRK07077 PRK07077
phosphorylase;
73-214 1.99e-04

phosphorylase;


Pssm-ID: 235926  Cd Length: 238  Bit Score: 41.18  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  73 VVSAGIAGGFQPEAPVGSLVIADEITAADLGAETPDGFvpvtelgfgtvtHRPPSALVRDLAAASGARTGAVLTVSTVTG 152
Cdd:PRK07077   57 IVSFGVAGGLDPDLAPGDLVVATAVDAPFGRVDTDARW------------SARLAAALELTPVARRVVRGGLAGVEAPVV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769574458 153 TAARAAELRARHPrALAEAMEGFGVAEAAAAHGIPVLELRAVSNPvgprdraAWRIGDALAA 214
Cdd:PRK07077  125 GAAAKAALHRATG-ALAVDMESHIAAAFAAARGLPFAACRVIVDP-------AWRTLPAAAT 178
PRK05584 PRK05584
5'-methylthioadenosine/adenosylhomocysteine nucleosidase;
73-195 5.09e-03

5'-methylthioadenosine/adenosylhomocysteine nucleosidase;


Pssm-ID: 180148  Cd Length: 230  Bit Score: 37.02  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769574458  73 VVSAGIAGGFQPEAPVGSLVIADEITAADLGAET---PDGFVPVTELGFgtvthrPPSALVRDLAAASGARTGAVLTVST 149
Cdd:PRK05584   71 VINTGVAGGLAPGLKVGDVVVADELVQHDVDVTAfgyPYGQVPGLPAAF------KADEKLVALAEKAAKELNLNVHRGL 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2769574458 150 -VTG-----TAARAAELRARHPRALAEAMEGFGVAEAAAAHGIPVLELRAVS 195
Cdd:PRK05584  145 iASGdqfiaGAEKVAAIRAEFPDALAVEMEGAAIAQVCHEFGVPFVVVRAIS 196
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH