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Conserved domains on  [gi|1397887279|gb|PXW88174|]
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nicotinate phosphoribosyltransferase [Streptohalobacillus salinus]

Protein Classification

nicotinate phosphoribosyltransferase( domain architecture ID 11482613)

nicotinate phosphoribosyltransferase (NAPRTase) catalyzes the first and rate limiting step of the NAD salvage pathway, the formation of nicotinic acid mononucleotide (NAMN) and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK07188 PRK07188
nicotinate phosphoribosyltransferase; Provisional
15-367 0e+00

nicotinate phosphoribosyltransferase; Provisional


:

Pssm-ID: 235953 [Multi-domain]  Cd Length: 352  Bit Score: 613.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  15 RLTNKTFKFDERIETGWFSAVYFLKTKEIAKQKRPNNEVVMQFFQK-DHAVLCGTDEAIALIHTFADQSDQLEIFSLKDG 93
Cdd:PRK07188    1 RLTNKTFKFDERIGEGWYSAVYFLKTREIIEKFNPNNIVTMQFFQRrENAVLCGTDEVIALLKTFAKDPSKLKIRYLKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  94 DKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAGDGYAAFIGG 173
Cdd:PRK07188   81 DIINPFETVLEIEGPYENFGFLEGIIDGILARRTSVATNAYNVVQAAN----EKPVIFMGDRADHYLQQAGDGYAAYIGG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 174 STAQATHAMNEWWGRTGIGTMPHALIQLFEGDVVEAAKAYRDVYPEDELTVLVDYNNDVITDSLKVAHEFKDELKGVRLD 253
Cdd:PRK07188  157 ISAFSTHAQNEWWGKSGFGTMPHALIQMFNGDVVEACKAYHKTFPEDELIALVDYNNDVITDSLKVAREFGDKLKGVRVD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 254 TSGNMVDKYFLDNQHLMGSFDPRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNVPVDIYGVGRSLLDI 333
Cdd:PRK07188  237 TSKNMIDKYFIRHPEVLGTFDPRGVNPELIKALRKALDENGGKHVKIIVSSGFDAKKIREFEAQNVPVDIYGVGSSLLKI 316
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1397887279 334 KVGFTGDSVILDGKPQSKFGRQYNPNPRLEKVSY 367
Cdd:PRK07188  317 NIGFTGDAVELNGKKEAKAGRKYRPNPRLERVKL 350
 
Name Accession Description Interval E-value
PRK07188 PRK07188
nicotinate phosphoribosyltransferase; Provisional
15-367 0e+00

nicotinate phosphoribosyltransferase; Provisional


Pssm-ID: 235953 [Multi-domain]  Cd Length: 352  Bit Score: 613.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  15 RLTNKTFKFDERIETGWFSAVYFLKTKEIAKQKRPNNEVVMQFFQK-DHAVLCGTDEAIALIHTFADQSDQLEIFSLKDG 93
Cdd:PRK07188    1 RLTNKTFKFDERIGEGWYSAVYFLKTREIIEKFNPNNIVTMQFFQRrENAVLCGTDEVIALLKTFAKDPSKLKIRYLKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  94 DKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAGDGYAAFIGG 173
Cdd:PRK07188   81 DIINPFETVLEIEGPYENFGFLEGIIDGILARRTSVATNAYNVVQAAN----EKPVIFMGDRADHYLQQAGDGYAAYIGG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 174 STAQATHAMNEWWGRTGIGTMPHALIQLFEGDVVEAAKAYRDVYPEDELTVLVDYNNDVITDSLKVAHEFKDELKGVRLD 253
Cdd:PRK07188  157 ISAFSTHAQNEWWGKSGFGTMPHALIQMFNGDVVEACKAYHKTFPEDELIALVDYNNDVITDSLKVAREFGDKLKGVRVD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 254 TSGNMVDKYFLDNQHLMGSFDPRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNVPVDIYGVGRSLLDI 333
Cdd:PRK07188  237 TSKNMIDKYFIRHPEVLGTFDPRGVNPELIKALRKALDENGGKHVKIIVSSGFDAKKIREFEAQNVPVDIYGVGSSLLKI 316
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1397887279 334 KVGFTGDSVILDGKPQSKFGRQYNPNPRLEKVSY 367
Cdd:PRK07188  317 NIGFTGDAVELNGKKEAKAGRKYRPNPRLERVKL 350
NAPRTase_B cd01571
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ...
30-354 8.62e-138

Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products.


Pssm-ID: 238805 [Multi-domain]  Cd Length: 302  Bit Score: 394.33  E-value: 8.62e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  30 GWFSAVYFLKTKEIAKQKRPNNEVVMQFFQKDH--AVLCGTDEAIALIHTFadqsdQLEIFSLKDGDKISPFETVLTIKG 107
Cdd:cd01571     1 GRFTDVYFLRTRKILEKKGPNPTVTMEFTQRSLpwAVLCGLEEVLALLEGL-----PVKVYALPEGTIFNPKEPVLRIEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 108 PYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAGDGYAAFIGGSTAQATHAMNEWWG 187
Cdd:cd01571    76 PYQDFGELETAILGILARASSIATNAARVKLAAG----DKPVISFGDRRDHPAIQPMDGRAAYIGGCDGVSTVLGAELLG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 188 RTGIGTMPHALIQLFEGDVVEAAKAYRDVYPED-ELTVLVDYNNDVITDSLKVAHEFKDELKGVRLDTSGNmvdkyfldn 266
Cdd:cd01571   152 EKPSGTMPHALIQIFGGDQVEAWKAFDETYPEDvPRIALIDTFNDEKEEALKAAKALGDKLDGVRLDTPSS--------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 267 qhlmgsfdPRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNvpVDIYGVGRSLLDIK-VGFTGDSVILD 345
Cdd:cd01571   223 --------RRGVFRYLIREVRWALDIRGYKHVKIFVSGGLDEEDIKELEDVG--VDAFGVGTAISKAPpVDFTMDIVEVN 292

                  ....*....
gi 1397887279 346 GKPQSKFGR 354
Cdd:cd01571   293 GQPIAKRGK 301
PncB COG1488
Nicotinic acid phosphoribosyltransferase [Coenzyme transport and metabolism]; Nicotinic acid ...
85-331 5.53e-33

Nicotinic acid phosphoribosyltransferase [Coenzyme transport and metabolism]; Nicotinic acid phosphoribosyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 441097 [Multi-domain]  Cd Length: 445  Bit Score: 127.57  E-value: 5.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  85 LEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAG 164
Cdd:COG1488    91 GDIRAVPEGTVVFPGEPLLTVEGTLPEAQLLETLLLNILNYPTLIATKAARIVQAAG----GRPLHDFGLRRAHGLEAAV 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 165 DG-YAAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVvEAAKAYRDVYPEDeLTVLVD-YN-NDVITDSLKVAH 241
Cdd:COG1488   167 AAaRAAYLAGFAGTSNVLAGRYYGIPSVGTMAHSFVQAHDDEL-EAFRAFAEAYPDG-TTLLVDtYDtLSGVPNAIELAK 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 242 EF--KDELKGVRLDtSGNMVDkyfldnqhlmgsfdprgvnpeLVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNV 319
Cdd:COG1488   245 ELlaRGGLLGIRLD-SGDLAY---------------------LSKQARELLDEAGLPDVRIIASDDLDEYRIAALLEQGA 302
                         250
                  ....*....|..
gi 1397887279 320 PVDIYGVGRSLL 331
Cdd:COG1488   303 PIDVFGVGTRLV 314
NAPRTase_put TIGR01513
putative nicotinate phosphoribosyltransferase; A deep split separates two related families of ...
68-367 4.26e-32

putative nicotinate phosphoribosyltransferase; A deep split separates two related families of proteins, one of which includes experimentally characterized examples of nicotinate phosphoribosyltransferase, an the first enzyme of NAD salvage biosynthesis. This model represents the other family. Members have a different (longer) spacing of several key motifs and have an additional C-terminal domain of up to 100 residues. One argument suggesting that this family represents the same enzyme is that no species has a member of both families. Another is that the gene encoding this protein is located near other NAD salvage biosynthesis genes in Nostoc and in at least four different Gram-positive bacteria. NAD and NADP are ubiquitous in life. Most members of this family are Gram-positive bacteria. An additional set of mutually closely related archaeal sequences score between the trusted and noise cutoffs. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273666 [Multi-domain]  Cd Length: 443  Bit Score: 125.16  E-value: 4.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  68 TDEAIALIHTFADQSDQ-----------LEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQV 136
Cdd:TIGR01513  59 DAEDIEYLASLGIFDDAfldylrefrfsGTVRALPEGSLVFPNEPLLQVEGPLIEAQLLETLVLNIINFQTLIATKAARI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 137 VKAGrtsgKQKPVMFMGDRDDHYTQQAGDGY-AAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVvEAAKAYRD 215
Cdd:TIGR01513 139 VLAA----GGKPLLEFGLRRAQGPDAALKAArAAYIGGADGTSNVLAGRLYGIPVSGTMAHSFVMSFDNEL-AAFRAYAK 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 216 VYPEDeLTVLVD-YN--NDVITDSLKVAHEFKDELK--GVRLDtSGNMVdkyfldnqhlmgsfdprgvnpELVFALRHAL 290
Cdd:TIGR01513 214 LYPKA-TVLLVDtYDtlRSGLPNAIAVAKELGEQGKvvGVRID-SGDLL---------------------YLSKQARKQL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 291 DEEGFKHVKIIASGGFTEEKIRRFEKQNVPVDIYGVGRSLldikVGFTGDS--------VILDGKPQSKFgrqyNPNPrl 362
Cdd:TIGR01513 271 DAAGLTQVKIVVSNDLDENSIAALKAEGAPIDVYGVGTSL----VTASDAPalggvyklVAYEGRPVMKL----SENP-- 340

                  ....*
gi 1397887279 363 EKVSY 367
Cdd:TIGR01513 341 EKSTL 345
QRPTase_N pfam02749
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ...
49-112 1.66e-05

Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The N-terminal domain has an alpha/beta hammerhead fold.


Pssm-ID: 460674 [Multi-domain]  Cd Length: 88  Bit Score: 42.86  E-value: 1.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397887279  49 PNNEVVMQFFQKDHAVLCGTDEAIALIhtfadqsDQLEI---FSLKDGDKISPFETVLTIKGPYQSF 112
Cdd:pfam02749  14 GDKKAKAVIIAKEEGVVAGLEEAERVF-------ELLGLeveWLVKDGDRVEAGDVILEIEGPARAL 73
 
Name Accession Description Interval E-value
PRK07188 PRK07188
nicotinate phosphoribosyltransferase; Provisional
15-367 0e+00

nicotinate phosphoribosyltransferase; Provisional


Pssm-ID: 235953 [Multi-domain]  Cd Length: 352  Bit Score: 613.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  15 RLTNKTFKFDERIETGWFSAVYFLKTKEIAKQKRPNNEVVMQFFQK-DHAVLCGTDEAIALIHTFADQSDQLEIFSLKDG 93
Cdd:PRK07188    1 RLTNKTFKFDERIGEGWYSAVYFLKTREIIEKFNPNNIVTMQFFQRrENAVLCGTDEVIALLKTFAKDPSKLKIRYLKDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  94 DKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAGDGYAAFIGG 173
Cdd:PRK07188   81 DIINPFETVLEIEGPYENFGFLEGIIDGILARRTSVATNAYNVVQAAN----EKPVIFMGDRADHYLQQAGDGYAAYIGG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 174 STAQATHAMNEWWGRTGIGTMPHALIQLFEGDVVEAAKAYRDVYPEDELTVLVDYNNDVITDSLKVAHEFKDELKGVRLD 253
Cdd:PRK07188  157 ISAFSTHAQNEWWGKSGFGTMPHALIQMFNGDVVEACKAYHKTFPEDELIALVDYNNDVITDSLKVAREFGDKLKGVRVD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 254 TSGNMVDKYFLDNQHLMGSFDPRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNVPVDIYGVGRSLLDI 333
Cdd:PRK07188  237 TSKNMIDKYFIRHPEVLGTFDPRGVNPELIKALRKALDENGGKHVKIIVSSGFDAKKIREFEAQNVPVDIYGVGSSLLKI 316
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1397887279 334 KVGFTGDSVILDGKPQSKFGRQYNPNPRLEKVSY 367
Cdd:PRK07188  317 NIGFTGDAVELNGKKEAKAGRKYRPNPRLERVKL 350
NAPRTase_B cd01571
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ...
30-354 8.62e-138

Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products.


Pssm-ID: 238805 [Multi-domain]  Cd Length: 302  Bit Score: 394.33  E-value: 8.62e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  30 GWFSAVYFLKTKEIAKQKRPNNEVVMQFFQKDH--AVLCGTDEAIALIHTFadqsdQLEIFSLKDGDKISPFETVLTIKG 107
Cdd:cd01571     1 GRFTDVYFLRTRKILEKKGPNPTVTMEFTQRSLpwAVLCGLEEVLALLEGL-----PVKVYALPEGTIFNPKEPVLRIEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 108 PYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAGDGYAAFIGGSTAQATHAMNEWWG 187
Cdd:cd01571    76 PYQDFGELETAILGILARASSIATNAARVKLAAG----DKPVISFGDRRDHPAIQPMDGRAAYIGGCDGVSTVLGAELLG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 188 RTGIGTMPHALIQLFEGDVVEAAKAYRDVYPED-ELTVLVDYNNDVITDSLKVAHEFKDELKGVRLDTSGNmvdkyfldn 266
Cdd:cd01571   152 EKPSGTMPHALIQIFGGDQVEAWKAFDETYPEDvPRIALIDTFNDEKEEALKAAKALGDKLDGVRLDTPSS--------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 267 qhlmgsfdPRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNvpVDIYGVGRSLLDIK-VGFTGDSVILD 345
Cdd:cd01571   223 --------RRGVFRYLIREVRWALDIRGYKHVKIFVSGGLDEEDIKELEDVG--VDAFGVGTAISKAPpVDFTMDIVEVN 292

                  ....*....
gi 1397887279 346 GKPQSKFGR 354
Cdd:cd01571   293 GQPIAKRGK 301
PRK08662 PRK08662
nicotinate phosphoribosyltransferase; Reviewed
24-365 4.84e-67

nicotinate phosphoribosyltransferase; Reviewed


Pssm-ID: 236328 [Multi-domain]  Cd Length: 343  Bit Score: 215.12  E-value: 4.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  24 DERIETGWFSAVYFLKTKEIAKQKRPNNEVVMQFF-----QKDHAVLCGTDEAIALIhtfadQSDQLEIFSLKDGDKISP 98
Cdd:PRK08662    9 EEEIKSGKTTDIYFERTVEILEHAGKNPKVVAEVTasslpKGEWGVFAGLEEVLELL-----EGKPVDVYALPEGTLFDP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  99 FETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAgrtsGKQKPVMFMGDRDDHYTQQAGDGYAAFIGGSTAQA 178
Cdd:PRK08662   84 KEPVMRIEGPYLEFGIYETALLGILAHASGIATAAARCKEA----AGDKPVLSFGARHVHPAIAPMMDRAAYIGGCDGVS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 179 THAMNEWWGRTGIGTMPHALIQLFeGDVVEAAKAYRDVYPEDE-LTVLVDYNNDVITDSLKVAHEFKDELKGVRLDTSGN 257
Cdd:PRK08662  160 GVLGAELLGIEPSGTMPHALILIF-GDQVEAWKAFDEVVPPDVpRIALVDTFKDEREEALRAAEALGDRLDGVRLDTPSS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 258 MvdkyfldnqhlmgsfdpRGVNPELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQnvpVDIYGVGRSLLDIK-VG 336
Cdd:PRK08662  239 R-----------------RGNFRKIVREVRWTLDIRGYEHVKIFVSGGLDPERIRELRDV---VDGFGVGTYISFAPpVD 298
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1397887279 337 FTGDSVILDGKPQSKFGR--QYNPNPRLEKV 365
Cdd:PRK08662  299 FSMDIVEVEGKPIAKRGKlpGIKQVPRLKEI 329
NAPRTase_PncB cd01567
Nicotinate phosphoribosyltransferase (NAPRTase) family. Nicotinate phosphoribosyltransferase ...
30-331 5.68e-56

Nicotinate phosphoribosyltransferase (NAPRTase) family. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products.


Pssm-ID: 238801 [Multi-domain]  Cd Length: 343  Bit Score: 186.32  E-value: 5.68e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  30 GWFSAVYFLKTKEIAKQKRPNNEVVMQFFQK------DHAVLCGTDEAIALIHTF------------------------A 79
Cdd:cd01567     1 LLDTDLYKLTMMQAYLYPYPNTRVVFEFTFRsnpfggDYIVFAGLEEVLKLLENLrfteeeieylkkllifgefflyllF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  80 DQSDQLEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKA--------GRTSGKQKPVMF 151
Cdd:cd01567    81 LGKLPLEIYALPEGTVVFPKEPLLTIEGPWPEAGLLETPLLAIWNEATSIATKAARKKLAagglletkDNLEELGFKLHD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 152 MGDRDDHYTQQAG-DGYAAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVVEAAKAYRDVYPE---DELTVLVD 227
Cdd:cd01567   161 FGTRRRHSPEAALsGGRAALIGGFGGTSNVAAAKKLGIPPIGTMAHSWIQAFGALEEAAFEAFARWLPQfggGLGIALID 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 228 YNND--VITDSLKVAHEF--KDELKGVRLDTsgnmvdkyfldnqhlmgsfdprGVNPELVFALRHALDEEGF--KHVKII 301
Cdd:cd01567   241 TYDTdnGFLNALKLAKALgaGGGLLGVRLDS----------------------GDPVELIKKVRKHLDELGIdlNKKKII 298
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1397887279 302 ASGGF-TEEKIRRFEKQN-VPVDIYGVGRSLL 331
Cdd:cd01567   299 ISGDLdTEEAIELLLEQGaSPNDAFGVGTSLT 330
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
35-335 2.71e-53

Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.


Pssm-ID: 238286 [Multi-domain]  Cd Length: 281  Bit Score: 177.43  E-value: 2.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  35 VYFLKTKEIAKqkRPNNEVVMQFFQKDH--AVLCGTDEAIALIHTFaDQSDQLEIFSLKDGDKISPFETVLTIKGPYQSF 112
Cdd:cd00516     2 LYKLTMIQAYP--PPDTRATAEFTAREDpyGVLAGLEEALELLELL-RFPGPLVILAVPEGTVVEPGEPLLTIEGPAREL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 113 GFLEGIIDGILARRTSVATNVYQVVKAGRtsGKQKPVMFMGDRDDHYTQQAGDGYAAFIGGSTAQATHAMNEWWGRTGIG 192
Cdd:cd00516    79 LLLERVLLNLLQRLSGIATATARYVEAAK--GANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 193 TMPHALIQLFegDVVEAAKAYRDVYPEDeLTVLVDYNNDVITDSLKVAHEFKdeLKGVRLDtsgnmvdkyfldnqhlmgS 272
Cdd:cd00516   157 TMAHSIIQAF--GELAAVKALRRWLPEL-FIALIDVEVDTLEEALEAAKAGG--ADGIRLD------------------S 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397887279 273 FDPRGVNP-ELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNvpVDIYGVGRSL-----LDIKV 335
Cdd:cd00516   214 GSPEELDPaVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETG--VDVFGVGTLLhsappLDIVL 280
PncB COG1488
Nicotinic acid phosphoribosyltransferase [Coenzyme transport and metabolism]; Nicotinic acid ...
85-331 5.53e-33

Nicotinic acid phosphoribosyltransferase [Coenzyme transport and metabolism]; Nicotinic acid phosphoribosyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 441097 [Multi-domain]  Cd Length: 445  Bit Score: 127.57  E-value: 5.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  85 LEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRtsgkQKPVMFMGDRDDHYTQQAG 164
Cdd:COG1488    91 GDIRAVPEGTVVFPGEPLLTVEGTLPEAQLLETLLLNILNYPTLIATKAARIVQAAG----GRPLHDFGLRRAHGLEAAV 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 165 DG-YAAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVvEAAKAYRDVYPEDeLTVLVD-YN-NDVITDSLKVAH 241
Cdd:COG1488   167 AAaRAAYLAGFAGTSNVLAGRYYGIPSVGTMAHSFVQAHDDEL-EAFRAFAEAYPDG-TTLLVDtYDtLSGVPNAIELAK 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 242 EF--KDELKGVRLDtSGNMVDkyfldnqhlmgsfdprgvnpeLVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNV 319
Cdd:COG1488   245 ELlaRGGLLGIRLD-SGDLAY---------------------LSKQARELLDEAGLPDVRIIASDDLDEYRIAALLEQGA 302
                         250
                  ....*....|..
gi 1397887279 320 PVDIYGVGRSLL 331
Cdd:COG1488   303 PIDVFGVGTRLV 314
NAPRTase_put TIGR01513
putative nicotinate phosphoribosyltransferase; A deep split separates two related families of ...
68-367 4.26e-32

putative nicotinate phosphoribosyltransferase; A deep split separates two related families of proteins, one of which includes experimentally characterized examples of nicotinate phosphoribosyltransferase, an the first enzyme of NAD salvage biosynthesis. This model represents the other family. Members have a different (longer) spacing of several key motifs and have an additional C-terminal domain of up to 100 residues. One argument suggesting that this family represents the same enzyme is that no species has a member of both families. Another is that the gene encoding this protein is located near other NAD salvage biosynthesis genes in Nostoc and in at least four different Gram-positive bacteria. NAD and NADP are ubiquitous in life. Most members of this family are Gram-positive bacteria. An additional set of mutually closely related archaeal sequences score between the trusted and noise cutoffs. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273666 [Multi-domain]  Cd Length: 443  Bit Score: 125.16  E-value: 4.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  68 TDEAIALIHTFADQSDQ-----------LEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQV 136
Cdd:TIGR01513  59 DAEDIEYLASLGIFDDAfldylrefrfsGTVRALPEGSLVFPNEPLLQVEGPLIEAQLLETLVLNIINFQTLIATKAARI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 137 VKAGrtsgKQKPVMFMGDRDDHYTQQAGDGY-AAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVvEAAKAYRD 215
Cdd:TIGR01513 139 VLAA----GGKPLLEFGLRRAQGPDAALKAArAAYIGGADGTSNVLAGRLYGIPVSGTMAHSFVMSFDNEL-AAFRAYAK 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 216 VYPEDeLTVLVD-YN--NDVITDSLKVAHEFKDELK--GVRLDtSGNMVdkyfldnqhlmgsfdprgvnpELVFALRHAL 290
Cdd:TIGR01513 214 LYPKA-TVLLVDtYDtlRSGLPNAIAVAKELGEQGKvvGVRID-SGDLL---------------------YLSKQARKQL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 291 DEEGFKHVKIIASGGFTEEKIRRFEKQNVPVDIYGVGRSLldikVGFTGDS--------VILDGKPQSKFgrqyNPNPrl 362
Cdd:TIGR01513 271 DAAGLTQVKIVVSNDLDENSIAALKAEGAPIDVYGVGTSL----VTASDAPalggvyklVAYEGRPVMKL----SENP-- 340

                  ....*
gi 1397887279 363 EKVSY 367
Cdd:TIGR01513 341 EKSTL 345
NAPRTase_A cd01570
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup A. Nicotinate ...
84-330 3.40e-29

Nicotinate phosphoribosyltransferase (NAPRTase), subgroup A. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products. This subgroup is present in bacteria and eukaryota (except funghi).


Pssm-ID: 238804 [Multi-domain]  Cd Length: 327  Bit Score: 114.98  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  84 QLEIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGrtsgKQKPVMFMGDRDDHYTQQA 163
Cdd:cd01570    86 TGTIYAIPEGEVVFPNEPLLTVEGPLIEAQLLETLLLNLINFQTLIATKAARVRLAA----GGRPLLEFGLRRAQGPDAA 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 164 GDGY-AAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFEGDVvEAAKAYRDVYPeDELTVLVD-YN--NDVITDSLKV 239
Cdd:cd01570   162 LSAArAAYIGGFDGTSNVLAGKLYGIPVSGTMAHSFVQAFDDEL-AAFRAFAEAYP-DNFTLLVDtYDtlRSGLPNAIAV 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 240 AHEFKD---ELKGVRLDtSGNMVdkyfldnqhlmgsfdprgvnpELVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEK 316
Cdd:cd01570   240 AKELGAlgyRLVGVRID-SGDLA---------------------YLSKEARKMLDEAGLTKVKIVASNDLDEYTIAALNA 297
                         250
                  ....*....|....
gi 1397887279 317 QNVPVDIYGVGRSL 330
Cdd:cd01570   298 QGAPIDAFGVGTRL 311
PRK09243 PRK09243
nicotinate phosphoribosyltransferase; Validated
87-330 5.93e-28

nicotinate phosphoribosyltransferase; Validated


Pssm-ID: 236426 [Multi-domain]  Cd Length: 464  Bit Score: 113.71  E-value: 5.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  87 IFSLKDGDKISPFETVLTIKGPyqsFG---FLEGIIDGILARRTSVATnvyqvvKAGR--TSGKQKPVMFMGDRDDHytq 161
Cdd:PRK09243   98 VRAVPEGELVFPNEPLLRVEGP---LAeaqLLETLLLNIINFQTLIAT------KAARivSAAGGRPLLEFGSRRAQ--- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 162 qagdGY--------AAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFeGDVVEAAKAYRDVYPeDELTVLVD-YnnDV 232
Cdd:PRK09243  166 ----GPdaavwaarAAYIGGFDATSNVLAGKRYGIPVSGTMAHSFVQAF-DDEYEAFRAYAETYP-DNTVLLVDtY--DT 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 233 ITDSL----KVAHEFKD--ELKGVRLDtSGNMVdkyfldnqhlmgsfdprgvnpELVFALRHALDEEGFKHVKIIASGGF 306
Cdd:PRK09243  238 LKSGVpnaiKVAKELGDgiELGGVRID-SGDLA---------------------YLSKKVRKMLDEAGFTDTKIVASNDL 295
                         250       260
                  ....*....|....*....|....
gi 1397887279 307 TEEKIRRFEKQNVPVDIYGVGRSL 330
Cdd:PRK09243  296 DEYTIASLKLQGAPIDGFGVGTKL 319
PRK12484 PRK12484
nicotinate phosphoribosyltransferase; Provisional
86-346 2.89e-21

nicotinate phosphoribosyltransferase; Provisional


Pssm-ID: 237112 [Multi-domain]  Cd Length: 443  Bit Score: 94.43  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  86 EIFSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVYQVVKAGRTsgkqKPVMFMGDRDDHYTQQAGD 165
Cdd:PRK12484   91 DVRAVPEGTVVFPNEPLLEVTAPLIEAQLVETFLLNQINHQSLIASKAARCVLAAAG----RPVVDFGARRAHGTDAACY 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 166 G-YAAFIGGSTAQATHAMNEWWGRTGIGTMPHALIQLFeGDVVEAAKAYRDVYPeDELTVLVDYNNDV--ITDSLKVAHE 242
Cdd:PRK12484  167 VaRASYLAGAAGTSNVLAARQYGIPASGTMAHSFVEAF-PDEVAAFRAFARLYP-DATTLLVDTYDTLrgVRNAIEVAKE 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279 243 FKD--ELKGVRLDtSGNMVDkyfldnqhlmgsfdprgvnpeLVFALRHALDEEGFKHVKIIASGGFTEEKIRRFEKQNVP 320
Cdd:PRK12484  245 LGNrfDPRGVRLD-SGDLAE---------------------LSKATRAILDAAGLEQVKIVASGGLDEYRIAALLAAGAP 302
                         250       260
                  ....*....|....*....|....*.
gi 1397887279 321 VDIYGVGRslldiKVGFTGDSVILDG 346
Cdd:PRK12484  303 IDGFGVGT-----RLGVAADAPVLDS 323
QRPTase_N pfam02749
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ...
49-112 1.66e-05

Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The N-terminal domain has an alpha/beta hammerhead fold.


Pssm-ID: 460674 [Multi-domain]  Cd Length: 88  Bit Score: 42.86  E-value: 1.66e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397887279  49 PNNEVVMQFFQKDHAVLCGTDEAIALIhtfadqsDQLEI---FSLKDGDKISPFETVLTIKGPYQSF 112
Cdd:pfam02749  14 GDKKAKAVIIAKEEGVVAGLEEAERVF-------ELLGLeveWLVKDGDRVEAGDVILEIEGPARAL 73
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
49-141 7.62e-05

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 44.00  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  49 PNNEVVMQFFQKDHAVLCGTDEAIALIhtfaDQSDQLEI-FSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRT 127
Cdd:cd01568    25 GDAPATATLIAKEEGVLAGLEVAEEVF----ELLDGIEVeWLVKDGDRVEAGQVLLEVEGPARSLLTAERVALNLLQRLS 100
                          90
                  ....*....|....
gi 1397887279 128 SVATNVYQVVKAGR 141
Cdd:cd01568   101 GIATATRRYVEAAR 114
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
56-139 1.80e-04

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238806 [Multi-domain]  Cd Length: 268  Bit Score: 42.85  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887279  56 QFFQKDHAVLCGTDEAIALihtFADQSDQLEI-FSLKDGDKISPFETVLTIKGPYQSFGFLEGIIDGILARRTSVATNVY 134
Cdd:cd01572    32 RLIAKEEGVLAGLPVAEEV---FELLDPGIEVeWLVKDGDRVEPGQVLATVEGPARSLLTAERTALNFLQRLSGIATLTR 108

                  ....*
gi 1397887279 135 QVVKA 139
Cdd:cd01572   109 RYVEA 113
 
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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