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Conserved domains on  [gi|1278648127|gb|PJB54559|]
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MAG: nicotinate-nucleotide diphosphorylase (carboxylating) [Bdellovibrio sp. CG_4_9_14_3_um_filter_39_7]

Protein Classification

nicotinate-nucleotide diphosphorylase( domain architecture ID 11415005)

nicotinate-nucleotide diphosphorylase catalyzes the reaction of quinolinic acid (QA) and 5-phosphoribosyl-1-pyrophosphate (PRPP) to nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide as part of the de novo synthesis of NAD

CATH:  3.90.1170.20
EC:  2.4.2.19
Gene Ontology:  GO:0004514|GO:0009435
PubMed:  11876660|9016724|11876660

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 12-282 1.25e-101

Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis


:

Pssm-ID: 439927 [Multi-domain]  Cd Length: 272  Bit Score: 297.70  E-value: 1.25e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  12 LKRDIERFLDED----DFFKHPLYfskLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGT 84
Cdd:COG0157     1 IDELIRRALAEDlgygDLTTEALI---PADARARARLIAREDGVLAGLEVAERVFRLLDPGLEV--EWlvaDGDRVEAGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  85 QIKLNDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTD 164
Cdd:COG0157    76 VLLEVEG-PARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 165 LWMIKDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAALLVKQPDVTYEISG 244
Cdd:COG0157   155 AVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASG 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278648127 245 GVTLENLESYCLKGIDAISVGALTHSAPSVDISFKYEI 282
Cdd:COG0157   235 GITLENIRAYAETGVDYISVGALTHSAPALDLSLRIEP 272
 
Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 12-282 1.25e-101

Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439927 [Multi-domain]  Cd Length: 272  Bit Score: 297.70  E-value: 1.25e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  12 LKRDIERFLDED----DFFKHPLYfskLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGT 84
Cdd:COG0157     1 IDELIRRALAEDlgygDLTTEALI---PADARARARLIAREDGVLAGLEVAERVFRLLDPGLEV--EWlvaDGDRVEAGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  85 QIKLNDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTD 164
Cdd:COG0157    76 VLLEVEG-PARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 165 LWMIKDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAALLVKQPDVTYEISG 244
Cdd:COG0157   155 AVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASG 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278648127 245 GVTLENLESYCLKGIDAISVGALTHSAPSVDISFKYEI 282
Cdd:COG0157   235 GITLENIRAYAETGVDYISVGALTHSAPALDLSLRIEP 272
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 13-279 7.35e-96

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: 282.83  E-value: 7.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  13 KRDIERFLDED-DFFKHPLYFSKLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGTQIKL 88
Cdd:cd01572     1 DAIVRLALAEDlGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEV--EWlvkDGDRVEPGQVLAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  89 NDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMI 168
Cdd:cd01572    79 VEG-PARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 169 KDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAAL-LVKQpDVTYEISGGVT 247
Cdd:cd01572   158 KDNHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVaLLKG-RVLLEASGGIT 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1278648127 248 LENLESYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:cd01572   237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 15-279 1.96e-82

nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase (decarboxylating) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 272894 [Multi-domain]  Cd Length: 265  Bit Score: 248.71  E-value: 1.96e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  15 DIERFLDEDDFFKHPLYFSKLPRHE-VEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSLKEwEGQQLKKGTQIKLNDGiP 93
Cdd:TIGR00078   1 LLDRWLREDLGSGDITTEALVPGSTrATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVK-DGDRVEPGEVVAEVEG-P 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  94 FAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHK 173
Cdd:TIGR00078  79 ARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 174 KCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAAL-LVKQPDVTyEISGGVTLENLE 252
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVqLLKGRVLL-EASGGITLDNLE 237

                         250       260
                  ....*....|....*....|....*..
gi 1278648127 253 SYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLK 264
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 114-279 1.02e-63

Quinolinate phosphoribosyl transferase, C-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 C-terminal domain has a 7 beta-stranded TIM barrel-like fold.


Pssm-ID: 396337  Cd Length: 169  Bit Score: 197.53  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 114 VATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGVKEAMDFFQGLQAFY 193
Cdd:pfam01729   1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 194 TPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAALLV---KQPDVTYEISGGVTLENLESYCLKGIDAISVGALTHS 270
Cdd:pfam01729  81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEEldeRNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160


                  ....*....
gi 1278648127 271 APSVDISFK 279
Cdd:pfam01729 161 VPPLDISLD 169
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 39-279 5.45e-60

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 193.01  E-value: 5.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  39 EVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGTQIKLNDGiPFAVALTAERVALNLLQRASAVA 115
Cdd:PLN02716   48 EAEATFLAKADGVLAGIALADMVFEEVDPSLKV--EWaaiDGDFVHKGLKFGKVTG-PAHSILVAERVVLNFMQRMSGIA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 116 THTKKFVDIAQKYNIkiLDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGVKEAM---DFFQGLQAF 192
Cdd:PLN02716  125 TLTKAMADAAKPACI--LETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVqsaDKYLEEKGL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 193 YTPIEVEIHDLKELDTAMKL------GVRHMMLDNF---------SLDQLKAALLVKQPDVTYEISGGVTLENLESYCLK 257
Cdd:PLN02716  203 SMKIEVETRTLEEVKEVLEYlsdtktSLTRVMLDNMvvplengdvDVSMLKEAVELINGRFETEASGNVTLDTVHKIGQT 282

                         250       260
                  ....*....|....*....|..
gi 1278648127 258 GIDAISVGALTHSAPSVDISFK 279
Cdd:PLN02716  283 GVTYISSGALTHSVKALDISLK 304
 
Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 12-282 1.25e-101

Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439927 [Multi-domain]  Cd Length: 272  Bit Score: 297.70  E-value: 1.25e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  12 LKRDIERFLDED----DFFKHPLYfskLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGT 84
Cdd:COG0157     1 IDELIRRALAEDlgygDLTTEALI---PADARARARLIAREDGVLAGLEVAERVFRLLDPGLEV--EWlvaDGDRVEAGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  85 QIKLNDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTD 164
Cdd:COG0157    76 VLLEVEG-PARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 165 LWMIKDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAALLVKQPDVTYEISG 244
Cdd:COG0157   155 AVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASG 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1278648127 245 GVTLENLESYCLKGIDAISVGALTHSAPSVDISFKYEI 282
Cdd:COG0157   235 GITLENIRAYAETGVDYISVGALTHSAPALDLSLRIEP 272
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 13-279 7.35e-96

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: 282.83  E-value: 7.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  13 KRDIERFLDED-DFFKHPLYFSKLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGTQIKL 88
Cdd:cd01572     1 DAIVRLALAEDlGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEV--EWlvkDGDRVEPGQVLAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  89 NDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMI 168
Cdd:cd01572    79 VEG-PARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 169 KDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAAL-LVKQpDVTYEISGGVT 247
Cdd:cd01572   158 KDNHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVaLLKG-RVLLEASGGIT 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1278648127 248 LENLESYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:cd01572   237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 13-279 3.21e-89

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: 266.26  E-value: 3.21e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  13 KRDIERFLDED----DFFKHPLYfskLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGyplkSLK-EW---EGQQLKKGT 84
Cdd:cd01568     1 DALLDRALAEDlgygDLTTEALI---PGDAPATATLIAKEEGVLAGLEVAEEVFELLD----GIEvEWlvkDGDRVEAGQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  85 QIKLNDGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTD 164
Cdd:cd01568    74 VLLEVEG-PARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 165 LWMIKDNHKKCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAA--LLVKQPDVTYEI 242
Cdd:cd01568   153 AVLIKDNHIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAvkLLKGLPRVLLEA 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1278648127 243 SGGVTLENLESYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:cd01568   233 SGGITLENIRAYAETGVDVISTGALTHSAPALDISLK 269
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 15-279 1.96e-82

nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase (decarboxylating) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 272894 [Multi-domain]  Cd Length: 265  Bit Score: 248.71  E-value: 1.96e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  15 DIERFLDEDDFFKHPLYFSKLPRHE-VEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSLKEwEGQQLKKGTQIKLNDGiP 93
Cdd:TIGR00078   1 LLDRWLREDLGSGDITTEALVPGSTrATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVK-DGDRVEPGEVVAEVEG-P 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  94 FAVALTAERVALNLLQRASAVATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHK 173
Cdd:TIGR00078  79 ARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 174 KCFGGVKEAMDFFQGLQAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAAL-LVKQPDVTyEISGGVTLENLE 252
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVqLLKGRVLL-EASGGITLDNLE 237

                         250       260
                  ....*....|....*....|....*..
gi 1278648127 253 SYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLK 264
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 114-279 1.02e-63

Quinolinate phosphoribosyl transferase, C-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 C-terminal domain has a 7 beta-stranded TIM barrel-like fold.


Pssm-ID: 396337  Cd Length: 169  Bit Score: 197.53  E-value: 1.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 114 VATHTKKFVDIAQKYNIKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGVKEAMDFFQGLQAFY 193
Cdd:pfam01729   1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 194 TPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAALLV---KQPDVTYEISGGVTLENLESYCLKGIDAISVGALTHS 270
Cdd:pfam01729  81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEEldeRNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160


                  ....*....
gi 1278648127 271 APSVDISFK 279
Cdd:pfam01729 161 VPPLDISLD 169
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 39-279 5.45e-60

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 193.01  E-value: 5.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  39 EVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSlkEW---EGQQLKKGTQIKLNDGiPFAVALTAERVALNLLQRASAVA 115
Cdd:PLN02716   48 EAEATFLAKADGVLAGIALADMVFEEVDPSLKV--EWaaiDGDFVHKGLKFGKVTG-PAHSILVAERVVLNFMQRMSGIA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 116 THTKKFVDIAQKYNIkiLDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGVKEAM---DFFQGLQAF 192
Cdd:PLN02716  125 TLTKAMADAAKPACI--LETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVqsaDKYLEEKGL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 193 YTPIEVEIHDLKELDTAMKL------GVRHMMLDNF---------SLDQLKAALLVKQPDVTYEISGGVTLENLESYCLK 257
Cdd:PLN02716  203 SMKIEVETRTLEEVKEVLEYlsdtktSLTRVMLDNMvvplengdvDVSMLKEAVELINGRFETEASGNVTLDTVHKIGQT 282

                         250       260
                  ....*....|....*....|..
gi 1278648127 258 GIDAISVGALTHSAPSVDISFK 279
Cdd:PLN02716  283 GVTYISSGALTHSVKALDISLK 304
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 36-279 1.49e-55

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: 180.51  E-value: 1.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  36 PRHEVEAQLFIKSD--LTLAGTPWFEATFDFLGYPLKsLKEWEgqqLKKGTQIKLNDGI-----PFAVALTAERVALNLL 108
Cdd:cd00516    14 PDTRATAEFTAREDpyGVLAGLEEALELLELLRFPGP-LVILA---VPEGTVVEPGEPLltiegPARELLLLERVLLNLL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 109 QRASAVATHTKKFVDIAQKYN--IKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGVKEAMDFF 186
Cdd:cd00516    90 QRLSGIATATARYVEAAKGANtkVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSIIQAFGEL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 187 QGLQAFY--------TPIEVEIHDLKELDTAMKLGVRHM-MLDNFSLDQLKAALLVKQ----------PDVTYEISGGVT 247
Cdd:cd00516   170 AAVKALRrwlpelfiALIDVEVDTLEEALEAAKAGGADGiRLDSGSPEELDPAVLILKarahldgkglPRVKIEASGGLD 249

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1278648127 248 LENLESYCLKGIDAISVGALTHSAPSVDISFK 279
Cdd:cd00516   250 EENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 14-276 5.01e-28

ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse 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.


Pssm-ID: 238807 [Multi-domain]  Cd Length: 272  Bit Score: 108.54  E-value: 5.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  14 RDIERFLDED----DFFKHPLyfsKLPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSLKEwEGQQLKKGTQIKLN 89
Cdd:cd01573     2 AELERLLLEDapygDLTTEAL---GIGEQPGKITFRARDPGVLCGTEEAARILELLGLEVDLAAA-SGSRVAAGAVLLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  90 DGiPFAVALTAERVALNLLQRASAVATHTKKFVDIAQKYN--IKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWM 167
Cdd:cd01573    78 EG-PAAALHLGWKVAQTLLEWASGIATATAEMVAAARAVNpdIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETIL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 168 IKDNHKKcFGGVKEAMDFFQGL--QAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAA---LLVKQPDVTYEI 242
Cdd:cd01573   157 VFAEHRA-FLGGPEPLKALARLraTAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELvpkLRSLAPPVLLAA 235

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1278648127 243 SGGVTLENLESYCLKGIDAISVGALTHsAPSVDI 276
Cdd:cd01573   236 AGGINIENAAAYAAAGADILVTSAPYY-AKPADI 268
PRK06096 PRK06096
molybdenum transport protein ModD; Provisional
 76-276 2.03e-15

molybdenum transport protein ModD; Provisional


Pssm-ID: 180397 [Multi-domain]  Cd Length: 284  Bit Score: 74.38  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127  76 EGQQLKKGTQIKLNDGIpfAVAL-TAERVALNLLQRASAVATHTKKFVDIAQKYNIK--ILDTRKTTPGLRNLEKYAVVQ 152
Cdd:PRK06096   69 DGSQANAGQRLISAQGN--AAALhQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDgnIACTRKAIPGTRLLATQAVLA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 153 GGGFNHRMGQTDLWMIKDNHKKCFggvkEAMDFFQGL------QAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQ 226
Cdd:PRK06096  147 AGGLIHRAGCAETILLFANHRHFL----HDPQDWSGAinqlrrHAPEKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQ 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1278648127 227 LKAALLV---KQPDVTYEISGGVTLENLESYCLKGIDAISVGALTHSAPSvDI 276
Cdd:PRK06096  223 ATEIAQIapsLAPHCTLSLAGGINLNTLKNYADCGIRLFITSAPYYAAPA-DI 274
modD TIGR01334
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ...
 102-279 2.33e-14

putative molybdenum utilization protein ModD; The gene modD for a member of this family is found with molybdenum transport genes modABC in Rhodobacter capsulatus. However, disruption of modD causes only a 4-fold (rather than 500-fold for modA, modB, modC) change in the external molybdenum concentration required to suppress an alternative nitrogenase. ModD proteins are highly similar to nicotinate-nucleotide pyrophosphorylase (also called quinolinate phosphoribosyltransferase). The function unknown. [Unknown function, General]


Pssm-ID: 130401 [Multi-domain]  Cd Length: 277  Bit Score: 71.47  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 102 RVALNLLQRASAVATHTKKFVDIAQKYN--IKILDTRKTTPGLRNLEKYAVVQGGGFNHRMGQTDLWMIKDNHKKCFGGV 179
Cdd:TIGR01334  93 KSAQSVLEWSCGVATYTHKMVTLAKKISpmAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANHRTFLNDN 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278648127 180 KEAMDFFQGL--QAFYTPIEVEIHDLKELDTAMKLGVRHMMLDNFSLDQLKAA---LLVKQPDVTYEISGGVTLENLESY 254
Cdd:TIGR01334 173 FDWGGAIGRLkqTAPERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLherLKFFDHIPTLAAAGGINPENIADY 252

                         170       180
                  ....*....|....*....|....*
gi 1278648127 255 CLKGIDAISVGALTHSAPSvDISFK 279
Cdd:TIGR01334 253 IEAGIDLFITSAPYYAAPC-DIKVK 276
QRPTase_N pfam02749
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ...
 35-112 5.02e-11

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: 57.89  E-value: 5.02e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278648127  35 LPRHEVEAQLFIKSDLTLAGTPWFEATFDFLGYPLKSLKEwEGQQLKKGTQIKLNDGiPFAVALTAERVALNLLQRAS 112
Cdd:pfam02749  13 PGDKKAKAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVK-DGDRVEAGDVILEIEG-PARALLTAERVALNLLQRLS 88
 
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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