|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
13-279 |
7.36e-144 |
|
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: 404.40 E-value: 7.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 13 ESVAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQG 91
Cdd:COG0157 3 ELIRRALAEDLGYGDLTTEaLIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEVEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 92 PARSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENH 171
Cdd:COG0157 83 PARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDNH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 172 IAACGSIANAVAEAHR-IAPGKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLV 250
Cdd:COG0157 163 IAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLENIR 242
|
250 260
....*....|....*....|....*....
gi 1430737938 251 PVAETGVDYISIGALTKDVRAIDLSMRLE 279
Cdd:COG0157 243 AYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-277 |
7.39e-136 |
|
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: 384.14 E-value: 7.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQGPA 93
Cdd:cd01572 4 VRLALAEDLGRGDITSEaIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 94 RSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIA 173
Cdd:cd01572 84 RSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 174 ACGSIANAVAEAHRIAP-GKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLVPV 252
Cdd:cd01572 164 AAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENIRAY 243
|
250 260
....*....|....*....|....*
gi 1430737938 253 AETGVDYISIGALTKDVRAIDLSMR 277
Cdd:cd01572 244 AETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
15-278 |
2.87e-107 |
|
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: 311.88 E-value: 2.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDpsVTLQWQFHDGDDVPANAVIFRMQGPA 93
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 94 RSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIA 173
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 174 ACGSIANAVAEAHRIAP-GKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLVPV 252
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 1430737938 253 AETGVDYISIGALTKDVRAIDLSMRL 278
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
15-279 |
4.23e-78 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 239.23 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGD-GDIT-AQLIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQGP 92
Cdd:PLN02716 23 IKLALAEDAGDrGDVTcLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 93 ARSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVrlLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHI 172
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAKPACI--LETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 173 AACGSIANAVAEAHRIAPGK----PVEVETESLAELDQALE------AGADIIMLDEF---------SLADMAEAVKRNA 233
Cdd:PLN02716 181 AAAGGITNAVQSADKYLEEKglsmKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDVSMLKEAVELIN 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1430737938 234 GKARLEASGGINAHTLVPVAETGVDYISIGALTKDVRAIDLSMRLE 279
Cdd:PLN02716 261 GRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKID 306
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
113-277 |
3.14e-65 |
|
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: 201.39 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 113 VATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIAACGSIANAVAEAHRIAP-G 191
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 192 KPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVK---RNAGKARLEASGGINAHTLVPVAETGVDYISIGALTKD 268
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEeldERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 1430737938 269 VRAIDLSMR 277
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
13-279 |
7.36e-144 |
|
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: 404.40 E-value: 7.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 13 ESVAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQG 91
Cdd:COG0157 3 ELIRRALAEDLGYGDLTTEaLIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEVEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 92 PARSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENH 171
Cdd:COG0157 83 PARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDNH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 172 IAACGSIANAVAEAHR-IAPGKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLV 250
Cdd:COG0157 163 IAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLENIR 242
|
250 260
....*....|....*....|....*....
gi 1430737938 251 PVAETGVDYISIGALTKDVRAIDLSMRLE 279
Cdd:COG0157 243 AYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-277 |
7.39e-136 |
|
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: 384.14 E-value: 7.39e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQGPA 93
Cdd:cd01572 4 VRLALAEDLGRGDITSEaIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 94 RSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIA 173
Cdd:cd01572 84 RSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 174 ACGSIANAVAEAHRIAP-GKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLVPV 252
Cdd:cd01572 164 AAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENIRAY 243
|
250 260
....*....|....*....|....*
gi 1430737938 253 AETGVDYISIGALTKDVRAIDLSMR 277
Cdd:cd01572 244 AETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-277 |
3.23e-119 |
|
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: 342.15 E-value: 3.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDpSVTLQWQFHDGDDVPANAVIFRMQGPA 93
Cdd:cd01568 4 LDRALAEDLGYGDLTTEaLIPGDAPATATLIAKEEGVLAGLEVAEEVFELLD-GIEVEWLVKDGDRVEAGQVLLEVEGPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 94 RSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIA 173
Cdd:cd01568 83 RSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDNHIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 174 ACGSIANAVAEAHRIAP-GKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAG--KARLEASGGINAHTLV 250
Cdd:cd01568 163 AAGGITEAVKRARAAAPfEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITLENIR 242
|
250 260
....*....|....*....|....*..
gi 1430737938 251 PVAETGVDYISIGALTKDVRAIDLSMR 277
Cdd:cd01568 243 AYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
15-278 |
2.87e-107 |
|
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: 311.88 E-value: 2.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDpsVTLQWQFHDGDDVPANAVIFRMQGPA 93
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 94 RSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIA 173
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 174 ACGSIANAVAEAHRIAP-GKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKARLEASGGINAHTLVPV 252
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 1430737938 253 AETGVDYISIGALTKDVRAIDLSMRL 278
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
15-279 |
4.23e-78 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 239.23 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 15 VAQSLREDIGD-GDIT-AQLIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQFHDGDDVPANAVIFRMQGP 92
Cdd:PLN02716 23 IKLALAEDAGDrGDVTcLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 93 ARSLLTAERAALNWLQTLSGVATACAHYARRVSHTNVrlLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHI 172
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAKPACI--LETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 173 AACGSIANAVAEAHRIAPGK----PVEVETESLAELDQALE------AGADIIMLDEF---------SLADMAEAVKRNA 233
Cdd:PLN02716 181 AAAGGITNAVQSADKYLEEKglsmKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDVSMLKEAVELIN 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1430737938 234 GKARLEASGGINAHTLVPVAETGVDYISIGALTKDVRAIDLSMRLE 279
Cdd:PLN02716 261 GRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKID 306
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
113-277 |
3.14e-65 |
|
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: 201.39 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 113 VATACAHYARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIAACGSIANAVAEAHRIAP-G 191
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 192 KPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVK---RNAGKARLEASGGINAHTLVPVAETGVDYISIGALTKD 268
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEeldERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 1430737938 269 VRAIDLSMR 277
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
27-277 |
9.75e-64 |
|
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: 201.31 E-value: 9.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 27 DITAQLI-----PAEKLATARVITREDAR--LAGSAWVEEVFHQVD-PSVTLQWQFHDGDDVPANAVIFRMQGPARSLLT 98
Cdd:cd00516 1 DLYKLTMiqaypPPDTRATAEFTAREDPYgvLAGLEEALELLELLRfPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 99 AERAALNWLQTLSGVATACAHY--ARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIAACG 176
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYveAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 177 SI------ANAVAEAHRIAPG---KPVEVETESLAELDQALEAG-ADIIMLDEFSLADMAEAVKRNAG----------KA 236
Cdd:cd00516 161 SIiqafgeLAAVKALRRWLPElfiALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKArahldgkglpRV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1430737938 237 RLEASGGINAHTLVPVAETGVDYISIGALTKDVRAIDLSMR 277
Cdd:cd00516 241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
19-265 |
2.94e-36 |
|
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: 130.11 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 19 LREDIGDGDITAQLIP-AEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQwqFHDGDDVPANAVIFRMQGPARSLL 97
Cdd:cd01573 8 LLEDAPYGDLTTEALGiGEQPGKITFRARDPGVLCGTEEAARILELLGLEVDLA--AASGSRVAAGAVLLEAEGPAAALH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 98 TAERAALNWLQTLSGVATACAHY--ARRVSHTNVRLLDTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENHIAAC 175
Cdd:cd01573 86 LGWKVAQTLLEWASGIATATAEMvaAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHRAFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 176 G--SIANAVAEAHRIAPGKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEAVKRNAGKA---RLEASGGINAHTLV 250
Cdd:cd01573 166 GgpEPLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAppvLLAAAGGINIENAA 245
|
250
....*....|....*
gi 1430737938 251 PVAETGVDYISIGAL 265
Cdd:cd01573 246 AYAAAGADILVTSAP 260
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
19-257 |
8.46e-24 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 97.49 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 19 LREDIGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDPSVTLQWQfhDGDDVPANAVIFRMQGPARSLL 97
Cdd:PRK06096 13 LLEDIQGGDLTTRaLGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDDAVS--DGSQANAGQRLISAQGNAAALH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 98 TAERAALNWLQTLSGV----ATACAHYARRVSHTNVRLldTRKTLPGLRLAQKYAVTCGDCDNHRLGLWDAFLIKENH-- 171
Cdd:PRK06096 91 QGWKAVQNVLEWSCGVsdylAQMLALLRERYPDGNIAC--TRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrh 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 172 -IAACGSIANAVAEAHRIAPGKPVEVETESLAELDQALEAGADIIMLDEFSLADMAEA---VKRNAGKARLEASGGINAH 247
Cdd:PRK06096 169 fLHDPQDWSGAINQLRRHAPEKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIaqiAPSLAPHCTLSLAGGINLN 248
|
250
....*....|
gi 1430737938 248 TLVPVAETGV 257
Cdd:PRK06096 249 TLKNYADCGI 258
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
23-111 |
5.13e-23 |
|
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: 89.86 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 23 IGDGDITAQ-LIPAEKLATARVITREDARLAGSAWVEEVFHQVDpsVTLQWQFHDGDDVPANAVIFRMQGPARSLLTAER 101
Cdd:pfam02749 1 IGRGDLTTEaLIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLG--LEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78
|
90
....*....|
gi 1430737938 102 AALNWLQTLS 111
Cdd:pfam02749 79 VALNLLQRLS 88
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
166-263 |
3.54e-03 |
|
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.
Pssm-ID: 238244 Cd Length: 211 Bit Score: 37.84 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737938 166 LIKENHIAAcgSIAnavaeahrIAPGKPVEVETESLAELDQALeagadiIM----------LDEFSL---ADMAEAVKRN 232
Cdd:cd00429 100 LIKELGMKA--GVA--------LNPGTPVEVLEPYLDEVDLVL------VMsvnpgfggqkFIPEVLekiRKLRELIPEN 163
|
90 100 110
....*....|....*....|....*....|.
gi 1430737938 233 AGKARLEASGGINAHTLVPVAETGVDYISIG 263
Cdd:cd00429 164 NLNLLIEVDGGINLETIPLLAEAGADVLVAG 194
|
|
| |
