|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
26-297 |
8.91e-134 |
|
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: 379.75 E-value: 8.91e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGGtvdanNDITAKLL-PENSRSHATVITRENGVFCGKRWVEEVFiQLAGDDVTIIWHVDDGDVINANQPL 104
Cdd:COG0157 4 LIRRALAEDLGY-----GDLTTEALiPADARARARLIAREDGVLAGLEVAERVF-RLLDPGLEVEWLVADGDRVEAGDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:COG0157 78 LEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKASWLHP-------------DApvevevenleelDEALKAGADIIMLDNFETEQMREAVKRTN 251
Cdd:COG0157 158 IKDNHIAAAGGIAEAVARARARAPpekkievevetleEL------------EEALAAGADIIMLDNMSPEELREAVALLR 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 476961649 252 GKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMRFR 297
Cdd:COG0157 226 GRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
26-295 |
4.21e-127 |
|
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: 362.95 E-value: 4.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGgtvdaNNDITAKLL-PENSRSHATVITRENGVFCGKRWVEEVFIQLaGDDVTIIWHVDDGDVINANQPL 104
Cdd:cd01572 3 IVRLALAEDLG-----RGDITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELL-DPGIEVEWLVKDGDRVEPGQVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:cd01572 77 ATVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKASWLHP-DAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVT 263
Cdd:cd01572 157 IKDNHIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 476961649 264 DKTLREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
26-296 |
9.76e-121 |
|
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: 346.55 E-value: 9.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGgtvdaNNDITAK-LLPENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWHVDDGDVINANQPL 104
Cdd:TIGR00078 1 LLDRWLREDLG-----SGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQL---GVQVEWLVKDGDRVEPGEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:TIGR00078 73 AEVEGPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKA-SWLHPDAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVT 263
Cdd:TIGR00078 153 IKDNHIAAAGSIEKAVKRArAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGIT 232
|
250 260 270
....*....|....*....|....*....|...
gi 476961649 264 DKTLREFAETGVDFISVGALTKHVQALDLSMRF 296
Cdd:TIGR00078 233 LDNLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-295 |
1.47e-71 |
|
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: 218.33 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 131 VASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKASWLHPDA 210
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 211 PV-EVEVENLEELDEALKAGADIIMLDNFETEQMREAVK---RTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKH 286
Cdd:pfam01729 81 VKiEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEeldERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 476961649 287 VQALDLSMR 295
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-295 |
2.76e-71 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 222.29 E-value: 2.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 22 DIPGAVAQALREDLGGTVDANndiTAKLLPENSRSHATVITRENGVFCGKRWVEEVFiQLAGDDVTIIWHVDDGDVINAN 101
Cdd:PLN02716 18 DIEAVIKLALAEDAGDRGDVT---CLATIPGDMEAEATFLAKADGVLAGIALADMVF-EEVDPSLKVEWAAIDGDFVHKG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 102 QPLFELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNtqLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSD 181
Cdd:PLN02716 94 LKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 182 AFLIKENHIIASGSVRQAVEKA-SWLHP---DAPVEVEVENLEELDEAL------KAGADIIMLDNFETEQ--------- 242
Cdd:PLN02716 172 MVMIKDNHIAAAGGITNAVQSAdKYLEEkglSMKIEVETRTLEEVKEVLeylsdtKTSLTRVMLDNMVVPLengdvdvsm 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 476961649 243 MREAVKRTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:PLN02716 252 LKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
26-297 |
8.91e-134 |
|
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: 379.75 E-value: 8.91e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGGtvdanNDITAKLL-PENSRSHATVITRENGVFCGKRWVEEVFiQLAGDDVTIIWHVDDGDVINANQPL 104
Cdd:COG0157 4 LIRRALAEDLGY-----GDLTTEALiPADARARARLIAREDGVLAGLEVAERVF-RLLDPGLEVEWLVADGDRVEAGDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:COG0157 78 LEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKASWLHP-------------DApvevevenleelDEALKAGADIIMLDNFETEQMREAVKRTN 251
Cdd:COG0157 158 IKDNHIAAAGGIAEAVARARARAPpekkievevetleEL------------EEALAAGADIIMLDNMSPEELREAVALLR 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 476961649 252 GKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMRFR 297
Cdd:COG0157 226 GRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
26-295 |
4.21e-127 |
|
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: 362.95 E-value: 4.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGgtvdaNNDITAKLL-PENSRSHATVITRENGVFCGKRWVEEVFIQLaGDDVTIIWHVDDGDVINANQPL 104
Cdd:cd01572 3 IVRLALAEDLG-----RGDITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELL-DPGIEVEWLVKDGDRVEPGQVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:cd01572 77 ATVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKASWLHP-DAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVT 263
Cdd:cd01572 157 IKDNHIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 476961649 264 DKTLREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
26-296 |
9.76e-121 |
|
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: 346.55 E-value: 9.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGgtvdaNNDITAK-LLPENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWHVDDGDVINANQPL 104
Cdd:TIGR00078 1 LLDRWLREDLG-----SGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQL---GVQVEWLVKDGDRVEPGEVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:TIGR00078 73 AEVEGPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKA-SWLHPDAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVT 263
Cdd:TIGR00078 153 IKDNHIAAAGSIEKAVKRArAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGIT 232
|
250 260 270
....*....|....*....|....*....|...
gi 476961649 264 DKTLREFAETGVDFISVGALTKHVQALDLSMRF 296
Cdd:TIGR00078 233 LDNLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
26-295 |
1.10e-113 |
|
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: 328.66 E-value: 1.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 26 AVAQALREDLGGtvdanNDITAKLL-PENSRSHATVITRENGVFCGKRWVEEVFIQLagDDVTIIWHVDDGDVINANQPL 104
Cdd:cd01568 3 LLDRALAEDLGY-----GDLTTEALiPGDAPATATLIAKEEGVLAGLEVAEEVFELL--DGIEVEWLVKDGDRVEAGQVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 105 FELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFL 184
Cdd:cd01568 76 LEVEGPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 185 IKENHIIASGSVRQAVEKASWLHP-DAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNG--KALLEVSGN 261
Cdd:cd01568 156 IKDNHIAAAGGITEAVKRARAAAPfEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGG 235
|
250 260 270
....*....|....*....|....*....|....
gi 476961649 262 VTDKTLREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:cd01568 236 ITLENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
51-295 |
7.63e-73 |
|
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: 225.58 E-value: 7.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 51 PENSRSHATVITREN--GVFCGKRWVEEVFIQLAGDDVTIIWHVDDGDVINANQPLFELEGPSRVLLTGERTALNFVQTL 128
Cdd:cd00516 13 PPDTRATAEFTAREDpyGVLAGLEEALELLELLRFPGPLVILAVPEGTVVEPGEPLLTIEGPARELLLLERVLLNLLQRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 129 SGVASKVRHYVELLEGTNTQL--LDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQ------AV 200
Cdd:cd00516 93 SGIATATARYVEAAKGANTKVhdFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSIIQafgelaAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 201 EKASWLHPDAPVEVEVENLEELDEALKA----GADIIMLDNFETEQMREAVKRTNG----------KALLEVSGNVTDKT 266
Cdd:cd00516 173 KALRRWLPELFIALIDVEVDTLEEALEAakagGADGIRLDSGSPEELDPAVLILKArahldgkglpRVKIEASGGLDEEN 252
|
250 260
....*....|....*....|....*....
gi 476961649 267 LREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:cd00516 253 IRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-295 |
1.47e-71 |
|
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: 218.33 E-value: 1.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 131 VASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKASWLHPDA 210
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 211 PV-EVEVENLEELDEALKAGADIIMLDNFETEQMREAVK---RTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKH 286
Cdd:pfam01729 81 VKiEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEeldERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 476961649 287 VQALDLSMR 295
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-295 |
2.76e-71 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 222.29 E-value: 2.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 22 DIPGAVAQALREDLGGTVDANndiTAKLLPENSRSHATVITRENGVFCGKRWVEEVFiQLAGDDVTIIWHVDDGDVINAN 101
Cdd:PLN02716 18 DIEAVIKLALAEDAGDRGDVT---CLATIPGDMEAEATFLAKADGVLAGIALADMVF-EEVDPSLKVEWAAIDGDFVHKG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 102 QPLFELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNtqLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSD 181
Cdd:PLN02716 94 LKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 182 AFLIKENHIIASGSVRQAVEKA-SWLHP---DAPVEVEVENLEELDEAL------KAGADIIMLDNFETEQ--------- 242
Cdd:PLN02716 172 MVMIKDNHIAAAGGITNAVQSAdKYLEEkglSMKIEVETRTLEEVKEVLeylsdtKTSLTRVMLDNMVVPLengdvdvsm 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 476961649 243 MREAVKRTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMR 295
Cdd:PLN02716 252 LKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
13-296 |
8.58e-33 |
|
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: 121.64 E-value: 8.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 13 DELLERInldipgavaqaLREDLGGtvdanNDITAKLLP-ENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWH 91
Cdd:cd01573 1 DAELERL-----------LLEDAPY-----GDLTTEALGiGEQPGKITFRARDPGVLCGTEEAARILELL---GLEVDLA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 92 VDDGDVINANQPLFELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTN--TQLLDTRKTLPGLRS-ALKyAVL 168
Cdd:cd01573 62 AASGSRVAAGAVLLEAEGPAAALHLGWKVAQTLLEWASGIATATAEMVAAARAVNpdIVVATTRKAFPGTRKlALK-AIL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 169 CGGGANHRLGLSDAFLIKENH--IIASGSVRQAVEKaswLHPDAPVEVEVENLEELDEALK---AGADIIMLDNFETEQM 243
Cdd:cd01573 141 AGGAVPHRLGLSETILVFAEHraFLGGPEPLKALAR---LRATAPEKKIVVEVDSLEEALAaaeAGADILQLDKFSPEEL 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 476961649 244 REAVKRTNGKA---LLEVSGNVTDKTLREFAETGVDFISVGALTkHVQALDLSMRF 296
Cdd:cd01573 218 AELVPKLRSLAppvLLAAAGGINIENAAAYAAAGADILVTSAPY-YAKPADIKVKI 272
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
44-129 |
2.78e-25 |
|
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: 96.41 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 44 DITAK-LLPENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWHVDDGDVINANQPLFELEGPSRVLLTGERTAL 122
Cdd:pfam02749 5 DLTTEaLIPGDKKAKAVIIAKEEGVVAGLEEAERVFELL---GLEVEWLVKDGDRVEAGDVILEIEGPARALLTAERVAL 81
|
....*..
gi 476961649 123 NFVQTLS 129
Cdd:pfam02749 82 NLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
31-275 |
4.15e-19 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 85.16 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 31 LREDLGGtvdanNDITAKLLP-ENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWHVDDGDVINANQPLFELEG 109
Cdd:PRK06096 13 LLEDIQG-----GDLTTRALGiGHQPGYIEFFHRQGGCVSGISVACKMLTTL---GLTIDDAVSDGSQANAGQRLISAQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 110 PSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTN--TQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKE 187
Cdd:PRK06096 85 NAAALHQGWKAVQNVLEWSCGVSDYLAQMLALLRERYpdGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 188 NH-----------IIASGSVRQAVEKASWLHPDAPVEVEvenleeldEALKAGADIIMLDNFETEQMREA---VKRTNGK 253
Cdd:PRK06096 165 NHrhflhdpqdwsGAINQLRRHAPEKKIVVEADTPKEAI--------AALRAQPDVLQLDKFSPQQATEIaqiAPSLAPH 236
|
250 260
....*....|....*....|..
gi 476961649 254 ALLEVSGNVTDKTLREFAETGV 275
Cdd:PRK06096 237 CTLSLAGGINLNTLKNYADCGI 258
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
31-282 |
1.20e-17 |
|
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: 80.72 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 31 LREDLGGtvdanNDITAKLLP-ENSRSHATVITRENGVFCGKRWVEEVFIQLagdDVTIIWHVDDGDVINANQPLFELEG 109
Cdd:TIGR01334 12 LLEDIGY-----GDLTTRALGiQDHPAHITFTARDEGIVSGVSEAAKLLKQL---GASIDYAVPSGSRALAGTLLLEAKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 110 PSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQ--LLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKE 187
Cdd:TIGR01334 84 SAGQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMavVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 188 NHIIA-------SGSV----RQAVEKASWLHPDAPVEVEvenleeldEALKAGADIIMLDNFETEQMREAVKRT---NGK 253
Cdd:TIGR01334 164 NHRTFlndnfdwGGAIgrlkQTAPERKITVEADTIEQAL--------TVLQASPDILQLDKFTPQQLHHLHERLkffDHI 235
|
250 260
....*....|....*....|....*....
gi 476961649 254 ALLEVSGNVTDKTLREFAETGVDFISVGA 282
Cdd:TIGR01334 236 PTLAAAGGINPENIADYIEAGIDLFITSA 264
|
|
| NAPRTase_B |
cd01571 |
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ... |
48-171 |
4.79e-06 |
|
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: 47.27 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 476961649 48 KLLPENSRSHATVITREN--GVFCGkrwVEEVFIQLAGDDVTIiWHVDDGDVINANQPLFELEGPSRVLLTGERTALNFV 125
Cdd:cd01571 16 EKKGPNPTVTMEFTQRSLpwAVLCG---LEEVLALLEGLPVKV-YALPEGTIFNPKEPVLRIEGPYQDFGELETAILGIL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 476961649 126 QTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGG 171
Cdd:cd01571 92 ARASSIATNAARVKLAAGDKPVISFGDRRDHPAIQPMDGRAAYIGG 137
|
|
| PRK07188 |
PRK07188 |
nicotinate phosphoribosyltransferase; Provisional |
63-110 |
3.37e-03 |
|
nicotinate phosphoribosyltransferase; Provisional
Pssm-ID: 235953 [Multi-domain] Cd Length: 352 Bit Score: 38.39 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 476961649 63 RENGVFCGkrwVEEV--FIQLAGDDVT--IIWHVDDGDVINANQPLFELEGP 110
Cdd:PRK07188 47 RENAVLCG---TDEViaLLKTFAKDPSklKIRYLKDGDIINPFETVLEIEGP 95
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
84-108 |
5.43e-03 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 35.04 E-value: 5.43e-03
10 20
....*....|....*....|....*.
gi 476961649 84 DDVTII-WHVDDGDVINANQPLFELE 108
Cdd:COG0508 15 TEGTIVeWLVKEGDTVKEGDPLAEVE 40
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
84-108 |
8.47e-03 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 34.30 E-value: 8.47e-03
10 20
....*....|....*....|....*.
gi 476961649 84 DDVTII-WHVDDGDVINANQPLFELE 108
Cdd:cd06849 13 TEGTIVeWLVKEGDSVEEGDVLAEVE 38
|
|
| |
