|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
23-297 |
8.36e-137 |
|
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: 387.45 E-value: 8.36e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 23 IPASVSHALKEDLGgdvnaDKDITAQLL-PKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVTAN 101
Cdd:COG0157 1 IDELIRRALAEDLG-----YGDLTTEALiPADARARARLIAREDGVLAGLEVAERVFRLL-DPGLEVEWLVADGDRVEAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 102 QPLFELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSD 181
Cdd:COG0157 75 DVLLEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 182 AFLIKENHIIASGSVRQAVEKAFWLHP------------DvpvevevesleELEQAIKAGADIIMLDNFETEQMREAVKL 249
Cdd:COG0157 155 AVLIKDNHIAAAGGIAEAVARARARAPpekkievevetlE-----------ELEEALAAGADIIMLDNMSPEELREAVAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 695734182 250 TNGRAQLEVSGNVTFETIREFAETGVDYISVGALTKHVRALDLSMRFK 297
Cdd:COG0157 224 LRGRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
27-295 |
1.19e-131 |
|
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: 374.51 E-value: 1.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 27 VSHALKEDLGGDvnadkDITAQLL-PKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVTANQPLF 105
Cdd:cd01572 4 VRLALAEDLGRG-----DITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELL-DPGIEVEWLVKDGDRVEPGQVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 106 ELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLI 185
Cdd:cd01572 78 TVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 186 KENHIIASGSVRQAVEKAFWLHP-DVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNGRAQLEVSGNVTF 264
Cdd:cd01572 158 KDNHIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITL 237
|
250 260 270
....*....|....*....|....*....|.
gi 695734182 265 ETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:cd01572 238 ENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
30-296 |
1.04e-115 |
|
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: 333.84 E-value: 1.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 30 ALKEDLGGDvnadkDITAQ-LLPKETRSHAVIITREDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELD 108
Cdd:TIGR00078 5 WLREDLGSG-----DITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQL---GVQVEWLVKDGDRVEPGEVVAEVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 109 GPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKEN 188
Cdd:TIGR00078 77 GPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 189 HIIASGSVRQAVEKA-FWLHPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNGRAQLEVSGNVTFETI 267
Cdd:TIGR00078 157 HIAAAGSIEKAVKRArAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNL 236
|
250 260
....*....|....*....|....*....
gi 695734182 268 REFAETGVDYISVGALTKHVRALDLSMRF 296
Cdd:TIGR00078 237 EEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-295 |
3.03e-74 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 229.99 E-value: 3.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 22 DIPASVSHALKEDLG--GDVNadkdiTAQLLPKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVT 99
Cdd:PLN02716 18 DIEAVIKLALAEDAGdrGDVT-----CLATIPGDMEAEATFLAKADGVLAGIALADMVFEEV-DPSLKVEWAAIDGDFVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 100 ANQPLFELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRtqLLDTRKTLPGLRTALKYAVLCGGGANHRLGL 179
Cdd:PLN02716 92 KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 180 SDAFLIKENHIIASGSVRQAVEKA----------FWLHPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQ------- 242
Cdd:PLN02716 170 FDMVMIKDNHIAAAGGITNAVQSAdkyleekglsMKIEVETRTLEEVKEVLEYLSDTKTSLTRVMLDNMVVPLengdvdv 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695734182 243 --MREAVKLTNGRAQLEVSGNVTFETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:PLN02716 250 smLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-295 |
2.46e-68 |
|
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: 209.86 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 131 VASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKAFWLHPDV 210
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 211 PV-EVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLT---NGRAQLEVSGNVTFETIREFAETGVDYISVGALTKH 286
Cdd:pfam01729 81 VKiEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELderNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 695734182 287 VRALDLSMR 295
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
23-297 |
8.36e-137 |
|
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: 387.45 E-value: 8.36e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 23 IPASVSHALKEDLGgdvnaDKDITAQLL-PKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVTAN 101
Cdd:COG0157 1 IDELIRRALAEDLG-----YGDLTTEALiPADARARARLIAREDGVLAGLEVAERVFRLL-DPGLEVEWLVADGDRVEAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 102 QPLFELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSD 181
Cdd:COG0157 75 DVLLEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 182 AFLIKENHIIASGSVRQAVEKAFWLHP------------DvpvevevesleELEQAIKAGADIIMLDNFETEQMREAVKL 249
Cdd:COG0157 155 AVLIKDNHIAAAGGIAEAVARARARAPpekkievevetlE-----------ELEEALAAGADIIMLDNMSPEELREAVAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 695734182 250 TNGRAQLEVSGNVTFETIREFAETGVDYISVGALTKHVRALDLSMRFK 297
Cdd:COG0157 224 LRGRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
27-295 |
1.19e-131 |
|
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: 374.51 E-value: 1.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 27 VSHALKEDLGGDvnadkDITAQLL-PKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVTANQPLF 105
Cdd:cd01572 4 VRLALAEDLGRG-----DITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELL-DPGIEVEWLVKDGDRVEPGQVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 106 ELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLI 185
Cdd:cd01572 78 TVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 186 KENHIIASGSVRQAVEKAFWLHP-DVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNGRAQLEVSGNVTF 264
Cdd:cd01572 158 KDNHIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITL 237
|
250 260 270
....*....|....*....|....*....|.
gi 695734182 265 ETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:cd01572 238 ENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
27-295 |
9.25e-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: 341.76 E-value: 9.25e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 27 VSHALKEDLGGDvnadkDITAQLL-PKETRSHAVIITREDGVFCGKRWVEEVFTQLagDDVQVTWHVEDGDAVTANQPLF 105
Cdd:cd01568 4 LDRALAEDLGYG-----DLTTEALiPGDAPATATLIAKEEGVLAGLEVAEEVFELL--DGIEVEWLVKDGDRVEAGQVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 106 ELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLI 185
Cdd:cd01568 77 EVEGPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 186 KENHIIASGSVRQAVEKAFWLHPDVPVEVE-VESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNG--RAQLEVSGNV 262
Cdd:cd01568 157 KDNHIAAAGGITEAVKRARAAAPFEKKIEVeVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGI 236
|
250 260 270
....*....|....*....|....*....|...
gi 695734182 263 TFETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:cd01568 237 TLENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
30-296 |
1.04e-115 |
|
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: 333.84 E-value: 1.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 30 ALKEDLGGDvnadkDITAQ-LLPKETRSHAVIITREDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELD 108
Cdd:TIGR00078 5 WLREDLGSG-----DITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQL---GVQVEWLVKDGDRVEPGEVVAEVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 109 GPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKEN 188
Cdd:TIGR00078 77 GPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 189 HIIASGSVRQAVEKA-FWLHPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNGRAQLEVSGNVTFETI 267
Cdd:TIGR00078 157 HIAAAGSIEKAVKRArAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNL 236
|
250 260
....*....|....*....|....*....
gi 695734182 268 REFAETGVDYISVGALTKHVRALDLSMRF 296
Cdd:TIGR00078 237 EEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-295 |
3.03e-74 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 229.99 E-value: 3.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 22 DIPASVSHALKEDLG--GDVNadkdiTAQLLPKETRSHAVIITREDGVFCGKRWVEEVFTQLaGDDVQVTWHVEDGDAVT 99
Cdd:PLN02716 18 DIEAVIKLALAEDAGdrGDVT-----CLATIPGDMEAEATFLAKADGVLAGIALADMVFEEV-DPSLKVEWAAIDGDFVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 100 ANQPLFELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRtqLLDTRKTLPGLRTALKYAVLCGGGANHRLGL 179
Cdd:PLN02716 92 KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 180 SDAFLIKENHIIASGSVRQAVEKA----------FWLHPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQ------- 242
Cdd:PLN02716 170 FDMVMIKDNHIAAAGGITNAVQSAdkyleekglsMKIEVETRTLEEVKEVLEYLSDTKTSLTRVMLDNMVVPLengdvdv 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 695734182 243 --MREAVKLTNGRAQLEVSGNVTFETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:PLN02716 250 smLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
44-295 |
7.37e-72 |
|
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: 222.89 E-value: 7.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 44 DITA-----QLLPKETRSHAVIITRED--GVFCGKRWVEEVFTQLAGDDVQVTWHVEDGDAVTANQPLFELDGPSRVLLT 116
Cdd:cd00516 1 DLYKltmiqAYPPPDTRATAEFTAREDpyGVLAGLEEALELLELLRFPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 117 GERTALNFVQTLSGVASEVRRYVDLLAGTRTQL--LDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKENHIIASG 194
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYVEAAKGANTKVhdFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 195 SVRQ------AVEKAFWLHPDVPVEVEVESLEELEQAIKA----GADIIMLDNFETEQMREAVKLTNGRAQL-------- 256
Cdd:cd00516 161 SIIQafgelaAVKALRRWLPELFIALIDVEVDTLEEALEAakagGADGIRLDSGSPEELDPAVLILKARAHLdgkglprv 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 695734182 257 --EVSGNVTFETIREFAETGVDYISVGALTKHVRALDLSMR 295
Cdd:cd00516 241 kiEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-295 |
2.46e-68 |
|
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: 209.86 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 131 VASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKAFWLHPDV 210
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 211 PV-EVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLT---NGRAQLEVSGNVTFETIREFAETGVDYISVGALTKH 286
Cdd:pfam01729 81 VKiEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELderNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 695734182 287 VRALDLSMR 295
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
31-296 |
6.63e-35 |
|
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: 127.03 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 31 LKEDLGGdvnadKDITAQLLP-KETRSHAVIITREDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELDG 109
Cdd:cd01573 8 LLEDAPY-----GDLTTEALGiGEQPGKITFRARDPGVLCGTEEAARILELL---GLEVDLAAASGSRVAAGAVLLEAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 110 PSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTR--TQLLDTRKTLPGLRT-ALKyAVLCGGGANHRLGLSDAFLIK 186
Cdd:cd01573 80 PAAALHLGWKVAQTLLEWASGIATATAEMVAAARAVNpdIVVATTRKAFPGTRKlALK-AILAGGAVPHRLGLSETILVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 187 ENH--IIASGSVRQAVEKAFWLHPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREAVKLTNGRA---QLEVSGN 261
Cdd:cd01573 159 AEHraFLGGPEPLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAppvLLAAAGG 238
|
250 260 270
....*....|....*....|....*....|....*
gi 695734182 262 VTFETIREFAETGVDYISVGALTkHVRALDLSMRF 296
Cdd:cd01573 239 INIENAAAYAAAGADILVTSAPY-YAKPADIKVKI 272
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
44-129 |
4.55e-27 |
|
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: 101.03 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 44 DITAQ-LLPKETRSHAVIITREDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELDGPSRVLLTGERTAL 122
Cdd:pfam02749 5 DLTTEaLIPGDKKAKAVIIAKEEGVVAGLEEAERVFELL---GLEVEWLVKDGDRVEAGDVILEIEGPARALLTAERVAL 81
|
....*..
gi 695734182 123 NFVQTLS 129
Cdd:pfam02749 82 NLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
63-275 |
1.22e-18 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 83.62 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 63 REDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELDGPSRVLLTGERTALNFVQTLSGVASEVRRYVDLL 142
Cdd:PRK06096 41 RQGGCVSGISVACKMLTTL---GLTIDDAVSDGSQANAGQRLISAQGNAAALHQGWKAVQNVLEWSCGVSDYLAQMLALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 143 AGT--RTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKENH-----------IIASGSVRQAVEKAFWLHPD 209
Cdd:PRK06096 118 RERypDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrhflhdpqdwsGAINQLRRHAPEKKIVVEAD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695734182 210 vpveveveSLEELEQAIKAGADIIMLDNFETEQMREAVKLT---NGRAQLEVSGNVTFETIREFAETGV 275
Cdd:PRK06096 198 --------TPKEAIAALRAQPDVLQLDKFSPQQATEIAQIApslAPHCTLSLAGGINLNTLKNYADCGI 258
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
31-282 |
4.19e-16 |
|
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: 76.48 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 31 LKEDLGGDvnadkDITAQLLPKETR-SHAVIITREDGVFCGKRWVEEVFTQLagdDVQVTWHVEDGDAVTANQPLFELDG 109
Cdd:TIGR01334 12 LLEDIGYG-----DLTTRALGIQDHpAHITFTARDEGIVSGVSEAAKLLKQL---GASIDYAVPSGSRALAGTLLLEAKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 110 PSRVLLTGERTALNFVQTLSGVASEVRRYVDLLAGTRTQ--LLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKE 187
Cdd:TIGR01334 84 SAGQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMavVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 188 NHIIA-------SGSVRQAVEKAfwlhPDVPVEVEVESLEELEQAIKAGADIIMLDNFETEQMREA---VKLTNGRAQLE 257
Cdd:TIGR01334 164 NHRTFlndnfdwGGAIGRLKQTA----PERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLherLKFFDHIPTLA 239
|
250 260
....*....|....*....|....*
gi 695734182 258 VSGNVTFETIREFAETGVDYISVGA 282
Cdd:TIGR01334 240 AAGGINPENIADYIEAGIDLFITSA 264
|
|
| NagE |
COG2190 |
Phosphotransferase system IIA component [Carbohydrate transport and metabolism]; |
57-108 |
2.51e-03 |
|
Phosphotransferase system IIA component [Carbohydrate transport and metabolism];
Pssm-ID: 441793 [Multi-domain] Cd Length: 154 Bit Score: 37.80 E-value: 2.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 695734182 57 HAVIITREDGVfcgkrwveEVFTQLAGDDVQV-----TWHVEDGDAVTANQPLFELD 108
Cdd:COG2190 61 HAIGLTSDDGL--------EVLIHIGIDTVKLngegfTVLVKEGDKVKAGDPLIEFD 109
|
|
| NAPRTase_B |
cd01571 |
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ... |
52-294 |
6.60e-03 |
|
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: 37.64 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 52 KETRSHAVIITRE--DGVFCGkrwVEEVFTQLAGDDVQVtWHVEDGDAVTANQPLFELDGPSRVLLTGERTALNFVQTLS 129
Cdd:cd01571 20 PNPTVTMEFTQRSlpWAVLCG---LEEVLALLEGLPVKV-YALPEGTIFNPKEPVLRIEGPYQDFGELETAILGILARAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 130 GVASEVRRYVDLLAGTRTQLLDTRKTLPGLRTALKYAVLCGGGANHRLGLSDAFLIKEN-----H--IIASGSVRQAVEK 202
Cdd:cd01571 96 SIATNAARVKLAAGDKPVISFGDRRDHPAIQPMDGRAAYIGGCDGVSTVLGAELLGEKPsgtmpHalIQIFGGDQVEAWK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 203 AFW-LHPDVPVEVEV--ESLEELEQAIKAGA------DIIMLD-------NFE--TEQMREAVKLtNGRAQLE--VSGNV 262
Cdd:cd01571 176 AFDeTYPEDVPRIALidTFNDEKEEALKAAKalgdklDGVRLDtpssrrgVFRylIREVRWALDI-RGYKHVKifVSGGL 254
|
250 260 270
....*....|....*....|....*....|..
gi 695734182 263 TFETIREFAETGVDYISVGALTKHVRALDLSM 294
Cdd:cd01571 255 DEEDIKELEDVGVDAFGVGTAISKAPPVDFTM 286
|
|
| arch_FMN |
cd02911 |
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent ... |
227-291 |
7.53e-03 |
|
Archeal FMN-binding domain. This family of archaeal proteins are part of the NAD(P)H-dependent flavin oxidoreductase (oxidored) FMN-binding family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN. The specific function of this group is unknown.
Pssm-ID: 239237 [Multi-domain] Cd Length: 233 Bit Score: 36.92 E-value: 7.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695734182 227 KAGADIIMLDNFETEQMREAVKLTNGRAQLEVSGN---VTFETIREFAETGVDYISVG--ALTKHVRALD 291
Cdd:cd02911 163 KAGADIIHVDAMDPGNHADLKKIRDISTELFIIGNnsvTTIESAKEMFSYGADMVSVAraSLPENIEWLV 232
|
|
| PBP2_AA_hypothetical |
cd13623 |
Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic ... |
139-203 |
7.64e-03 |
|
Substrate-binding domain of putative amino-acid transport system; the type 2 periplasmic binding protein fold; This putative amino acid-binding protein belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
Pssm-ID: 270341 [Multi-domain] Cd Length: 220 Bit Score: 36.88 E-value: 7.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695734182 139 VDLLAGTRTQLLDTRKTLPGLR------TALKYAVLCGGGANHRLGLSDAFLikeNHIIASGSVRQAVEKA 203
Cdd:cd13623 153 IDVAAGVRQQLEAMAKQHPGSRvldgrfTAIHQAIAIPKGRPAALEYLNEFV---EEAKASGLLERALQRA 220
|
|
| |
