|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
12-279 |
3.29e-141 |
|
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: 397.85 E-value: 3.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 12 IQINIQQALQEDIGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQEGDRVAANEAFLKL 90
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALiPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 91 AGSARSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKE 170
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 171 NHIMAAGGIAQAIAKAHQ-IAPGKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIEN 249
Cdd:COG0157 161 NHIAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLEN 240
|
250 260 270
....*....|....*....|....*....|
gi 445949072 250 LREVATTGVDYISMGVLTKDVKAVDLSMRF 279
Cdd:COG0157 241 IRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-278 |
1.40e-130 |
|
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: 371.04 E-value: 1.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 15 NIQQALQEDIGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQEGDRVAANEAFLKLAGS 93
Cdd:cd01572 3 IVRLALAEDLGRGDITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 94 ARSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHI 173
Cdd:cd01572 83 ARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 174 MAAGGIAQAIAKAHQIAP-GKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIENLRE 252
Cdd:cd01572 163 AAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENIRA 242
|
250 260
....*....|....*....|....*.
gi 445949072 253 VATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:cd01572 243 YAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
16-279 |
5.33e-104 |
|
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: 303.41 E-value: 5.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 16 IQQALQEDIGDGDITAM-LTPEDEQATATIISREDMVLAGQPWVNALISAYDntVQVTWLKQEGDRVAANEAFLKLAGSA 94
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 95 RSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHIM 174
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 175 AAGGIAQAIAKAHQIAP-GKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIENLREV 253
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 445949072 254 ATTGVDYISMGVLTKDVKAVDLSMRF 279
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-278 |
9.28e-82 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 248.48 E-value: 9.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 1 MSIPQSLLEQ-SIQINIQQALQEDIGD-GDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQE 77
Cdd:PLN02716 7 MAIPPPSHPTyDIEAVIKLALAEDAGDrGDVTCLATiPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 78 GDRVAANEAFLKLAGSARSLLTVERPALNFIQTLSAVATKTAEYVQHLEglNTKLLDTRKTLPGLRIAQKYAVTVGGGQN 157
Cdd:PLN02716 87 GDFVHKGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 158 HRLGLFDAFLIKENHIMAAGGIAQAIAKAHQIAPGK----PVEVEVETWDELNQALE------AGADIVMLDNFSQQQ-- 225
Cdd:PLN02716 165 HRMGLFDMVMIKDNHIAAAGGITNAVQSADKYLEEKglsmKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVVPLen 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 226 -------MIDAVKHVAGRCKLEASGNITIENLREVATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:PLN02716 245 gdvdvsmLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
114-278 |
3.16e-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: 196.38 E-value: 3.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 114 VATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHIMAAGGIAQAIAKAHQIAP-G 192
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 193 KPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHV---AGRCKLEASGNITIENLREVATTGVDYISMGVLTKD 269
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELderNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 445949072 270 VKAVDLSMR 278
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
12-279 |
3.29e-141 |
|
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: 397.85 E-value: 3.29e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 12 IQINIQQALQEDIGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQEGDRVAANEAFLKL 90
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALiPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 91 AGSARSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKE 170
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 171 NHIMAAGGIAQAIAKAHQ-IAPGKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIEN 249
Cdd:COG0157 161 NHIAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLEN 240
|
250 260 270
....*....|....*....|....*....|
gi 445949072 250 LREVATTGVDYISMGVLTKDVKAVDLSMRF 279
Cdd:COG0157 241 IRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-278 |
1.40e-130 |
|
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: 371.04 E-value: 1.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 15 NIQQALQEDIGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQEGDRVAANEAFLKLAGS 93
Cdd:cd01572 3 IVRLALAEDLGRGDITSEAIiPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 94 ARSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHI 173
Cdd:cd01572 83 ARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 174 MAAGGIAQAIAKAHQIAP-GKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIENLRE 252
Cdd:cd01572 163 AAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENIRA 242
|
250 260
....*....|....*....|....*.
gi 445949072 253 VATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:cd01572 243 YAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
16-278 |
2.91e-118 |
|
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: 339.84 E-value: 2.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 16 IQQALQEDIGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNtVQVTWLKQEGDRVAANEAFLKLAGSA 94
Cdd:cd01568 4 LDRALAEDLGYGDLTTEALiPGDAPATATLIAKEEGVLAGLEVAEEVFELLDG-IEVEWLVKDGDRVEAGQVLLEVEGPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 95 RSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHIM 174
Cdd:cd01568 83 RSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDNHIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 175 AAGGIAQAIAKAHQIAP-GKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAG--RCKLEASGNITIENLR 251
Cdd:cd01568 163 AAGGITEAVKRARAAAPfEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITLENIR 242
|
250 260
....*....|....*....|....*..
gi 445949072 252 EVATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:cd01568 243 AYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
16-279 |
5.33e-104 |
|
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: 303.41 E-value: 5.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 16 IQQALQEDIGDGDITAM-LTPEDEQATATIISREDMVLAGQPWVNALISAYDntVQVTWLKQEGDRVAANEAFLKLAGSA 94
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 95 RSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHIM 174
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 175 AAGGIAQAIAKAHQIAP-GKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGRCKLEASGNITIENLREV 253
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 445949072 254 ATTGVDYISMGVLTKDVKAVDLSMRF 279
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-278 |
9.28e-82 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 248.48 E-value: 9.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 1 MSIPQSLLEQ-SIQINIQQALQEDIGD-GDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTWLKQE 77
Cdd:PLN02716 7 MAIPPPSHPTyDIEAVIKLALAEDAGDrGDVTCLATiPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 78 GDRVAANEAFLKLAGSARSLLTVERPALNFIQTLSAVATKTAEYVQHLEglNTKLLDTRKTLPGLRIAQKYAVTVGGGQN 157
Cdd:PLN02716 87 GDFVHKGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 158 HRLGLFDAFLIKENHIMAAGGIAQAIAKAHQIAPGK----PVEVEVETWDELNQALE------AGADIVMLDNFSQQQ-- 225
Cdd:PLN02716 165 HRMGLFDMVMIKDNHIAAAGGITNAVQSADKYLEEKglsmKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVVPLen 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 226 -------MIDAVKHVAGRCKLEASGNITIENLREVATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:PLN02716 245 gdvdvsmLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLK 304
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
28-278 |
2.14e-67 |
|
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: 210.94 E-value: 2.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 28 DITAMLT-----PEDEQATATIISRED--MVLAGQPWVNALISAYDNT-VQVTWLKQEGDRVAANEAFLKLAGSARSLLT 99
Cdd:cd00516 1 DLYKLTMiqaypPPDTRATAEFTAREDpyGVLAGLEEALELLELLRFPgPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 100 VERPALNFIQTLSAVATKTAEYVQHLEGLNTKL--LDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHI---- 173
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYVEAAKGANTKVhdFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGtmah 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 174 --MAAGGIAQAIAKAHQIAPG---KPVEVEVETWDELNQALEAG-ADIVMLDNFSQQQMIDAVK----------HVAGRC 237
Cdd:cd00516 161 siIQAFGELAAVKALRRWLPElfiALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLilkarahldgKGLPRV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 445949072 238 KLEASGNITIENLREVATTGVDYISMGVLTKDVKAVDLSMR 278
Cdd:cd00516 241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
114-278 |
3.16e-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: 196.38 E-value: 3.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 114 VATKTAEYVQHLEGLNTKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENHIMAAGGIAQAIAKAHQIAP-G 192
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 193 KPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHV---AGRCKLEASGNITIENLREVATTGVDYISMGVLTKD 269
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELderNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 445949072 270 VKAVDLSMR 278
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
20-261 |
9.03e-42 |
|
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: 144.75 E-value: 9.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 20 LQEDIGDGDITA-MLTPEDEQATATIISREDMVLAGQPWVNALISAYDntVQVTWLKQEGDRVAANEAFLKLAGSARSLL 98
Cdd:cd01573 8 LLEDAPYGDLTTeALGIGEQPGKITFRARDPGVLCGTEEAARILELLG--LEVDLAAASGSRVAAGAVLLEAEGPAAALH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 99 TVERPALNFIQTLSAVATKTAEYVQHLEGLNTKL--LDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENH--IM 174
Cdd:cd01573 86 LGWKVAQTLLEWASGIATATAEMVAAARAVNPDIvvATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHraFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 175 AAGGIAQAIAKAHQIAPGKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDAVKHVAGR---CKLEASGNITIENLR 251
Cdd:cd01573 166 GGPEPLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLappVLLAAAGGINIENAA 245
|
250
....*....|
gi 445949072 252 EVATTGVDYI 261
Cdd:cd01573 246 AYAAAGADIL 255
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
24-112 |
4.61e-26 |
|
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: 97.95 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 24 IGDGDITAMLT-PEDEQATATIISREDMVLAGQPWVNALISAYDntVQVTWLKQEGDRVAANEAFLKLAGSARSLLTVER 102
Cdd:pfam02749 1 IGRGDLTTEALiPGDKKAKAVIIAKEEGVVAGLEEAERVFELLG--LEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78
|
90
....*....|
gi 445949072 103 PALNFIQTLS 112
Cdd:pfam02749 79 VALNLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
20-258 |
2.81e-23 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 95.95 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 20 LQEDIGDGDITA-MLTPEDEQATATIISREDMVLAGQPWVNALISAYDntVQVTWLKQEGDRVAANEAFLKLAGSARSLL 98
Cdd:PRK06096 13 LLEDIQGGDLTTrALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLG--LTIDDAVSDGSQANAGQRLISAQGNAAALH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 99 TVERPALNFIQTLSAVATKTAEYVQHLEGLNTK--LLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENH---I 173
Cdd:PRK06096 91 QGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDgnIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrhfL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 174 MAAGGIAQAIAKAHQIAPGKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDA---VKHVAGRCKLEASGNITIENL 250
Cdd:PRK06096 171 HDPQDWSGAINQLRRHAPEKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIaqiAPSLAPHCTLSLAGGINLNTL 250
|
....*...
gi 445949072 251 REVATTGV 258
Cdd:PRK06096 251 KNYADCGI 258
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
16-261 |
4.87e-22 |
|
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: 92.66 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 16 IQQALQEDIGDGDITA-MLTPEDEQATATIISREDMVLAGQPWVNALISAYDNTVQVTwlKQEGDRVAANEAFLKLAGSA 94
Cdd:TIGR01334 8 IDNLLLEDIGYGDLTTrALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYA--VPSGSRALAGTLLLEAKGSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 95 RSLLTVERPALNFIQTLSAVATKTAEYVQHLEGLN--TKLLDTRKTLPGLRIAQKYAVTVGGGQNHRLGLFDAFLIKENH 172
Cdd:TIGR01334 86 GQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISpmAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 173 ---IMAAGGIAQAIAKAHQIAPGKPVEVEVETWDELNQALEAGADIVMLDNFSQQQMIDA---VKHVAGRCKLEASGNIT 246
Cdd:TIGR01334 166 rtfLNDNFDWGGAIGRLKQTAPERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLherLKFFDHIPTLAAAGGIN 245
|
250
....*....|....*
gi 445949072 247 IENLREVATTGVDYI 261
Cdd:TIGR01334 246 PENIADYIEAGIDLF 260
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
192-269 |
8.90e-04 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 39.42 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445949072 192 GKPVEVEVETWDELNQALEAGADIVMLDNFSQQ--QMIDAVKHVAGRCKLEASGNITIENLREVATTGVDYISMG-VLTK 268
Cdd:cd00452 97 GIPLLPGVATPTEIMQALELGADIVKLFPAEAVgpAYIKALKGPFPQVRFMPTGGVSLDNAAEWLAAGVVAVGGGsLLPK 176
|
.
gi 445949072 269 D 269
Cdd:cd00452 177 D 177
|
|
| |
