|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
17-293 |
1.03e-137 |
|
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: 389.69 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 17 DVTNWLSEDVPSFDFG--GYVVGSDLKEANLYCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPSKndsgkiVVAK 94
Cdd:TIGR00078 1 LLDRWLREDLGSGDITteALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGE------VVAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 95 ITGPAKNILLAERTALNILSRSSGIATASHKIISLARSTGykGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVM 174
Cdd:TIGR00078 75 VEGPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 175 LKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKwngkkhFLLE 254
Cdd:TIGR00078 153 IKDNHIAAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR------VLLE 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 398364399 255 CSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKL 293
Cdd:TIGR00078 227 ASGGITLDNLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-292 |
5.50e-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: 369.88 E-value: 5.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 15 RQDVTNWLSEDVPSFDFGGYVV--GSDLKEANLYCKQDGMLCGVPFAQEVFNQC--ELQVEWLFKEGSFLEPskndsgKI 90
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEAIipPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEP------GQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 91 VVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLS 170
Cdd:cd01572 75 VLATVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 171 SMVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNkwngkkH 250
Cdd:cd01572 153 DAVLIKDNHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKG------R 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 398364399 251 FLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLK 292
Cdd:cd01572 227 VLLEASGGITLENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
15-293 |
4.68e-103 |
|
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: 301.94 E-value: 4.68e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 15 RQDVTNWLSEDVPSFD-FGGYVVGSDLK-EANLYCKQDGMLCGVPFAQEVFNQC--ELQVEWLFKEGSFLEPskNDsgki 90
Cdd:COG0157 2 DELIRRALAEDLGYGDlTTEALIPADARaRARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEA--GD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 91 VVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLS 170
Cdd:COG0157 76 VLLEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVA--GTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 171 SMVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLknkwngKKH 250
Cdd:COG0157 154 DAVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALL------RGR 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 398364399 251 FLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKL 293
Cdd:COG0157 228 ALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
119-292 |
4.16e-87 |
|
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: 257.62 E-value: 4.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 119 IATASHKIISLARSTgyKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNARAVCG 198
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 199 FAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKWNGkkhFLLECSGGLNLDNLEEYLCDDIDIYSTS 278
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPR---VLLEVSGGVTLDNVLEYAKTGVDVISVG 155
|
170
....*....|....
gi 398364399 279 SIHQGTPVIDFSLK 292
Cdd:pfam01729 156 ALTHSVPPLDISLD 169
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-295 |
5.94e-86 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 259.65 E-value: 5.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 1 MPVYEHLLP---VNGAWRQdvtnWLSEDVPS---FDFGGYVVGSDLKEANLYCKQDGMLCGVPFAQEVFNQC--ELQVEW 72
Cdd:PLN02716 7 MAIPPPSHPtydIEAVIKL----ALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVdpSLKVEW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 73 LFKEGSFLEpskndsGKIVVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstgyKGTIAGTRKTTPGLRRL 152
Cdd:PLN02716 83 AAIDGDFVH------KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK----PACILETRKTAPGLRLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 153 EKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNAR---AVCGFAVKIEVECLSEDEATEAIE------AGADV 223
Cdd:PLN02716 153 DKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVQSADkylEEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364399 224 IMLDNFKG--DGLKMCAQSLKNKW---NGKkhFLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKLAH 295
Cdd:PLN02716 233 VMLDNMVVplENGDVDVSMLKEAVeliNGR--FETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKIDT 307
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
17-293 |
1.03e-137 |
|
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: 389.69 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 17 DVTNWLSEDVPSFDFG--GYVVGSDLKEANLYCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPSKndsgkiVVAK 94
Cdd:TIGR00078 1 LLDRWLREDLGSGDITteALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGE------VVAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 95 ITGPAKNILLAERTALNILSRSSGIATASHKIISLARSTGykGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVM 174
Cdd:TIGR00078 75 VEGPARSLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 175 LKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKwngkkhFLLE 254
Cdd:TIGR00078 153 IKDNHIAAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR------VLLE 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 398364399 255 CSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKL 293
Cdd:TIGR00078 227 ASGGITLDNLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-292 |
5.50e-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: 369.88 E-value: 5.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 15 RQDVTNWLSEDVPSFDFGGYVV--GSDLKEANLYCKQDGMLCGVPFAQEVFNQC--ELQVEWLFKEGSFLEPskndsgKI 90
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEAIipPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEP------GQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 91 VVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLS 170
Cdd:cd01572 75 VLATVEGPARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 171 SMVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNkwngkkH 250
Cdd:cd01572 153 DAVLIKDNHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKG------R 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 398364399 251 FLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLK 292
Cdd:cd01572 227 VLLEASGGITLENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
15-292 |
2.02e-122 |
|
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: 351.01 E-value: 2.02e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 15 RQDVTNWLSEDVPSFDFGGYVV--GSDLKEANLYCKQDGMLCGVPFAQEVFNQC-ELQVEWLFKEGSFLEPskndsgKIV 91
Cdd:cd01568 1 DALLDRALAEDLGYGDLTTEALipGDAPATATLIAKEEGVLAGLEVAEEVFELLdGIEVEWLVKDGDRVEA------GQV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 92 VAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARSTgyKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSS 171
Cdd:cd01568 75 LLEVEGPARSLLTAERVALNLLQRLSGIATATRRYVEAARGT--KARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 172 MVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKnkwnGKKHF 251
Cdd:cd01568 153 AVLIKDNHIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLK----GLPRV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 398364399 252 LLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLK 292
Cdd:cd01568 229 LLEASGGITLENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
15-293 |
4.68e-103 |
|
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: 301.94 E-value: 4.68e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 15 RQDVTNWLSEDVPSFD-FGGYVVGSDLK-EANLYCKQDGMLCGVPFAQEVFNQC--ELQVEWLFKEGSFLEPskNDsgki 90
Cdd:COG0157 2 DELIRRALAEDLGYGDlTTEALIPADARaRARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEA--GD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 91 VVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLS 170
Cdd:COG0157 76 VLLEVEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVA--GTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 171 SMVMLKDNHIWATGSITNAVKNARAVCGFAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLknkwngKKH 250
Cdd:COG0157 154 DAVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALL------RGR 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 398364399 251 FLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKL 293
Cdd:COG0157 228 ALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
119-292 |
4.16e-87 |
|
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: 257.62 E-value: 4.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 119 IATASHKIISLARSTgyKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNARAVCG 198
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 199 FAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKWNGkkhFLLECSGGLNLDNLEEYLCDDIDIYSTS 278
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPR---VLLEVSGGVTLDNVLEYAKTGVDVISVG 155
|
170
....*....|....
gi 398364399 279 SIHQGTPVIDFSLK 292
Cdd:pfam01729 156 ALTHSVPPLDISLD 169
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-295 |
5.94e-86 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 259.65 E-value: 5.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 1 MPVYEHLLP---VNGAWRQdvtnWLSEDVPS---FDFGGYVVGSDLKEANLYCKQDGMLCGVPFAQEVFNQC--ELQVEW 72
Cdd:PLN02716 7 MAIPPPSHPtydIEAVIKL----ALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVdpSLKVEW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 73 LFKEGSFLEpskndsGKIVVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLARstgyKGTIAGTRKTTPGLRRL 152
Cdd:PLN02716 83 AAIDGDFVH------KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK----PACILETRKTAPGLRLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 153 EKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNAR---AVCGFAVKIEVECLSEDEATEAIE------AGADV 223
Cdd:PLN02716 153 DKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVQSADkylEEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364399 224 IMLDNFKG--DGLKMCAQSLKNKW---NGKkhFLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTPVIDFSLKLAH 295
Cdd:PLN02716 233 VMLDNMVVplENGDVDVSMLKEAVeliNGR--FETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKIDT 307
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
42-292 |
1.27e-79 |
|
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: 242.53 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 42 EANLYCKQD--GMLCGVPFAQEVFNQC---ELQVEWLFKEGSFLEPskndsgKIVVAKITGPAKNILLAERTALNILSRS 116
Cdd:cd00516 19 TAEFTAREDpyGVLAGLEEALELLELLrfpGPLVILAVPEGTVVEP------GEPLLTIEGPARELLLLERVLLNLLQRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 117 SGIATASHKIISLARSTGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSIT------NAV 190
Cdd:cd00516 93 SGIATATARYVEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSIIqafgelAAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 191 KNARAVCG--FAVKIEVECLSEDEATEAIEAG-ADVIMLDNFKGDGLKMCAQSLKNKW----NGKKHFLLECSGGLNLDN 263
Cdd:cd00516 173 KALRRWLPelFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARAhldgKGLPRVKIEASGGLDEEN 252
|
250 260
....*....|....*....|....*....
gi 398364399 264 LEEYLCDDIDIYSTSSIHQGTPVIDFSLK 292
Cdd:cd00516 253 IRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
20-293 |
1.61e-39 |
|
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: 139.36 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 20 NWLSEDVPSFDFGGYVVGSDLKEANL--YCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPskndsGKIVVAkITG 97
Cdd:cd01573 6 RLLLEDAPYGDLTTEALGIGEQPGKItfRARDPGVLCGTEEAARILELLGLEVDLAAASGSRVAA-----GAVLLE-AEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 98 PAKNILLAERTALNILSRSSGIATASHKIISLARSTGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKD 177
Cdd:cd01573 80 PAAALHLGWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 178 NH--IWATGSITNAVKNARAVCGfAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKWNGKkhfLLEC 255
Cdd:cd01573 160 EHraFLGGPEPLKALARLRATAP-EKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPV---LLAA 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 398364399 256 SGGLNLDNLEEYLCDDIDIYSTSSIHQGTPViDFSLKL 293
Cdd:cd01573 236 AGGINIENAAAYAAAGADILVTSAPYYAKPA-DIKVKI 272
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
42-117 |
1.89e-22 |
|
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: 88.70 E-value: 1.89e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364399 42 EANLYCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPskNDsgkiVVAKITGPAKNILLAERTALNILSRSS 117
Cdd:pfam02749 19 KAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVKDGDRVEA--GD----VILEIEGPARALLTAERVALNLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
20-285 |
2.55e-22 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 94.02 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 20 NWLSEDVPSFDFGGYVVGSDLKEANL--YCKQDGMLCGVPFAQEVFNQCELQVEWLFKEGSFLEPskndsGKIVVAkITG 97
Cdd:PRK06096 11 ALLLEDIQGGDLTTRALGIGHQPGYIefFHRQGGCVSGISVACKMLTTLGLTIDDAVSDGSQANA-----GQRLIS-AQG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 98 PAKNILLAERTALNILSRSSGIATASHKIISLARSTGYKGTIAGTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKD 177
Cdd:PRK06096 85 NAAALHQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 178 NH--IWA-----TGSITNAVKNARavcgfAVKIEVECLSEDEATEAIEAGADVIMLDNFKGDGLKMCAQSLKNKwngKKH 250
Cdd:PRK06096 165 NHrhFLHdpqdwSGAINQLRRHAP-----EKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSL---APH 236
|
250 260 270
....*....|....*....|....*....|....*
gi 398364399 251 FLLECSGGLNLDNLEEYLCDDIDIYSTSSIHQGTP 285
Cdd:PRK06096 237 CTLSLAGGINLNTLKNYADCGIRLFITSAPYYAAP 271
|
|
| NAPRTase_B |
cd01571 |
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ... |
50-293 |
1.02e-11 |
|
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: 64.22 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 50 DGMLCGVPFAQEVFNQCELQVEWLfKEGSFLEPskndsgKIVVAKITGPAKNILLAERTALNILSRSSGIATASHKIISL 129
Cdd:cd01571 35 WAVLCGLEEVLALLEGLPVKVYAL-PEGTIFNP------KEPVLRIEGPYQDFGELETAILGILARASSIATNAARVKLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 130 ArstGYKGTIA-GTRKTTPGLRRLEKYSMLVGGCDTHRYDLSSMVMLKDnhiwATGSITNA---------VKNARAvcgF 199
Cdd:cd01571 108 A---GDKPVISfGDRRDHPAIQPMDGRAAYIGGCDGVSTVLGAELLGEK----PSGTMPHAliqifggdqVEAWKA---F 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 200 AVKIEVECLS-------EDEATEAIEAGA------DVIMLDNFKGDGLKMCAQSLKNKW----NGKKHFLLECSGGLNLD 262
Cdd:cd01571 178 DETYPEDVPRialidtfNDEKEEALKAAKalgdklDGVRLDTPSSRRGVFRYLIREVRWaldiRGYKHVKIFVSGGLDEE 257
|
250 260 270
....*....|....*....|....*....|.
gi 398364399 263 NLEEYLCDDIDIYSTSSIHQGTPVIDFSLKL 293
Cdd:cd01571 258 DIKELEDVGVDAFGVGTAISKAPPVDFTMDI 288
|
|
| PRK08662 |
PRK08662 |
nicotinate phosphoribosyltransferase; Reviewed |
51-291 |
1.32e-05 |
|
nicotinate phosphoribosyltransferase; Reviewed
Pssm-ID: 236328 [Multi-domain] Cd Length: 343 Bit Score: 46.02 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 51 GMLCGVPFAQEVFNQCELQVeWLFKEGSFLEPskndsgKIVVAKITGPAKNILLAERTALNILSRSSGIATASHKIISLA 130
Cdd:PRK08662 53 GVFAGLEEVLELLEGKPVDV-YALPEGTLFDP------KEPVMRIEGPYLEFGIYETALLGILAHASGIATAAARCKEAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 131 rstGYKGTIA-GTRKTTPGLRRLEKYSMLVGGCDthryDLSSMVMLKDNHIWATGSITNA--------VKNARAvcgF-- 199
Cdd:PRK08662 126 ---GDKPVLSfGARHVHPAIAPMMDRAAYIGGCD----GVSGVLGAELLGIEPSGTMPHAlilifgdqVEAWKA---Fde 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364399 200 AVKIEVECLS-----EDEATEAIEAGA------DVIMLD-------NFKGdglkmCAQSLknKWN----GKKHFLLECSG 257
Cdd:PRK08662 196 VVPPDVPRIAlvdtfKDEREEALRAAEalgdrlDGVRLDtpssrrgNFRK-----IVREV--RWTldirGYEHVKIFVSG 268
|
250 260 270
....*....|....*....|....*....|....*
gi 398364399 258 GLNLDNLEEyLCDDIDIYST-SSIHQGTPvIDFSL 291
Cdd:PRK08662 269 GLDPERIRE-LRDVVDGFGVgTYISFAPP-VDFSM 301
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
207-268 |
2.08e-03 |
|
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: 38.27 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364399 207 CLSEDEATEAIEAGADVIMLDNFKGDGLKMcAQSLKnkwnGK-KHFLLECSGGLNLDNLEEYL 268
Cdd:cd00452 104 VATPTEIMQALELGADIVKLFPAEAVGPAY-IKALK----GPfPQVRFMPTGGVSLDNAAEWL 161
|
|
| |
