|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
2-273 |
1.46e-116 |
|
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: 335.06 E-value: 1.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 2 LLKEIEAFLEEDVGHEDY--EEIVPYTS-CKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTI 76
Cdd:COG0157 1 IDELIRRALAEDLGYGDLttEALIPADArARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 77 SGAGAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAvnERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVII 156
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAG--TGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 157 KDNHIKLMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLlnvraVRDRVIVEAS 235
Cdd:COG0157 159 KDNHIAAAGgIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVAL-----LRGRALLEAS 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1904408593 236 GGIDMANIKEFASTGVDVISIGMITHSARWLGFSMNVV 273
Cdd:COG0157 234 GGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
3-271 |
2.66e-114 |
|
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: 329.44 E-value: 2.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 3 LKEIEAFLEEDVGHEDYEE---IVPYTSCKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTIS 77
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSeaiIPPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 78 GAGAKILKAERLVLNFLGRMSGVATLTDRCVNEVRavNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIK 157
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 158 DNHIKLMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLlnvraVRDRVIVEASG 236
Cdd:cd01572 159 DNHIAAAGsITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVAL-----LKGRVLLEASG 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1904408593 237 GIDMANIKEFASTGVDVISIGMITHSARWLGFSMN 271
Cdd:cd01572 234 GITLENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
6-272 |
2.05e-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: 304.18 E-value: 2.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 6 IEAFLEEDVGHEDY--EEIVPY-TSCKAEIQVKEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILTISGAGAK 82
Cdd:TIGR00078 2 LDRWLREDLGSGDIttEALVPGsTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPARS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 83 ILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNERvlVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHIK 162
Cdd:TIGR00078 82 LLTAERTALNFLGRLSGIATATRKYVEAARGTNVR--IADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 163 LMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLnvravRDRVIVEASGGIDMA 241
Cdd:TIGR00078 160 AAGsIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLL-----KGRVLLEASGGITLD 234
|
250 260 270
....*....|....*....|....*....|.
gi 1904408593 242 NIKEFASTGVDVISIGMITHSARWLGFSMNV 272
Cdd:TIGR00078 235 NLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
6-273 |
1.03e-63 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 202.25 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 6 IEAFLEEDVG-HEDYE---EIVPYTSCKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTISGA 79
Cdd:PLN02716 23 IKLALAEDAGdRGDVTclaTIPGDMEAEATFLAKADGVLAGIALADMVFEEVdpSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 80 GAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNervlVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDN 159
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 160 HIKLMG-LESAVKRAK---EKVSFTRKIEVEVESVEDALSVAEL------DVDIIMLDNMS--AAEVRTCVKLLN--VRA 225
Cdd:PLN02716 179 HIAAAGgITNAVQSADkylEEKGLSMKIEVETRTLEEVKEVLEYlsdtktSLTRVMLDNMVvpLENGDVDVSMLKeaVEL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1904408593 226 VRDRVIVEASGGIDMANIKEFASTGVDVISIGMITHSARWLGFSMNVV 273
Cdd:PLN02716 259 INGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKID 306
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
100-270 |
1.75e-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: 196.76 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 100 VATLTDRCVNEVRAVneRVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHIKLMG-LESAVKRAKEKVS 178
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGsITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 179 FTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLNVRAVrdRVIVEASGGIDMANIKEFASTGVDVISIGM 258
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNP--RVLLEVSGGVTLDNVLEYAKTGVDVISVGA 156
|
170
....*....|..
gi 1904408593 259 ITHSARWLGFSM 270
Cdd:pfam01729 157 LTHSVPPLDISL 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
2-273 |
1.46e-116 |
|
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: 335.06 E-value: 1.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 2 LLKEIEAFLEEDVGHEDY--EEIVPYTS-CKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTI 76
Cdd:COG0157 1 IDELIRRALAEDLGYGDLttEALIPADArARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 77 SGAGAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAvnERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVII 156
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAG--TGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 157 KDNHIKLMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLlnvraVRDRVIVEAS 235
Cdd:COG0157 159 KDNHIAAAGgIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVAL-----LRGRALLEAS 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1904408593 236 GGIDMANIKEFASTGVDVISIGMITHSARWLGFSMNVV 273
Cdd:COG0157 234 GGITLENIRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
3-271 |
2.66e-114 |
|
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: 329.44 E-value: 2.66e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 3 LKEIEAFLEEDVGHEDYEE---IVPYTSCKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTIS 77
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSeaiIPPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 78 GAGAKILKAERLVLNFLGRMSGVATLTDRCVNEVRavNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIK 157
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 158 DNHIKLMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLlnvraVRDRVIVEASG 236
Cdd:cd01572 159 DNHIAAAGsITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVAL-----LKGRVLLEASG 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1904408593 237 GIDMANIKEFASTGVDVISIGMITHSARWLGFSMN 271
Cdd:cd01572 234 GITLENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
4-271 |
1.52e-110 |
|
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: 319.81 E-value: 1.52e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 4 KEIEAFLEEDVGHEDY-EEIVPYTSCKAEIQV--KEEGVLAGLEEVKQIFDYL-SVQYSTEFEDGARLKSGDIILTISGA 79
Cdd:cd01568 2 ALLDRALAEDLGYGDLtTEALIPGDAPATATLiaKEEGVLAGLEVAEEVFELLdGIEVEWLVKDGDRVEAGQVLLEVEGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 80 GAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAvnERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDN 159
Cdd:cd01568 82 ARSLLTAERVALNLLQRLSGIATATRRYVEAARG--TKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 160 HIKLMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLnvrAVRDRVIVEASGGI 238
Cdd:cd01568 160 HIAAAGgITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLL---KGLPRVLLEASGGI 236
|
250 260 270
....*....|....*....|....*....|...
gi 1904408593 239 DMANIKEFASTGVDVISIGMITHSARWLGFSMN 271
Cdd:cd01568 237 TLENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
6-272 |
2.05e-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: 304.18 E-value: 2.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 6 IEAFLEEDVGHEDY--EEIVPY-TSCKAEIQVKEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILTISGAGAK 82
Cdd:TIGR00078 2 LDRWLREDLGSGDIttEALVPGsTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPARS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 83 ILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNERvlVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHIK 162
Cdd:TIGR00078 82 LLTAERTALNFLGRLSGIATATRKYVEAARGTNVR--IADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 163 LMG-LESAVKRAKEKVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLnvravRDRVIVEASGGIDMA 241
Cdd:TIGR00078 160 AAGsIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLL-----KGRVLLEASGGITLD 234
|
250 260 270
....*....|....*....|....*....|.
gi 1904408593 242 NIKEFASTGVDVISIGMITHSARWLGFSMNV 272
Cdd:TIGR00078 235 NLEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
24-270 |
4.58e-75 |
|
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: 230.20 E-value: 4.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 24 PYTSCKAEIQVKEE--GVLAGLEEVKQIFDYLSVQYSTEF---EDGARLKSGDIILTISGAGAKILKAERLVLNFLGRMS 98
Cdd:cd00516 14 PDTRATAEFTAREDpyGVLAGLEEALELLELLRFPGPLVIlavPEGTVVEPGEPLLTIEGPARELLLLERVLLNLLQRLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 99 GVATLTDRCVNEVRAVNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHIKLMG-------LESAVK 171
Cdd:cd00516 94 GIATATARYVEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHsiiqafgELAAVK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 172 RAKEKV--SFTRKIEVEVESVEDALSVAE-LDVDIIMLDNMSAAEVRTCVKLLNVRA-----VRDRVIVEASGGIDMANI 243
Cdd:cd00516 174 ALRRWLpeLFIALIDVEVDTLEEALEAAKaGGADGIRLDSGSPEELDPAVLILKARAhldgkGLPRVKIEASGGLDEENI 253
|
250 260
....*....|....*....|....*..
gi 1904408593 244 KEFASTGVDVISIGMITHSARWLGFSM 270
Cdd:cd00516 254 RAYAETGVDVFGVGTLLHSAPPLDIVL 280
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
6-273 |
1.03e-63 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 202.25 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 6 IEAFLEEDVG-HEDYE---EIVPYTSCKAEIQVKEEGVLAGLEEVKQIFDYL--SVQYSTEFEDGARLKSGDIILTISGA 79
Cdd:PLN02716 23 IKLALAEDAGdRGDVTclaTIPGDMEAEATFLAKADGVLAGIALADMVFEEVdpSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 80 GAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNervlVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDN 159
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 160 HIKLMG-LESAVKRAK---EKVSFTRKIEVEVESVEDALSVAEL------DVDIIMLDNMS--AAEVRTCVKLLN--VRA 225
Cdd:PLN02716 179 HIAAAGgITNAVQSADkylEEKGLSMKIEVETRTLEEVKEVLEYlsdtktSLTRVMLDNMVvpLENGDVDVSMLKeaVEL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1904408593 226 VRDRVIVEASGGIDMANIKEFASTGVDVISIGMITHSARWLGFSMNVV 273
Cdd:PLN02716 259 INGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKID 306
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
100-270 |
1.75e-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: 196.76 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 100 VATLTDRCVNEVRAVneRVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHIKLMG-LESAVKRAKEKVS 178
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGsITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 179 FTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLNVRAVrdRVIVEASGGIDMANIKEFASTGVDVISIGM 258
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNP--RVLLEVSGGVTLDNVLEYAKTGVDVISVGA 156
|
170
....*....|..
gi 1904408593 259 ITHSARWLGFSM 270
Cdd:pfam01729 157 LTHSVPPLDISL 168
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
4-254 |
8.17e-57 |
|
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: 183.27 E-value: 8.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 4 KEIEAFLEEDVGHEDY-EEIVPYTSCKAEIQV--KEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILTISGAG 80
Cdd:cd01573 2 AELERLLLEDAPYGDLtTEALGIGEQPGKITFraRDPGVLCGTEEAARILELLGLEVDLAAASGSRVAAGAVLLEAEGPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 81 AKILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNH 160
Cdd:cd01573 82 AALHLGWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 161 IKLMGLESAVKRAKE--KVSFTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLnvRAVRDRVIVEASGGI 238
Cdd:cd01573 162 RAFLGGPEPLKALARlrATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKL--RSLAPPVLLAAAGGI 239
|
250
....*....|....*.
gi 1904408593 239 DMANIKEFASTGVDVI 254
Cdd:cd01573 240 NIENAAAYAAAGADIL 255
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
5-254 |
3.11e-32 |
|
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: 119.62 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 5 EIEAFLEEDVGHEDYE-EIVPYTSCKAEIQ--VKEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILTISGAGA 81
Cdd:TIGR01334 7 LIDNLLLEDIGYGDLTtRALGIQDHPAHITftARDEGIVSGVSEAAKLLKQLGASIDYAVPSGSRALAGTLLLEAKGSAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 82 KILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVIIKDNHI 161
Cdd:TIGR01334 87 QLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 162 KLMG----LESAVKRAKEKVSfTRKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLnvrAVRDRVI-VEASG 236
Cdd:TIGR01334 167 TFLNdnfdWGGAIGRLKQTAP-ERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERL---KFFDHIPtLAAAG 242
|
250
....*....|....*...
gi 1904408593 237 GIDMANIKEFASTGVDVI 254
Cdd:TIGR01334 243 GINPENIADYIEAGIDLF 260
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
4-251 |
8.40e-24 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 97.49 E-value: 8.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 4 KEIEAFLEEDVGHEDYE------EIVPytsckAEIQV--KEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILT 75
Cdd:PRK06096 7 AQLDALLLEDIQGGDLTtralgiGHQP-----GYIEFfhRQGGCVSGISVACKMLTTLGLTIDDAVSDGSQANAGQRLIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 76 ISGAGAKILKAERLVLNFLGRMSGVATLTDRCVNEVRAVNERVLVAGTRKTTPGFRKYEKKAIAIGGGDPHRFGLYEAVI 155
Cdd:PRK06096 82 AQGNAAALHQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 156 IKDNHIKLM-------GLESAVKR-AKEKvsftrKIEVEVESVEDALSVAELDVDIIMLDNMSAAEVRTCVKLLNVRAvr 227
Cdd:PRK06096 162 LFANHRHFLhdpqdwsGAINQLRRhAPEK-----KIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSLA-- 234
|
250 260
....*....|....*....|....
gi 1904408593 228 DRVIVEASGGIDMANIKEFASTGV 251
Cdd:PRK06096 235 PHCTLSLAGGINLNTLKNYADCGI 258
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
28-98 |
4.36e-20 |
|
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: 82.15 E-value: 4.36e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904408593 28 CKAEIQVKEEGVLAGLEEVKQIFDYLSVQYSTEFEDGARLKSGDIILTISGAGAKILKAERLVLNFLGRMS 98
Cdd:pfam02749 18 AKAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVKDGDRVEAGDVILEIEGPARALLTAERVALNLLQRLS 88
|
|
| NAPRTase_B |
cd01571 |
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ... |
38-273 |
1.52e-08 |
|
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: 54.59 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 38 GVLAGLEEVKQIFDYLSVQ-YSteFEDGARLKSGDIILTISGAGAKILKAERLVLNFLGRMSGVATLTDRCVNEvrAVNE 116
Cdd:cd01571 36 AVLCGLEEVLALLEGLPVKvYA--LPEGTIFNPKEPVLRIEGPYQDFGELETAILGILARASSIATNAARVKLA--AGDK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 117 RVLVAGTRKTTPGFRKYEKKAIAIGGGDphRFGLYEAVIIKDnhIKLMG-----LESAVKRAKEKV--SFTRKIEVEVES 189
Cdd:cd01571 112 PVISFGDRRDHPAIQPMDGRAAYIGGCD--GVSTVLGAELLG--EKPSGtmphaLIQIFGGDQVEAwkAFDETYPEDVPR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 190 V----------EDALSVAEL---DVDIIMLDNMSAAevRTCVKLLnVRAVRDR--------VIVEASGGIDMANIKEFAS 248
Cdd:cd01571 188 IalidtfndekEEALKAAKAlgdKLDGVRLDTPSSR--RGVFRYL-IREVRWAldirgykhVKIFVSGGLDEEDIKELED 264
|
250 260
....*....|....*....|....*
gi 1904408593 249 TGVDVISIGMITHSARWLGFSMNVV 273
Cdd:cd01571 265 VGVDAFGVGTAISKAPPVDFTMDIV 289
|
|
| PRK08662 |
PRK08662 |
nicotinate phosphoribosyltransferase; Reviewed |
36-273 |
5.18e-03 |
|
nicotinate phosphoribosyltransferase; Reviewed
Pssm-ID: 236328 [Multi-domain] Cd Length: 343 Bit Score: 37.93 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 36 EEGVLAGLEEVKQIFDYLSVQ-YSteFEDGARLKSGDIILTISGAGAKILKAERLVLNFLGRMSGVATLTDRCVneVRAV 114
Cdd:PRK08662 51 EWGVFAGLEEVLELLEGKPVDvYA--LPEGTLFDPKEPVMRIEGPYLEFGIYETALLGILAHASGIATAAARCK--EAAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 115 NERVLVAGTRKTTPGFRKYEKKAIAIGGGD-------------------PHrfglyeAVIIkdnhikLMGLESAVKRAke 175
Cdd:PRK08662 127 DKPVLSFGARHVHPAIAPMMDRAAYIGGCDgvsgvlgaellgiepsgtmPH------ALIL------IFGDQVEAWKA-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408593 176 kvsFTRKIEVEV----------ESVEDALSVAEL---DVDIIMLD-------NMSA--AEVRtcvKLLNVRAVRDrVIVE 233
Cdd:PRK08662 193 ---FDEVVPPDVprialvdtfkDEREEALRAAEAlgdRLDGVRLDtpssrrgNFRKivREVR---WTLDIRGYEH-VKIF 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1904408593 234 ASGGIDMANIKEFASTgVDVISIGMITHSARWLGFSMNVV 273
Cdd:PRK08662 266 VSGGLDPERIRELRDV-VDGFGVGTYISFAPPVDFSMDIV 304
|
|
| |
