|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
1-273 |
1.63e-134 |
|
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439927 [Multi-domain] Cd Length: 272 Bit Score: 380.90 E-value: 1.63e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 1 MRKAVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLIV 80
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 81 EGDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKE 160
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 161 NHLALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLA 240
Cdd:COG0157 161 NHIAAAG-GIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLE 239
|
250 260 270
....*....|....*....|....*....|...
gi 1125448618 241 TVREIAAAGPDFISIGALTHSAPAANLSMDILP 273
Cdd:COG0157 240 NIRAYAETGVDYISVGALTHSAPALDLSLRIEP 272
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
2-270 |
4.22e-127 |
|
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
Pssm-ID: 238806 [Multi-domain] Cd Length: 268 Bit Score: 362.18 E-value: 4.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 2 RKAVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLIVE 81
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 82 GDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKEN 161
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 162 HLALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLAT 241
Cdd:cd01572 161 HIAAAG-SITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLEN 239
|
250 260
....*....|....*....|....*....
gi 1125448618 242 VREIAAAGPDFISIGALTHSAPAANLSMD 270
Cdd:cd01572 240 IRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
4-271 |
1.42e-100 |
|
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: 294.93 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 4 AVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDrsVKVVRTVRDGLTIEGESPVLIVEGD 83
Cdd:TIGR00078 1 LLDRWLREDLGSGDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 84 ARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHL 163
Cdd:TIGR00078 79 ARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 164 ALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLATVR 243
Cdd:TIGR00078 159 AAAG-SIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLE 237
|
250 260
....*....|....*....|....*...
gi 1125448618 244 EIAAAGPDFISIGALTHSAPAANLSMDI 271
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-271 |
1.29e-77 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 238.08 E-value: 1.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 1 MRKAVQVALEEDLG-QGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLI 79
Cdd:PLN02716 19 IEAVIKLALAEDAGdRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 80 VEGDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRgyRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIK 159
Cdd:PLN02716 99 VTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 160 ENHLALAGhDVASACRLAREGAAH---GLKIEVEAQTLDEVRAALD------GQADIILLDNM---------DVPSIRTA 221
Cdd:PLN02716 177 DNHIAAAG-GITNAVQSADKYLEEkglSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDVSMLKEA 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1125448618 222 VDLIKGRALVEVSGGVTLATVREIAAAGPDFISIGALTHSAPAANLSMDI 271
Cdd:PLN02716 256 VELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
104-270 |
1.37e-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: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 104 IATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLALAGhDVASACRLAREGAAH 183
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAG-SITEAVRRARQVAPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 184 GLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIK---GRALVEVSGGVTLATVREIAAAGPDFISIGALTH 260
Cdd:pfam01729 80 AVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDernPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTH 159
|
170
....*....|
gi 1125448618 261 SAPAANLSMD 270
Cdd:pfam01729 160 SVPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
1-273 |
1.63e-134 |
|
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439927 [Multi-domain] Cd Length: 272 Bit Score: 380.90 E-value: 1.63e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 1 MRKAVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLIV 80
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 81 EGDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKE 160
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 161 NHLALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLA 240
Cdd:COG0157 161 NHIAAAG-GIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLE 239
|
250 260 270
....*....|....*....|....*....|...
gi 1125448618 241 TVREIAAAGPDFISIGALTHSAPAANLSMDILP 273
Cdd:COG0157 240 NIRAYAETGVDYISVGALTHSAPALDLSLRIEP 272
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
2-270 |
4.22e-127 |
|
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
Pssm-ID: 238806 [Multi-domain] Cd Length: 268 Bit Score: 362.18 E-value: 4.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 2 RKAVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLIVE 81
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 82 GDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKEN 161
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 162 HLALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLAT 241
Cdd:cd01572 161 HIAAAG-SITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLEN 239
|
250 260
....*....|....*....|....*....
gi 1125448618 242 VREIAAAGPDFISIGALTHSAPAANLSMD 270
Cdd:cd01572 240 IRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
2-270 |
2.92e-115 |
|
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: 332.13 E-value: 2.92e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 2 RKAVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDrSVKVVRTVRDGLTIEGESPVLIVE 81
Cdd:cd01568 1 DALLDRALAEDLGYGDLTTEALIPGDAPATATLIAKEEGVLAGLEVAEEVFELLD-GIEVEWLVKDGDRVEAGQVLLEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 82 GDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKEN 161
Cdd:cd01568 80 GPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 162 HLALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKG--RALVEVSGGVTL 239
Cdd:cd01568 160 HIAAAG-GITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITL 238
|
250 260 270
....*....|....*....|....*....|.
gi 1125448618 240 ATVREIAAAGPDFISIGALTHSAPAANLSMD 270
Cdd:cd01568 239 ENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
4-271 |
1.42e-100 |
|
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: 294.93 E-value: 1.42e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 4 AVQVALEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDrsVKVVRTVRDGLTIEGESPVLIVEGD 83
Cdd:TIGR00078 1 LLDRWLREDLGSGDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 84 ARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHL 163
Cdd:TIGR00078 79 ARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 164 ALAGhDVASACRLAREGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRALVEVSGGVTLATVR 243
Cdd:TIGR00078 159 AAAG-SIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLE 237
|
250 260
....*....|....*....|....*...
gi 1125448618 244 EIAAAGPDFISIGALTHSAPAANLSMDI 271
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
1-271 |
1.29e-77 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 238.08 E-value: 1.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 1 MRKAVQVALEEDLG-QGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVVRTVRDGLTIEGESPVLI 79
Cdd:PLN02716 19 IEAVIKLALAEDAGdRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 80 VEGDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRgyRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIK 159
Cdd:PLN02716 99 VTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 160 ENHLALAGhDVASACRLAREGAAH---GLKIEVEAQTLDEVRAALD------GQADIILLDNM---------DVPSIRTA 221
Cdd:PLN02716 177 DNHIAAAG-GITNAVQSADKYLEEkglSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDVSMLKEA 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1125448618 222 VDLIKGRALVEVSGGVTLATVREIAAAGPDFISIGALTHSAPAANLSMDI 271
Cdd:PLN02716 256 VELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
17-270 |
4.33e-69 |
|
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: 215.18 E-value: 4.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 17 DATTAALF----PKPVPARGTIVA--HEAMTVAGVAAARQTFLAVD-RSVKVVRTVRDGLTIEGESPVLIVEGDARSLLM 89
Cdd:cd00516 1 DLYKLTMIqaypPPDTRATAEFTAreDPYGVLAGLEEALELLELLRfPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 90 AERVSLNFLQHLSGIATLTARFCQAVRG--YRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLALAG 167
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYVEAAKGanTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 168 -----HDVASACRLARE--GAAHGLKIEVEAQTLDEVRAALD-GQADIILLDNMDVPSIRTAVDLIKGRA---------- 229
Cdd:cd00516 161 siiqaFGELAAVKALRRwlPELFIALIDVEVDTLEEALEAAKaGGADGIRLDSGSPEELDPAVLILKARAhldgkglprv 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1125448618 230 LVEVSGGVTLATVREIAAAGPDFISIGALTHSAPAANLSMD 270
Cdd:cd00516 241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
104-270 |
1.37e-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: 1.37e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 104 IATLTARFCQAVRGYRVKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLALAGhDVASACRLAREGAAH 183
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAG-SITEAVRRARQVAPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 184 GLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIK---GRALVEVSGGVTLATVREIAAAGPDFISIGALTH 260
Cdd:pfam01729 80 AVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDernPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTH 159
|
170
....*....|
gi 1125448618 261 SAPAANLSMD 270
Cdd:pfam01729 160 SVPPLDISLD 169
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
9-264 |
5.52e-48 |
|
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: 160.54 E-value: 5.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 9 LEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDrsVKVVRTVRDGLTIEGESPVLIVEGDARSLL 88
Cdd:cd01573 8 LLEDAPYGDLTTEALGIGEQPGKITFRARDPGVLCGTEEAARILELLG--LEVDLAAASGSRVAAGAVLLEAEGPAAALH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 89 MAERVSLNFLQHLSGIATLTARFCQAVRGYR--VKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLALA 166
Cdd:cd01573 86 LGWKVAQTLLEWASGIATATAEMVAAARAVNpdIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHRAFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 167 GHDvASACRLAR-EGAAHGLKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRA---LVEVSGGVTLATV 242
Cdd:cd01573 166 GGP-EPLKALARlRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAppvLLAAAGGINIENA 244
|
250 260
....*....|....*....|..
gi 1125448618 243 REIAAAGPDFISIGALTHSAPA 264
Cdd:cd01573 245 AAYAAAGADILVTSAPYYAKPA 266
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
9-271 |
1.38e-27 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 107.50 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 9 LEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVvrTVRDGLTIEGESPVLIVEGDARSLL 88
Cdd:PRK06096 13 LLEDIQGGDLTTRALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDD--AVSDGSQANAGQRLISAQGNAAALH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 89 MAERVSLNFLQHLSGIATLTARFCQAVRGYRVK--ILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLALA 166
Cdd:PRK06096 91 QGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDgnIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHRHFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 167 GHD---VASACRLAREgaAHGLKIEVEAQTLDEVRAALDGQADIILLDNM---DVPSIRTAVDLIKGRALVEVSGGVTLA 240
Cdd:PRK06096 171 HDPqdwSGAINQLRRH--APEKKIVVEADTPKEAIAALRAQPDVLQLDKFspqQATEIAQIAPSLAPHCTLSLAGGINLN 248
|
250 260 270
....*....|....*....|....*....|.
gi 1125448618 241 TVREIAAAGpdfisIGALTHSAPAANLSMDI 271
Cdd:PRK06096 249 TLKNYADCG-----IRLFITSAPYYAAPADI 274
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
13-102 |
1.33e-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: 89.09 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 13 LGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDrsVKVVRTVRDGLTIEGESPVLIVEGDARSLLMAER 92
Cdd:pfam02749 1 IGRGDLTTEALIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLG--LEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78
|
90
....*....|
gi 1125448618 93 VSLNFLQHLS 102
Cdd:pfam02749 79 VALNLLQRLS 88
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
9-264 |
4.68e-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: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 9 LEEDLGQGDATTAALFPKPVPARGTIVAHEAMTVAGVAAARQTFLAVDRSVKVvrTVRDGLTIEGESPVLIVEGDARSLL 88
Cdd:TIGR01334 12 LLEDIGYGDLTTRALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDY--AVPSGSRALAGTLLLEAKGSAGQLH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 89 MAERVSLNFLQHLSGIATLTARFCQAVRGYR--VKILDTRKTTPGLRALEKWAVRLGGGRNHRHSLSDGILIKENHLAL- 165
Cdd:TIGR01334 90 QGWKSAQSVLEWSCGVATYTHKMVTLAKKISpmAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANHRTFl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 166 -AGHDVASACRLAREGAAHGlKIEVEAQTLDEVRAALDGQADIILLDNMDVPSIRTAVDLIKGRA---LVEVSGGVTLAT 241
Cdd:TIGR01334 170 nDNFDWGGAIGRLKQTAPER-KITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDhipTLAAAGGINPEN 248
|
250 260
....*....|....*....|...
gi 1125448618 242 VREIAAAGPDFISIGALTHSAPA 264
Cdd:TIGR01334 249 IADYIEAGIDLFITSAPYYAAPC 271
|
|
| NAPRTase_B |
cd01571 |
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate ... |
53-271 |
6.83e-06 |
|
Nicotinate phosphoribosyltransferase (NAPRTase), subgroup B. Nicotinate phosphoribosyltransferase catalyses the formation of NAMN and PPi from 5-phosphoribosy -1-pyrophosphate (PRPP) and nicotinic acid, this is the first, and also rate limiting, reaction in the NAD salvage synthesis. This salvage pathway serves to recycle NAD degradation products.
Pssm-ID: 238805 [Multi-domain] Cd Length: 302 Bit Score: 46.50 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 53 LAVDRSVKV-VRTVRDGLTIEGESPVLIVEGDARSLLMAERVSLNFLQHLSGIATLTARFCQAVRGYRVKILDTRKTTPG 131
Cdd:cd01571 45 LALLEGLPVkVYALPEGTIFNPKEPVLRIEGPYQDFGELETAILGILARASSIATNAARVKLAAGDKPVISFGDRRDHPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 132 LRALEKWAVRLGGGRNHRHSLSDGILIKEN-----HlALA---GHDVASACRLAREgaahGLKIEVEAQTL-----DEVR 198
Cdd:cd01571 125 IQPMDGRAAYIGGCDGVSTVLGAELLGEKPsgtmpH-ALIqifGGDQVEAWKAFDE----TYPEDVPRIALidtfnDEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125448618 199 AALDgQADIIL--LD--NMDVPS------------IRTAVDlIKGRALVE--VSGGVTLATVREIAAAGPDFISIGALTH 260
Cdd:cd01571 200 EALK-AAKALGdkLDgvRLDTPSsrrgvfrylireVRWALD-IRGYKHVKifVSGGLDEEDIKELEDVGVDAFGVGTAIS 277
|
250
....*....|.
gi 1125448618 261 SAPAANLSMDI 271
Cdd:cd01571 278 KAPPVDFTMDI 288
|
|
| |
