|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
13-281 |
1.49e-152 |
|
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: 426.74 E-value: 1.49e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 13 IEANVRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQVLFHL 91
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEaLIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 92 EGPARSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKE 171
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 172 NHIAACGGIAQAIDAAHK-IAPGKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINEST 250
Cdd:COG0157 161 NHIAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLEN 240
|
250 260 270
....*....|....*....|....*....|.
gi 829035479 251 LLPIAQTGVDYISIGAMTKDVKAVDLSMRLS 281
Cdd:COG0157 241 IRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-279 |
2.47e-144 |
|
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: 405.71 E-value: 2.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 14 EANVRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQVLFHLE 92
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEaIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 93 GPARSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKEN 172
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 173 HIAACGGIAQAIDAAHKIAP-GKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINESTL 251
Cdd:cd01572 161 HIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENI 240
|
250 260
....*....|....*....|....*...
gi 829035479 252 LPIAQTGVDYISIGAMTKDVKAVDLSMR 279
Cdd:cd01572 241 RAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
17-280 |
6.99e-107 |
|
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: 310.73 E-value: 6.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 17 VRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVLFHLEGPA 95
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 96 RSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENHIA 175
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 176 ACGGIAQAIDAAHKIAP-GKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINESTLLPI 254
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 829035479 255 AQTGVDYISIGAMTKDVKAVDLSMRL 280
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
10-282 |
1.93e-81 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 247.71 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 10 TAEIEANVRRALAEDIGS-GDIT-ARLIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQV 87
Cdd:PLN02716 16 TYDIEAVIKLALAEDAGDrGDVTcLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 88 LFHLEGPARSLLSGERSALNFLQMLSGVATHARQLADhvADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAF 167
Cdd:PLN02716 96 FGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMAD--AAKPACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 168 LIKENHIAACGGIAQAIDAAHKI--APGKPVEIEVE--SLDELREALA------AGADIIMLD---------ELSLDDMR 228
Cdd:PLN02716 174 MIKDNHIAAAGGITNAVQSADKYleEKGLSMKIEVEtrTLEEVKEVLEylsdtkTSLTRVMLDnmvvplengDVDVSMLK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 829035479 229 EAVRLNAGKAKLEASGGINESTLLPIAQTGVDYISIGAMTKDVKAVDLSMRLSL 282
Cdd:PLN02716 254 EAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKIDT 307
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
115-279 |
2.09e-66 |
|
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: 204.47 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 115 VATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENHIAACGGIAQAIDAAHKIAP-G 193
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 194 KPVEIEVESLDELREALAAGADIIMLDELSLDDMREAV---RLNAGKAKLEASGGINESTLLPIAQTGVDYISIGAMTKD 270
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVeelDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 829035479 271 VKAVDLSMR 279
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
13-281 |
1.49e-152 |
|
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: 426.74 E-value: 1.49e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 13 IEANVRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQVLFHL 91
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEaLIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 92 EGPARSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKE 171
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 172 NHIAACGGIAQAIDAAHK-IAPGKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINEST 250
Cdd:COG0157 161 NHIAAAGGIAEAVARARArAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLEN 240
|
250 260 270
....*....|....*....|....*....|.
gi 829035479 251 LLPIAQTGVDYISIGAMTKDVKAVDLSMRLS 281
Cdd:COG0157 241 IRAYAETGVDYISVGALTHSAPALDLSLRIE 271
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-279 |
2.47e-144 |
|
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: 405.71 E-value: 2.47e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 14 EANVRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQVLFHLE 92
Cdd:cd01572 1 DAIVRLALAEDLGRGDITSEaIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 93 GPARSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKEN 172
Cdd:cd01572 81 GPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 173 HIAACGGIAQAIDAAHKIAP-GKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINESTL 251
Cdd:cd01572 161 HIAAAGSITEAVRRARAAAPfTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENI 240
|
250 260
....*....|....*....|....*...
gi 829035479 252 LPIAQTGVDYISIGAMTKDVKAVDLSMR 279
Cdd:cd01572 241 RAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-279 |
2.57e-129 |
|
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: 367.96 E-value: 2.57e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 14 EANVRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDpRVAVHWQVVDGERVSPNQVLFHLE 92
Cdd:cd01568 1 DALLDRALAEDLGYGDLTTEaLIPGDAPATATLIAKEEGVLAGLEVAEEVFELLD-GIEVEWLVKDGDRVEAGQVLLEVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 93 GPARSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKEN 172
Cdd:cd01568 80 GPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 173 HIAACGGIAQAIDAAHKIAP-GKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAG--KAKLEASGGINES 249
Cdd:cd01568 160 HIAAAGGITEAVKRARAAAPfEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITLE 239
|
250 260 270
....*....|....*....|....*....|
gi 829035479 250 TLLPIAQTGVDYISIGAMTKDVKAVDLSMR 279
Cdd:cd01568 240 NIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
17-280 |
6.99e-107 |
|
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: 310.73 E-value: 6.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 17 VRRALAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVLFHLEGPA 95
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 96 RSLLSGERSALNFLQMLSGVATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENHIA 175
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 176 ACGGIAQAIDAAHKIAP-GKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAKLEASGGINESTLLPI 254
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPfTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEEY 239
|
250 260
....*....|....*....|....*.
gi 829035479 255 AQTGVDYISIGAMTKDVKAVDLSMRL 280
Cdd:TIGR00078 240 AETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
10-282 |
1.93e-81 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 247.71 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 10 TAEIEANVRRALAEDIGS-GDIT-ARLIPAERLAKATIITRDAAVISGTAWVDAVFRQLDPRVAVHWQVVDGERVSPNQV 87
Cdd:PLN02716 16 TYDIEAVIKLALAEDAGDrGDVTcLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 88 LFHLEGPARSLLSGERSALNFLQMLSGVATHARQLADhvADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAF 167
Cdd:PLN02716 96 FGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMAD--AAKPACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 168 LIKENHIAACGGIAQAIDAAHKI--APGKPVEIEVE--SLDELREALA------AGADIIMLD---------ELSLDDMR 228
Cdd:PLN02716 174 MIKDNHIAAAGGITNAVQSADKYleEKGLSMKIEVEtrTLEEVKEVLEylsdtkTSLTRVMLDnmvvplengDVDVSMLK 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 829035479 229 EAVRLNAGKAKLEASGGINESTLLPIAQTGVDYISIGAMTKDVKAVDLSMRLSL 282
Cdd:PLN02716 254 EAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKIDT 307
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
29-279 |
8.95e-72 |
|
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.
Pssm-ID: 238286 [Multi-domain] Cd Length: 281 Bit Score: 222.12 E-value: 8.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 29 DITARLI-----PAERLAKATIITRDA--AVISGTAWVDAVFRQLD-PRVAVHWQVVDGERVSPNQVLFHLEGPARSLLS 100
Cdd:cd00516 1 DLYKLTMiqaypPPDTRATAEFTAREDpyGVLAGLEEALELLELLRfPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 101 GERSALNFLQMLSGVATHARQLADHVAD--TQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENHIAACG 178
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYVEAAKGanTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 179 GIAQ------AIDAAHKIAPG---KPVEIEVESLDELREALAAG-ADIIMLDELSLDDMREAVRLNAG----------KA 238
Cdd:cd00516 161 SIIQafgelaAVKALRRWLPElfiALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKArahldgkglpRV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 829035479 239 KLEASGGINESTLLPIAQTGVDYISIGAMTKDVKAVDLSMR 279
Cdd:cd00516 241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
115-279 |
2.09e-66 |
|
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: 204.47 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 115 VATHARQLADHVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENHIAACGGIAQAIDAAHKIAP-G 193
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPfA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 194 KPVEIEVESLDELREALAAGADIIMLDELSLDDMREAV---RLNAGKAKLEASGGINESTLLPIAQTGVDYISIGAMTKD 270
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVeelDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 829035479 271 VKAVDLSMR 279
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
10-266 |
1.33e-45 |
|
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: 154.76 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 10 TAEIEanvrRALAEDIGSGDITARLIP-AERLAKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVL 88
Cdd:cd01573 1 DAELE----RLLLEDAPYGDLTTEALGiGEQPGKITFRARDPGVLCGTEEAARILELLG--LEVDLAAASGSRVAAGAVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 89 FHLEGPARSLLSGERSALNFLQMLSGVATHARQLAD--HVADTQVKLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDA 166
Cdd:cd01573 75 LEAEGPAAALHLGWKVAQTLLEWASGIATATAEMVAaaRAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 167 FLIKENHIAACGG--IAQAIDAAHKIAPGKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAK---LE 241
Cdd:cd01573 155 ILVFAEHRAFLGGpePLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPpvlLA 234
|
250 260
....*....|....*....|....*
gi 829035479 242 ASGGINESTLLPIAQTGVDYISIGA 266
Cdd:cd01573 235 AAGGINIENAAAYAAAGADILVTSA 259
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
21-259 |
4.95e-32 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 119.44 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 21 LAEDIGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVLFHLEGPARSLL 99
Cdd:PRK06096 13 LLEDIQGGDLTTRaLGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLG--LTIDDAVSDGSQANAGQRLISAQGNAAALH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 100 SGERSALNFLQMLSGVATHARQLAD----HVADTQVKLldTRKTLPGLRLAQKYAVTCGGCHNHRIGLYDAFLIKENH-- 173
Cdd:PRK06096 91 QGWKAVQNVLEWSCGVSDYLAQMLAllreRYPDGNIAC--TRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrh 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 174 -IAACGGIAQAIDAAHKIAPGKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAK---LEASGGINES 249
Cdd:PRK06096 169 fLHDPQDWSGAINQLRRHAPEKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSLAPhctLSLAGGINLN 248
|
250
....*....|
gi 829035479 250 TLLPIAQTGV 259
Cdd:PRK06096 249 TLKNYADCGI 258
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
25-113 |
1.36e-27 |
|
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The N-terminal domain has an alpha/beta hammerhead fold.
Pssm-ID: 460674 [Multi-domain] Cd Length: 88 Bit Score: 102.19 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 25 IGSGDITAR-LIPAERLAKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVLFHLEGPARSLLSGER 103
Cdd:pfam02749 1 IGRGDLTTEaLIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLG--LEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78
|
90
....*....|
gi 829035479 104 SALNFLQMLS 113
Cdd:pfam02749 79 VALNLLQRLS 88
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
10-266 |
2.15e-25 |
|
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: 101.90 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 10 TAEIEAnvrrALAEDIGSGDITARLIPAERL-AKATIITRDAAVISGTAWVDAVFRQLDprVAVHWQVVDGERVSPNQVL 88
Cdd:TIGR01334 5 TGLIDN----LLLEDIGYGDLTTRALGIQDHpAHITFTARDEGIVSGVSEAAKLLKQLG--ASIDYAVPSGSRALAGTLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 89 FHLEGPARSLLSGERSALNFLQMLSGVATHARQ---LADHVADTQVkLLDTRKTLPGLRLAQKYAVTCGGCHNHRIGLYD 165
Cdd:TIGR01334 79 LEAKGSAGQLHQGWKSAQSVLEWSCGVATYTHKmvtLAKKISPMAV-VACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829035479 166 AFLIKENH---IAACGGIAQAIDAAHKIAPGKPVEIEVESLDELREALAAGADIIMLDELSLDDMREAVRLNAGKAK--- 239
Cdd:TIGR01334 158 TLLVFANHrtfLNDNFDWGGAIGRLKQTAPERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHipt 237
|
250 260
....*....|....*....|....*..
gi 829035479 240 LEASGGINESTLLPIAQTGVDYISIGA 266
Cdd:TIGR01334 238 LAAAGGINPENIADYIEAGIDLFITSA 264
|
|
| |
