|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
10-282 |
3.62e-160 |
|
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: 446.39 E-value: 3.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 10 LIESIKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEV 89
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 90 EGSTHSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKD 169
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 170 NHIKGAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIheqAPHVKVEASGNVS 249
Cdd:COG0157 161 NHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALL---RGRALLEASGGIT 237
|
250 260 270
....*....|....*....|....*....|...
gi 1011417753 250 LDTIRGIAESGVDVISVGRLTYSFESLDISLDL 282
Cdd:COG0157 238 LENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-281 |
2.74e-156 |
|
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: 436.14 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEVEGST 93
Cdd:cd01572 4 VRLALAEDLGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 94 HSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIK 173
Cdd:cd01572 84 RSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 174 GAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEqapHVKVEASGNVSLDTI 253
Cdd:cd01572 164 AAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKG---RVLLEASGGITLENI 240
|
250 260
....*....|....*....|....*...
gi 1011417753 254 RGIAESGVDVISVGRLTYSFESLDISLD 281
Cdd:cd01572 241 RAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
14-282 |
1.95e-129 |
|
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: 368.12 E-value: 1.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDpgLVFTPMVKDGDAVKSGTILAEVEGST 93
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 94 HSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIK 173
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 174 GAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQaphVKVEASGNVSLDTI 253
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNL 236
|
250 260
....*....|....*....|....*....
gi 1011417753 254 RGIAESGVDVISVGRLTYSFESLDISLDL 282
Cdd:TIGR00078 237 EEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
14-280 |
1.21e-102 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 302.02 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVG-AGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEVEGS 92
Cdd:PLN02716 23 IKLALAEDAGdRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 93 THSLLTGERLALNLLQRMSGIATRTRTYVDALNglSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHI 172
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 173 KGAGGITEAVQRARAIIPHT---MTIEVETENLEQVKEALQ------SGADIIMLDNMH--PDQMREAVSLIHEQAPHV- 240
Cdd:PLN02716 181 AAAGGITNAVQSADKYLEEKglsMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVvpLENGDVDVSMLKEAVELIn 260
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1011417753 241 ---KVEASGNVSLDTIRGIAESGVDVISVGRLTYSFESLDISL 280
Cdd:PLN02716 261 grfETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISL 303
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
113-281 |
2.93e-82 |
|
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: 244.91 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 113 IATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIKGAGGITEAVQRARAIIPHT 192
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 193 MTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQAPHVKVEASGNVSLDTIRGIAESGVDVISVGRLTYS 272
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 1011417753 273 FESLDISLD 281
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
10-282 |
3.62e-160 |
|
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: 446.39 E-value: 3.62e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 10 LIESIKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEV 89
Cdd:COG0157 1 IDELIRRALAEDLGYGDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 90 EGSTHSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKD 169
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 170 NHIKGAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIheqAPHVKVEASGNVS 249
Cdd:COG0157 161 NHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALL---RGRALLEASGGIT 237
|
250 260 270
....*....|....*....|....*....|...
gi 1011417753 250 LDTIRGIAESGVDVISVGRLTYSFESLDISLDL 282
Cdd:COG0157 238 LENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-281 |
2.74e-156 |
|
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: 436.14 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEVEGST 93
Cdd:cd01572 4 VRLALAEDLGRGDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATVEGPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 94 HSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIK 173
Cdd:cd01572 84 RSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDNHIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 174 GAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEqapHVKVEASGNVSLDTI 253
Cdd:cd01572 164 AAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKG---RVLLEASGGITLENI 240
|
250 260
....*....|....*....|....*...
gi 1011417753 254 RGIAESGVDVISVGRLTYSFESLDISLD 281
Cdd:cd01572 241 RAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
14-281 |
2.01e-143 |
|
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: 403.78 E-value: 2.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDpGLVFTPMVKDGDAVKSGTILAEVEGST 93
Cdd:cd01568 4 LDRALAEDLGYGDLTTEALIPGDAPATATLIAKEEGVLAGLEVAEEVFELLD-GIEVEWLVKDGDRVEAGQVLLEVEGPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 94 HSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIK 173
Cdd:cd01568 83 RSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDNHIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 174 GAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIhEQAPHVKVEASGNVSLDTI 253
Cdd:cd01568 163 AAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLL-KGLPRVLLEASGGITLENI 241
|
250 260
....*....|....*....|....*...
gi 1011417753 254 RGIAESGVDVISVGRLTYSFESLDISLD 281
Cdd:cd01568 242 RAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
14-282 |
1.95e-129 |
|
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: 368.12 E-value: 1.95e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDpgLVFTPMVKDGDAVKSGTILAEVEGST 93
Cdd:TIGR00078 2 LDRWLREDLGSGDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEGPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 94 HSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIK 173
Cdd:TIGR00078 80 RSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 174 GAGGITEAVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQaphVKVEASGNVSLDTI 253
Cdd:TIGR00078 160 AAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNL 236
|
250 260
....*....|....*....|....*....
gi 1011417753 254 RGIAESGVDVISVGRLTYSFESLDISLDL 282
Cdd:TIGR00078 237 EEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
14-280 |
1.21e-102 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 302.02 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVG-AGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVDPGLVFTPMVKDGDAVKSGTILAEVEGS 92
Cdd:PLN02716 23 IKLALAEDAGdRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVHKGLKFGKVTGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 93 THSLLTGERLALNLLQRMSGIATRTRTYVDALNglSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHI 172
Cdd:PLN02716 103 AHSILVAERVVLNFMQRMSGIATLTKAMADAAK--PACILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 173 KGAGGITEAVQRARAIIPHT---MTIEVETENLEQVKEALQ------SGADIIMLDNMH--PDQMREAVSLIHEQAPHV- 240
Cdd:PLN02716 181 AAAGGITNAVQSADKYLEEKglsMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVvpLENGDVDVSMLKEAVELIn 260
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1011417753 241 ---KVEASGNVSLDTIRGIAESGVDVISVGRLTYSFESLDISL 280
Cdd:PLN02716 261 grfETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISL 303
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
26-281 |
7.96e-83 |
|
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: 250.62 E-value: 7.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 26 DVTTSVTI----PAGSQSKAIIHAKDN--GIIAGITVAELVFQVVD-PGLVFTPMVKDGDAVKSGTILAEVEGSTHSLLT 98
Cdd:cd00516 1 DLYKLTMIqaypPPDTRATAEFTAREDpyGVLAGLEEALELLELLRfPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 99 GERLALNLLQRMSGIATRTRTYVDALNGLSTRLVD--TRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIKGAG 176
Cdd:cd00516 81 LERVLLNLLQRLSGIATATARYVEAAKGANTKVHDfgTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 177 GIT------EAVQRARAIIP--HTMTIEVETENLEQVKEALQSG-ADIIMLDNMHPDQMREAV-------SLIHEQAPHV 240
Cdd:cd00516 161 SIIqafgelAAVKALRRWLPelFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVlilkaraHLDGKGLPRV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1011417753 241 KVEASGNVSLDTIRGIAESGVDVISVGRLTYSFESLDISLD 281
Cdd:cd00516 241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
113-281 |
2.93e-82 |
|
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: 244.91 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 113 IATRTRTYVDALNGLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNHIKGAGGITEAVQRARAIIPHT 192
Cdd:pfam01729 1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 193 MTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQAPHVKVEASGNVSLDTIRGIAESGVDVISVGRLTYS 272
Cdd:pfam01729 81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160
|
....*....
gi 1011417753 273 FESLDISLD 281
Cdd:pfam01729 161 VPPLDISLD 169
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
11-278 |
3.71e-47 |
|
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: 159.00 E-value: 3.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 11 IESIKSWLREDVGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVdpGLVFTPMVKDGDAVKSGTILAEVE 90
Cdd:cd01573 1 DAELERLLLEDAPYGDLTTEALGIGEQPGKITFRARDPGVLCGTEEAARILELL--GLEVDLAAASGSRVAAGAVLLEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 91 GSTHSLLTGERLALNLLQRMSGIATRTRTYVDA---LNgLSTRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMI 167
Cdd:cd01573 79 GPAAALHLGWKVAQTLLEWASGIATATAEMVAAaraVN-PDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 168 KDNHIKGAGGITE--AVQRARAIIPHTmTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQAPHVKVEAS 245
Cdd:cd01573 158 FAEHRAFLGGPEPlkALARLRATAPEK-KIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPVLLAAA 236
|
250 260 270
....*....|....*....|....*....|...
gi 1011417753 246 GNVSLDTIRGIAESGVDVIsVGRLTYSFESLDI 278
Cdd:cd01573 237 GGINIENAAAYAAAGADIL-VTSAPYYAKPADI 268
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
17-261 |
5.46e-32 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 119.44 E-value: 5.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 17 WLREDVGAGDVTTSvTIPAGSQSKAI-IHAKDNGIIAGITVAELVFQVVdpGLVFTPMVKDGDAVKSGTILAEVEGSTHS 95
Cdd:PRK06096 12 LLLEDIQGGDLTTR-ALGIGHQPGYIeFFHRQGGCVSGISVACKMLTTL--GLTIDDAVSDGSQANAGQRLISAQGNAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 96 LLTGERLALNLLQRMSGIATRTRTYVDALNGL--STRLVDTRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDNH-- 171
Cdd:PRK06096 89 LHQGWKAVQNVLEWSCGVSDYLAQMLALLRERypDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrh 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 172 -IKGAGGITEAVQRARAIIPHTmTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQAPHVKVEASGNVSL 250
Cdd:PRK06096 169 fLHDPQDWSGAINQLRRHAPEK-KIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSLAPHCTLSLAGGINL 247
|
250
....*....|.
gi 1011417753 251 DTIRGIAESGV 261
Cdd:PRK06096 248 NTLKNYADCGI 258
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
14-264 |
1.05e-31 |
|
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: 118.85 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 14 IKSWLREDVGAGDVTTSvTIPAGSQSKAI-IHAKDNGIIAGITVAELVFQVVdpGLVFTPMVKDGDAVKSGTILAEVEGS 92
Cdd:TIGR01334 8 IDNLLLEDIGYGDLTTR-ALGIQDHPAHItFTARDEGIVSGVSEAAKLLKQL--GASIDYAVPSGSRALAGTLLLEAKGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 93 THSLLTGERLALNLLQRMSGIATRTRTYVDALNGLSTRLVD--TRKTTPGHRLLEKYAVRVGGGSNHRFGLYDAVMIKDN 170
Cdd:TIGR01334 85 AGQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVacTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFAN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 171 H---IKGAGGITEAVQRARAIIPHTmTIEVETENLEQVKEALQSGADIIMLDNMHPDQMREAVSLIHEQAPHVKVEASGN 247
Cdd:TIGR01334 165 HrtfLNDNFDWGGAIGRLKQTAPER-KITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGG 243
|
250
....*....|....*..
gi 1011417753 248 VSLDTIRGIAESGVDVI 264
Cdd:TIGR01334 244 INPENIADYIEAGIDLF 260
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
22-111 |
2.55e-30 |
|
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: 109.12 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 22 VGAGDVTTSVTIPAGSQSKAIIHAKDNGIIAGITVAELVFQVVdpGLVFTPMVKDGDAVKSGTILAEVEGSTHSLLTGER 101
Cdd:pfam02749 1 IGRGDLTTEALIPGDKKAKAVIIAKEEGVVAGLEEAERVFELL--GLEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78
|
90
....*....|
gi 1011417753 102 LALNLLQRMS 111
Cdd:pfam02749 79 VALNLLQRLS 88
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
185-274 |
5.53e-06 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 46.09 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 185 ARAIIPHTMTIEVETENLEQVKEALQSGADIIMLDNMHPDQMR---------EAVSLIHEQAPHVKVEASGNVSLDTIRG 255
Cdd:TIGR00693 89 ARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKkdpappagvELLREIAATLIDIPIVAIGGITLENAAE 168
|
90
....*....|....*....
gi 1011417753 256 IAESGVDVISVGRLTYSFE 274
Cdd:TIGR00693 169 VLAAGADGVAVVSAIMQAA 187
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
181-266 |
5.63e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 43.25 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011417753 181 AVQRARAIIPHTMTIEVETENLEQVKEALQSGADIIML---------DNMHPDQMREAVSLIHEQAPHVKVEASGNVSLD 251
Cdd:PRK00043 93 PVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVgpifptptkKDAKAPQGLEGLREIRAAVGDIPIVAIGGITPE 172
|
90
....*....|....*
gi 1011417753 252 TIRGIAESGVDVISV 266
Cdd:PRK00043 173 NAPEVLEAGADGVAV 187
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
227-279 |
1.19e-03 |
|
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.
Pssm-ID: 238244 Cd Length: 211 Bit Score: 39.39 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1011417753 227 REAVSLIHEQAPHVKVEASGNVSLDTIRGIAESGVDVISVGrlTYSFESLDIS 279
Cdd:cd00429 154 RKLRELIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAG--SALFGSDDYA 204
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
206-267 |
3.73e-03 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 38.73 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011417753 206 KEALQSGADIIMLDNMHPDQ--MREAVSLIHEQAPHVKVEASGNVSLDTIRGIAESGVDVISVG 267
Cdd:PRK07807 233 RALLEAGVDVLVVDTAHGHQekMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVG 296
|
|
| RlhA |
COG0826 |
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family ... |
201-242 |
6.86e-03 |
|
23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family [Translation, ribosomal structure and biogenesis]; 23S rRNA C2501 and tRNA U34 5'-hydroxylation protein RlhA/YrrN/YrrO, U32 peptidase family is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440588 Cd Length: 311 Bit Score: 37.43 E-value: 6.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1011417753 201 NLEQVKEALQSGADIIML-----------DNMHPDQMREAVSLIHEQapHVKV 242
Cdd:COG0826 12 SLEALKAAVEAGADAVYIggkrfnararaGNFSLEELAEAVEYAHER--GKKV 62
|
|
| |
