|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
18-285 |
1.86e-124 |
|
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: 356.18 E-value: 1.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 18 LVDSWLREDCPGLNYA--ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAH 95
Cdd:TIGR00078 1 LLDRWLREDLGSGDITteALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 96 CLLLGERVALNTLARCSGIASAAAAAVEAARGAGwtGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHV 175
Cdd:TIGR00078 81 SLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 176 VAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDN 255
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDN 235
|
250 260 270
....*....|....*....|....*....|
gi 13477197 256 LPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:TIGR00078 236 LEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
4.25e-116 |
|
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: 334.83 E-value: 4.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPGLNYA--ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQL--NCQVSWFLPEGSKLVPVARVAEVRG 92
Cdd:cd01572 2 AIVRLALAEDLGRGDITseAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 93 PAHCLLLGERVALNTLARCSGIASAAAAAVEAARgaGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKD 172
Cdd:cd01572 82 PARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 173 NHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGIT 252
Cdd:cd01572 160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 13477197 253 LDNLPQFCGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
15-285 |
6.06e-93 |
|
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: 276.13 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 15 LAALVDSWLREDCPGLNY--AALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQL--NCQVSWFLPEGSKLVPVARVAEV 90
Cdd:COG0157 1 IDELIRRALAEDLGYGDLttEALIPADARARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 91 RGPAHCLLLGERVALNTLARCSGIAsaaaaaveaargagwT-------------GHVAGTRKTTPGFRLVEKYGLLVGGA 157
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIA---------------TltrryvdavagtgARILDTRKTTPGLRALEKYAVRAGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 158 ASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLK 237
Cdd:COG0157 146 VNHRLGLSDAVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13477197 238 aqfPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:COG0157 226 ---GRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
9-285 |
6.53e-84 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 254.64 E-value: 6.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 9 LLPPVTLAALVDSWLREDCPG---LNYAALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLN--CQVSWFLPEGSKLVP 83
Cdd:PLN02716 13 SHPTYDIEAVIKLALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDpsLKVEWAAIDGDFVHK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 84 VARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGwtghVAGTRKTTPGFRLVEKYGLLVGGAASHRYD 163
Cdd:PLN02716 93 GLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 164 LGGLVMVKDNHVVAAGGVEKAVRAARQ---AADFALKVEVECSSLQEAVQAAE------AGADLVLLDNF--KPEELHPT 232
Cdd:PLN02716 169 LFDMVMIKDNHIAAAGGITNAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVD 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13477197 233 ATVLKAQFPSVA----VEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:PLN02716 249 VSMLKEAVELINgrfeTEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-284 |
9.76e-79 |
|
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: 236.44 E-value: 9.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 131 TGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQ 210
Cdd:pfam01729 16 KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFAVKIEVEVESLEEAEE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13477197 211 AAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:pfam01729 96 ALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
18-285 |
1.86e-124 |
|
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: 356.18 E-value: 1.86e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 18 LVDSWLREDCPGLNYA--ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAH 95
Cdd:TIGR00078 1 LLDRWLREDLGSGDITteALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 96 CLLLGERVALNTLARCSGIASAAAAAVEAARGAGwtGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHV 175
Cdd:TIGR00078 81 SLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 176 VAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDN 255
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDN 235
|
250 260 270
....*....|....*....|....*....|
gi 13477197 256 LPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:TIGR00078 236 LEEYAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
4.25e-116 |
|
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: 334.83 E-value: 4.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPGLNYA--ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQL--NCQVSWFLPEGSKLVPVARVAEVRG 92
Cdd:cd01572 2 AIVRLALAEDLGRGDITseAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 93 PAHCLLLGERVALNTLARCSGIASAAAAAVEAARgaGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKD 172
Cdd:cd01572 82 PARSLLTAERTALNFLQRLSGIATLTRRYVEALA--GTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 173 NHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGIT 252
Cdd:cd01572 160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 13477197 253 LDNLPQFCGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
4.64e-109 |
|
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: 317.11 E-value: 4.64e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPGLNYA--ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQL-NCQVSWFLPEGSKLVPVARVAEVRGP 93
Cdd:cd01568 2 ALLDRALAEDLGYGDLTteALIPGDAPATATLIAKEEGVLAGLEVAEEVFELLdGIEVEWLVKDGDRVEAGQVLLEVEGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 94 AHCLLLGERVALNTLARCSGIASAAAAAVEAARgaGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDN 173
Cdd:cd01568 82 ARSLLTAERVALNLLQRLSGIATATRRYVEAAR--GTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 174 HVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaQFPSVAVEASGGITL 253
Cdd:cd01568 160 HIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLK-GLPRVLLEASGGITL 238
|
250 260 270
....*....|....*....|....*....|.
gi 13477197 254 DNLPQFCGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:cd01568 239 ENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
15-285 |
6.06e-93 |
|
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: 276.13 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 15 LAALVDSWLREDCPGLNY--AALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQL--NCQVSWFLPEGSKLVPVARVAEV 90
Cdd:COG0157 1 IDELIRRALAEDLGYGDLttEALIPADARARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 91 RGPAHCLLLGERVALNTLARCSGIAsaaaaaveaargagwT-------------GHVAGTRKTTPGFRLVEKYGLLVGGA 157
Cdd:COG0157 81 EGPARALLTAERVALNLLQRLSGIA---------------TltrryvdavagtgARILDTRKTTPGLRALEKYAVRAGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 158 ASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLK 237
Cdd:COG0157 146 VNHRLGLSDAVLIKDNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 13477197 238 aqfPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:COG0157 226 ---GRALLEASGGITLENIRAYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
9-285 |
6.53e-84 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 254.64 E-value: 6.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 9 LLPPVTLAALVDSWLREDCPG---LNYAALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLN--CQVSWFLPEGSKLVP 83
Cdd:PLN02716 13 SHPTYDIEAVIKLALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDpsLKVEWAAIDGDFVHK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 84 VARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGwtghVAGTRKTTPGFRLVEKYGLLVGGAASHRYD 163
Cdd:PLN02716 93 GLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 164 LGGLVMVKDNHVVAAGGVEKAVRAARQ---AADFALKVEVECSSLQEAVQAAE------AGADLVLLDNF--KPEELHPT 232
Cdd:PLN02716 169 LFDMVMIKDNHIAAAGGITNAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVD 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13477197 233 ATVLKAQFPSVA----VEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 285
Cdd:PLN02716 249 VSMLKEAVELINgrfeTEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
131-284 |
9.76e-79 |
|
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: 236.44 E-value: 9.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 131 TGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEVECSSLQEAVQ 210
Cdd:pfam01729 16 KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFAVKIEVEVESLEEAEE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13477197 211 AAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:pfam01729 96 ALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVPPLDISLD 169
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
41-284 |
3.25e-67 |
|
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: 210.94 E-value: 3.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 41 PSQAALWAKSP--GILAGQPFFDAIFTQLN---CQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIA 115
Cdd:cd00516 17 RATAEFTAREDpyGVLAGLEEALELLELLRfpgPLVILAVPEGTVVEPGEPLLTIEGPARELLLLERVLLNLLQRLSGIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 116 SAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGV------EKAVRAAR 189
Cdd:cd00516 97 TATARYVEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSIiqafgeLAAVKALR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 190 QAA--DFALKVEVECSSLQEAVQAAEAG-ADLVLLDNFKPEELHPTATVLKAQ-------FPSVAVEASGGITLDNLPQF 259
Cdd:cd00516 177 RWLpeLFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARahldgkgLPRVKIEASGGLDEENIRAY 256
|
250 260
....*....|....*....|....*
gi 13477197 260 CGPHIDVISMGMLTQAAPALDFSLK 284
Cdd:cd00516 257 AETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
17-285 |
1.16e-38 |
|
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: 137.05 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPG--LNYAALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPA 94
Cdd:cd01573 2 AELERLLLEDAPYgdLTTEALGIGEQPGKITFRARDPGVLCGTEEAARILELLGLEVDLAAASGSRVAAGAVLLEAEGPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 95 HCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNH 174
Cdd:cd01573 82 AALHLGWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 175 VVAAGG--VEKAVRAARQAADfALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGIT 252
Cdd:cd01573 162 RAFLGGpePLKALARLRATAP-EKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPVLLAAAGGIN 240
|
250 260 270
....*....|....*....|....*....|...
gi 13477197 253 LDNLPQFCGPHIDVISMGMLTQAAPAlDFSLKL 285
Cdd:cd01573 241 IENAAAYAAAGADILVTSAPYYAKPA-DIKVKI 272
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
17-285 |
2.33e-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: 93.81 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPG--LNYAALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPA 94
Cdd:TIGR01334 6 GLIDNLLLEDIGYgdLTTRALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYAVPSGSRALAGTLLLEAKGSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 95 HCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNH 174
Cdd:TIGR01334 86 GQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 175 VVAAGGVE---KAVRAARQAADfALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGI 251
Cdd:TIGR01334 166 RTFLNDNFdwgGAIGRLKQTAP-ERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGGI 244
|
250 260 270
....*....|....*....|....*....|....
gi 13477197 252 TLDNLPQFCGPHIDVISMGMLTQAAPAlDFSLKL 285
Cdd:TIGR01334 245 NPENIADYIEAGIDLFITSAPYYAAPC-DIKVKL 277
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
34-112 |
3.87e-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: 87.93 E-value: 3.87e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13477197 34 ALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCS 112
Cdd:pfam02749 10 ALIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVKDGDRVEAGDVILEIEGPARALLTAERVALNLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
17-268 |
8.68e-19 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 84.01 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 17 ALVDSWLREDCPG--LNYAALVSGAGPSQAALWAKSPGILAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPA 94
Cdd:PRK06096 7 AQLDALLLEDIQGgdLTTRALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDDAVSDGSQANAGQRLISAQGNA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 95 HCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNH 174
Cdd:PRK06096 87 AALHQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 175 ---VVAAGGVEKAVRAARQAADfALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGI 251
Cdd:PRK06096 167 rhfLHDPQDWSGAINQLRRHAP-EKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSLAPHCTLSLAGGI 245
|
250
....*....|....*....
gi 13477197 252 TLDNLPQF--CGPHIDVIS 268
Cdd:PRK06096 246 NLNTLKNYadCGIRLFITS 264
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
145-279 |
1.97e-12 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 64.46 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 145 RLVEKYGLLVGGAAS--HRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALkveVECSSLQEAVQAAEAGADLVLLD 222
Cdd:cd00452 48 ALRKEFPEALIGAGTvlTPEQADAAIAAGAQFIVSPGLDPEVVKAANRAGIPLL---PGVATPTEIMQALELGADIVKLF 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 13477197 223 NFKPEeLHPTATVLKAQFPSVAVEASGGITLDNLPQFCGphIDVISMGMLTQAAPAL 279
Cdd:cd00452 125 PAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEWLA--AGVVAVGGGSLLPKDA 178
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
202-283 |
7.08e-04 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 39.98 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 202 CSSLQEAVQAAEAGADLVlldnfkpeELHPTATV-------LKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMG-MLT 273
Cdd:PRK06552 116 CMTVTEIVTALEAGSEIV--------KLFPGSTLgpsfikaIKGPLPQVNVMVTGGVNLDNVKDWFAAGADAVGIGgELN 187
|
90
....*....|
gi 13477197 274 QAAPALDFSL 283
Cdd:PRK06552 188 KLASQGDFDL 197
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
185-258 |
6.27e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 37.11 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13477197 185 VRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNF-----KPEELHP------TATVLKAQFPSVAVeasGGITL 253
Cdd:cd00564 85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVfptptKPGAGPPlglellREIAELVEIPVVAI---GGITP 161
|
....*
gi 13477197 254 DNLPQ 258
Cdd:cd00564 162 ENAAE 166
|
|
| |
