|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
21-285 |
2.75e-125 |
|
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: 358.11 E-value: 2.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 21 SWLQEDCPGLNFAS--LVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPAHHLL 98
Cdd:TIGR00078 4 RWLREDLGSGDITTeaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPARSLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 99 LGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVAA 178
Cdd:TIGR00078 84 TAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 179 GSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARfpsVSVEASGGVTLDNLTQ 258
Cdd:TIGR00078 162 GSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEE 238
|
250 260
....*....|....*....|....*..
gi 19526852 259 FCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:TIGR00078 239 YAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
2.99e-121 |
|
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: 347.93 E-value: 2.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 17 ALANSWLQEDCPGLNFASLVT--GSAPSQAVLWAKSPGVLAGRPFFDAIFTQL--NCQVSWFLPEGSKLVPVVKVAEVKG 92
Cdd:cd01572 2 AIVRLALAEDLGRGDITSEAIipPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 93 PAHHLLLGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKD 172
Cdd:cd01572 82 PARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTK--ARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 173 NHVVAAGSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPsvsVEASGGVT 252
Cdd:cd01572 160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVL---LEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 19526852 253 LDNLTQFCGTHIDVISLGMLTQAAPALDFSLK 284
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
22-285 |
1.74e-101 |
|
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: 298.09 E-value: 1.74e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 22 WLQEDCPG--LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQL--NCQVSWFLPEGSKLVPVVKVAEVKGPAHHL 97
Cdd:COG0157 8 ALAEDLGYgdLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEVEGPARAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 98 LLGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVA 177
Cdd:COG0157 88 LTAERVALNLLQRLSGIATLTRRYVDAVAGTG--ARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDNHIAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 178 AGSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARfpsVSVEASGGVTLDNLT 257
Cdd:COG0157 166 AGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGR---ALLEASGGITLENIR 242
|
250 260
....*....|....*....|....*...
gi 19526852 258 QFCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:COG0157 243 AYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-285 |
1.42e-89 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 269.28 E-value: 1.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 22 WLQEDCPG---LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLN--CQVSWFLPEGSKLVPVVKVAEVKGPAHH 96
Cdd:PLN02716 26 ALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDpsLKVEWAAIDGDFVHKGLKFGKVTGPAHS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 97 LLLGERVALNTLARCSGIASAAATAVEVARSTGwtghVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVV 176
Cdd:PLN02716 106 ILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 177 AAGSMERAVLKARQ---AAGFSLKVEVECSSLEEAFRAAE------AGADLVMLDNF--KPEELHPTAATLKARFP---- 241
Cdd:PLN02716 182 AAGGITNAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVDVSMLKEAVEling 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19526852 242 SVSVEASGGVTLDNLTQFCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:PLN02716 262 RFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
114-284 |
6.40e-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: 236.82 E-value: 6.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 114 IASAAATAVEVARSTgwTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVAAGSMERAVLKARQAAG 193
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 194 FSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPSVSVEASGGVTLDNLTQFCGTHIDVISLGMLT 273
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
|
170
....*....|.
gi 19526852 274 QAAPALDFSLK 284
Cdd:pfam01729 159 HSVPPLDISLD 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nadC |
TIGR00078 |
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ... |
21-285 |
2.75e-125 |
|
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: 358.11 E-value: 2.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 21 SWLQEDCPGLNFAS--LVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPAHHLL 98
Cdd:TIGR00078 4 RWLREDLGSGDITTeaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPARSLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 99 LGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVAA 178
Cdd:TIGR00078 84 TAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHIAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 179 GSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARfpsVSVEASGGVTLDNLTQ 258
Cdd:TIGR00078 162 GSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEE 238
|
250 260
....*....|....*....|....*..
gi 19526852 259 FCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:TIGR00078 239 YAETGVDVISSGALTHSVPALDFSLKI 265
|
|
| QPRTase |
cd01572 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
2.99e-121 |
|
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: 347.93 E-value: 2.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 17 ALANSWLQEDCPGLNFASLVT--GSAPSQAVLWAKSPGVLAGRPFFDAIFTQL--NCQVSWFLPEGSKLVPVVKVAEVKG 92
Cdd:cd01572 2 AIVRLALAEDLGRGDITSEAIipPDARAEARLIAKEEGVLAGLPVAEEVFELLdpGIEVEWLVKDGDRVEPGQVLATVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 93 PAHHLLLGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKD 172
Cdd:cd01572 82 PARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTK--ARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 173 NHVVAAGSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPsvsVEASGGVT 252
Cdd:cd01572 160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVL---LEASGGIT 236
|
250 260 270
....*....|....*....|....*....|..
gi 19526852 253 LDNLTQFCGTHIDVISLGMLTQAAPALDFSLK 284
Cdd:cd01572 237 LENIRAYAETGVDYISVGALTHSAPALDISLD 268
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
17-284 |
3.78e-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: 332.52 E-value: 3.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 17 ALANSWLQEDCPGLNFASLVT--GSAPSQAVLWAKSPGVLAGRPFFDAIFTQL-NCQVSWFLPEGSKLVPVVKVAEVKGP 93
Cdd:cd01568 2 ALLDRALAEDLGYGDLTTEALipGDAPATATLIAKEEGVLAGLEVAEEVFELLdGIEVEWLVKDGDRVEAGQVLLEVEGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 94 AHHLLLGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDN 173
Cdd:cd01568 82 ARSLLTAERVALNLLQRLSGIATATRRYVEAARGTK--ARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 174 HVVAAGSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHpTAATLKARFPSVSVEASGGVTL 253
Cdd:cd01568 160 HIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELK-EAVKLLKGLPRVLLEASGGITL 238
|
250 260 270
....*....|....*....|....*....|.
gi 19526852 254 DNLTQFCGTHIDVISLGMLTQAAPALDFSLK 284
Cdd:cd01568 239 ENIRAYAETGVDVISTGALTHSAPALDISLK 269
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
22-285 |
1.74e-101 |
|
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: 298.09 E-value: 1.74e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 22 WLQEDCPG--LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQL--NCQVSWFLPEGSKLVPVVKVAEVKGPAHHL 97
Cdd:COG0157 8 ALAEDLGYgdLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLdpGLEVEWLVADGDRVEAGDVLLEVEGPARAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 98 LLGERVALNTLARCSGIASAAATAVEVARSTGwtGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVA 177
Cdd:COG0157 88 LTAERVALNLLQRLSGIATLTRRYVDAVAGTG--ARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDNHIAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 178 AGSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARfpsVSVEASGGVTLDNLT 257
Cdd:COG0157 166 AGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGR---ALLEASGGITLENIR 242
|
250 260
....*....|....*....|....*...
gi 19526852 258 QFCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:COG0157 243 AYAETGVDYISVGALTHSAPALDLSLRI 270
|
|
| PLN02716 |
PLN02716 |
nicotinate-nucleotide diphosphorylase (carboxylating) |
22-285 |
1.42e-89 |
|
nicotinate-nucleotide diphosphorylase (carboxylating)
Pssm-ID: 178318 [Multi-domain] Cd Length: 308 Bit Score: 269.28 E-value: 1.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 22 WLQEDCPG---LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLN--CQVSWFLPEGSKLVPVVKVAEVKGPAHH 96
Cdd:PLN02716 26 ALAEDAGDrgdVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDpsLKVEWAAIDGDFVHKGLKFGKVTGPAHS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 97 LLLGERVALNTLARCSGIASAAATAVEVARSTGwtghVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVV 176
Cdd:PLN02716 106 ILVAERVVLNFMQRMSGIATLTKAMADAAKPAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 177 AAGSMERAVLKARQ---AAGFSLKVEVECSSLEEAFRAAE------AGADLVMLDNF--KPEELHPTAATLKARFP---- 241
Cdd:PLN02716 182 AAGGITNAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVDVSMLKEAVEling 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19526852 242 SVSVEASGGVTLDNLTQFCGTHIDVISLGMLTQAAPALDFSLKL 285
Cdd:PLN02716 262 RFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
114-284 |
6.40e-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: 236.82 E-value: 6.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 114 IASAAATAVEVARSTgwTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVAAGSMERAVLKARQAAG 193
Cdd:pfam01729 1 IATATRRMVEAARSV--KVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 194 FSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPSVSVEASGGVTLDNLTQFCGTHIDVISLGMLT 273
Cdd:pfam01729 79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
|
170
....*....|.
gi 19526852 274 QAAPALDFSLK 284
Cdd:pfam01729 159 HSVPPLDISLD 169
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
38-284 |
4.43e-76 |
|
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: 233.67 E-value: 4.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 38 GSAPSQAVLWAKSP--GVLAGRPFFDAIFTQLN---CQVSWFLPEGSKLVPVVKVAEVKGPAHHLLLGERVALNTLARCS 112
Cdd:cd00516 14 PDTRATAEFTAREDpyGVLAGLEEALELLELLRfpgPLVILAVPEGTVVEPGEPLLTIEGPARELLLLERVLLNLLQRLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 113 GIASAAATAVEVARSTGWTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNHVVAAGS------MERAVL 186
Cdd:cd00516 94 GIATATARYVEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSiiqafgELAAVK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 187 KARQAAG--FSLKVEVECSSLEEAFRAAEAG-ADLVMLDNFKPEELHPTAATLKAR-------FPSVSVEASGGVTLDNL 256
Cdd:cd00516 174 ALRRWLPelFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARahldgkgLPRVKIEASGGLDEENI 253
|
250 260
....*....|....*....|....*...
gi 19526852 257 TQFCGTHIDVISLGMLTQAAPALDFSLK 284
Cdd:cd00516 254 RAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
22-285 |
1.97e-46 |
|
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: 157.46 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 22 WLQEDCPGLNFASLVTG--SAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPAHHLLL 99
Cdd:cd01573 7 LLLEDAPYGDLTTEALGigEQPGKITFRARDPGVLCGTEEAARILELLGLEVDLAAASGSRVAAGAVLLEAEGPAAALHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 100 GERVALNTLARCSGIASAAATAVEVARSTGWTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNH-VVAA 178
Cdd:cd01573 87 GWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHrAFLG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 179 GSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPSVSVEASGGVTLDNLTQ 258
Cdd:cd01573 167 GPEPLKALARLRATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPVLLAAAGGINIENAAA 246
|
250 260
....*....|....*....|....*..
gi 19526852 259 FCGTHIDVISLGMLTQAAPAlDFSLKL 285
Cdd:cd01573 247 YAAAGADILVTSAPYYAKPA-DIKVKI 272
|
|
| modD |
TIGR01334 |
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ... |
16-285 |
7.79e-24 |
|
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: 98.05 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 16 AALANSWLQEDCPG-LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPA 94
Cdd:TIGR01334 6 GLIDNLLLEDIGYGdLTTRALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYAVPSGSRALAGTLLLEAKGSA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 95 HHLLLGERVALNTLARCSGIASAAATAVEVARSTGWTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNH 174
Cdd:TIGR01334 86 GQLHQGWKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 175 VVAAGSME---RAVLKARQAAGfSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPSVSVEASGGV 251
Cdd:TIGR01334 166 RTFLNDNFdwgGAIGRLKQTAP-ERKITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGGI 244
|
250 260 270
....*....|....*....|....*....|....
gi 19526852 252 TLDNLTQFCGTHIDVISLGMLTQAAPAlDFSLKL 285
Cdd:TIGR01334 245 NPENIADYIEAGIDLFITSAPYYAAPC-DIKVKL 277
|
|
| QRPTase_N |
pfam02749 |
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ... |
34-112 |
2.37e-23 |
|
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: 91.40 E-value: 2.37e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19526852 34 SLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPAHHLLLGERVALNTLARCS 112
Cdd:pfam02749 10 ALIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVKDGDRVEAGDVILEIEGPARALLTAERVALNLLQRLS 88
|
|
| PRK06096 |
PRK06096 |
molybdenum transport protein ModD; Provisional |
20-268 |
5.45e-20 |
|
molybdenum transport protein ModD; Provisional
Pssm-ID: 180397 [Multi-domain] Cd Length: 284 Bit Score: 87.47 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 20 NSWLQEDCPG--LNFASLVTGSAPSQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWFLPEGSKLVPVVKVAEVKGPAHHL 97
Cdd:PRK06096 10 DALLLEDIQGgdLTTRALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDDAVSDGSQANAGQRLISAQGNAAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 98 LLGERVALNTLARCSGIASAAATAVEVARSTGWTGHVAGTRKTTPGFRLVEKYGLQVGGAACHRYDLGGMVMVKDNH--- 174
Cdd:PRK06096 90 HQGWKAVQNVLEWSCGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANHrhf 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 175 VVAAGSMERAVLKARQAAGfSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAATLKARFPSVSVEASGGVTLD 254
Cdd:PRK06096 170 LHDPQDWSGAINQLRRHAP-EKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSLAPHCTLSLAGGINLN 248
|
250
....*....|....*.
gi 19526852 255 NLTQF--CGTHIDVIS 268
Cdd:PRK06096 249 TLKNYadCGIRLFITS 264
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
104-279 |
8.01e-16 |
|
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: 74.09 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 104 ALNTLARCSGIASAAATAVEVArstgWTGHVAGtrkttPGFRLVEKY--GLQVGGAACH-RYDLGGMVMVKDNHVVAAGS 180
Cdd:cd00452 15 AEDALALAEALIEGGIRAIEIT----LRTPGAL-----EAIRALRKEfpEALIGAGTVLtPEQADAAIAAGAQFIVSPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 181 MeRAVLKARQAAGFSLKVEveCSSLEEAFRAAEAGADLVMLDNFKPEeLHPTAATLKARFPSVSVEASGGVTLDNLTQFC 260
Cdd:cd00452 86 D-PEVVKAANRAGIPLLPG--VATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEWL 161
|
170
....*....|....*....
gi 19526852 261 GthIDVISLGMLTQAAPAL 279
Cdd:cd00452 162 A--AGVVAVGGGSLLPKDA 178
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
202-283 |
6.53e-04 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 39.98 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 202 CSSLEEAFRAAEAGADLVML---DNFKPEelhpTAATLKARFPSVSVEASGGVTLDNLTQFCGTHIDVISLG-MLTQAAP 277
Cdd:PRK06552 116 CMTVTEIVTALEAGSEIVKLfpgSTLGPS----FIKAIKGPLPQVNVMVTGGVNLDNVKDWFAAGADAVGIGgELNKLAS 191
|
....*.
gi 19526852 278 ALDFSL 283
Cdd:PRK06552 192 QGDFDL 197
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
188-276 |
1.34e-03 |
|
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: 39.15 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 188 ARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPEELHPTAA---------TLKARFPSVSVEASGGVTLDNLTQ 258
Cdd:TIGR00693 89 ARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAppagvellrEIAATLIDIPIVAIGGITLENAAE 168
|
90 100
....*....|....*....|.
gi 19526852 259 FCGTHID---VISLgmLTQAA 276
Cdd:TIGR00693 169 VLAAGADgvaVVSA--IMQAA 187
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
159-258 |
1.78e-03 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 39.47 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 159 CHRYdlGGMVMVKDNHVVAA---------GSMERAVLKARQAAGFSLkVEVECSSLEEAFRAAEAGADLVMLDNFKPEEL 229
Cdd:PRK08999 184 CRRA--GAQLLLNGDPELAEdlgadgvhlTSAQLAALAARPLPAGRW-VAASCHDAEELARAQRLGVDFAVLSPVQPTAS 260
|
90 100 110
....*....|....*....|....*....|....*..
gi 19526852 230 HP--------TAATLKARFPsVSVEASGGVTLDNLTQ 258
Cdd:PRK08999 261 HPgaaplgweGFAALIAGVP-LPVYALGGLGPGDLEE 296
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
157-268 |
4.15e-03 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 37.86 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526852 157 AACHRYdlGGMVMVKDNHVVAA---------GSMERAVLKARQAAGFSLKVEVECSSLEEAFRAAEAGADLVMLDNFKPE 227
Cdd:COG0352 55 ALCRAY--GVPLIINDRVDLALalgadgvhlGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPT 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19526852 228 ELHPTA---------ATLKARF--PSVsveASGGVTLDNLTQFCGTHID---VIS 268
Cdd:COG0352 133 PTKPGAppplgleglAWWAELVeiPVV---AIGGITPENAAEVLAAGADgvaVIS 184
|
|
| |
