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Conserved domains on  [gi|646375756|ref|WP_025515690|]
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carboxylating nicotinate-nucleotide diphosphorylase [Bordetella trematum]

Protein Classification

nicotinate-nucleotide diphosphorylase( domain architecture ID 11415005)

nicotinate-nucleotide diphosphorylase catalyzes the reaction of quinolinic acid (QA) and 5-phosphoribosyl-1-pyrophosphate (PRPP) to nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide as part of the de novo synthesis of NAD

CATH:  3.90.1170.20
EC:  2.4.2.19
Gene Ontology:  GO:0004514|GO:0009435
PubMed:  11876660|9016724|11876660

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 26-295 1.39e-146

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: 412.10  E-value: 1.39e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  26 LEPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLEPGAEIAR 105
Cdd:COG0157    1 IDELIRRALAEDLGY-GDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 106 IDGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIK 185
Cdd:COG0157   80 VEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 186 DNHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPE 265
Cdd:COG0157  160 DNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 646375756 266 TAPAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:COG0157  240 NIRAYAETGVDYISVGALTHSAPALDLSLR 269
 
Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 26-295 1.39e-146

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: 412.10  E-value: 1.39e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  26 LEPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLEPGAEIAR 105
Cdd:COG0157    1 IDELIRRALAEDLGY-GDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 106 IDGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIK 185
Cdd:COG0157   80 VEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 186 DNHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPE 265
Cdd:COG0157  160 DNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 646375756 266 TAPAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:COG0157  240 NIRAYAETGVDYISVGALTHSAPALDLSLR 269
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 27-295 3.55e-146

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: 411.10  E-value: 3.55e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  27 EPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLEPGAEIARI 106
Cdd:cd01572    1 DAIVRLALAEDLGR-GDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 107 DGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKD 186
Cdd:cd01572   80 EGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 187 NHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPET 266
Cdd:cd01572  160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLEN 239

                        250       260
                 ....*....|....*....|....*....
gi 646375756 267 APAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:cd01572  240 IRAYAETGVDYISVGALTHSAPALDISLD 268
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 29-295 5.38e-116

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: 334.61  E-value: 5.38e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756   29 LVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDpeIRFHALLADGARLEPGAEIARIDG 108
Cdd:TIGR00078   1 LLDRWLREDLGS-GDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  109 PARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNH 188
Cdd:TIGR00078  78 PARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  189 VALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPETAP 268
Cdd:TIGR00078 158 IAAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLE 237

                         250       260
                  ....*....|....*....|....*..
gi 646375756  269 AIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLK 264
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 19-294 1.12e-79

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 243.86  E-value: 1.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  19 PALPQVMLEPLVRATLLEDLGRAGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLE 98
Cdd:PLN02716  12 PSHPTYDIEAVIKLALAEDAGDRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  99 PGAEIARIDGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRckVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGL 178
Cdd:PLN02716  92 KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 179 DDAVLIKDNHVALAGGVAQALTLARAHI---GHMVKIELEVDTLAQLDEALQ------AGVDVLLLDNM---------DN 240
Cdd:PLN02716 170 FDMVMIKDNHIAAAGGITNAVQSADKYLeekGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDV 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 646375756 241 DTLREAVRRVAGRAITEASGRITPETAPAIAETGVDLMAIGWLTHSARVLDIGL 294
Cdd:PLN02716 250 SMLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISL 303
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 130-295 3.50e-70

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: 214.48  E-value: 3.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  130 VATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNHVALAGGVAQALTLARAHIGHM 209
Cdd:pfam01729   1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  210 VKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAV---RRVAGRAITEASGRITPETAPAIAETGVDLMAIGWLTHS 286
Cdd:pfam01729  81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVeelDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160


                  ....*....
gi 646375756  287 ARVLDIGLD 295
Cdd:pfam01729 161 VPPLDISLD 169
 
Name Accession Description Interval E-value
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 26-295 1.39e-146

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: 412.10  E-value: 1.39e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  26 LEPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLEPGAEIAR 105
Cdd:COG0157    1 IDELIRRALAEDLGY-GDLTTEALIPADARARARLIAREDGVLAGLEVAERVFRLLDPGLEVEWLVADGDRVEAGDVLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 106 IDGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIK 185
Cdd:COG0157   80 VEGPARALLTAERVALNLLQRLSGIATLTRRYVDAVAGTGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 186 DNHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPE 265
Cdd:COG0157  160 DNHIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 646375756 266 TAPAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:COG0157  240 NIRAYAETGVDYISVGALTHSAPALDLSLR 269
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 27-295 3.55e-146

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: 411.10  E-value: 3.55e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  27 EPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLEPGAEIARI 106
Cdd:cd01572    1 DAIVRLALAEDLGR-GDITSEAIIPPDARAEARLIAKEEGVLAGLPVAEEVFELLDPGIEVEWLVKDGDRVEPGQVLATV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 107 DGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKD 186
Cdd:cd01572   80 EGPARSLLTAERTALNFLQRLSGIATLTRRYVEALAGTKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 187 NHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPET 266
Cdd:cd01572  160 NHIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLEN 239

                        250       260
                 ....*....|....*....|....*....
gi 646375756 267 APAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:cd01572  240 IRAYAETGVDYISVGALTHSAPALDISLD 268
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 27-295 1.07e-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: 369.50  E-value: 1.07e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  27 EPLVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDpEIRFHALLADGARLEPGAEIARI 106
Cdd:cd01568    1 DALLDRALAEDLGY-GDLTTEALIPGDAPATATLIAKEEGVLAGLEVAEEVFELLD-GIEVEWLVKDGDRVEAGQVLLEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 107 DGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKD 186
Cdd:cd01568   79 EGPARSLLTAERVALNLLQRLSGIATATRRYVEAARGTKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 187 NHVALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAG--RAITEASGRITP 264
Cdd:cd01568  159 NHIAAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITL 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 646375756 265 ETAPAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:cd01568  239 ENIRAYAETGVDVISTGALTHSAPALDISLK 269
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 29-295 5.38e-116

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: 334.61  E-value: 5.38e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756   29 LVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDpeIRFHALLADGARLEPGAEIARIDG 108
Cdd:TIGR00078   1 LLDRWLREDLGS-GDITTEALVPGSTRATASLVAKEDGVLAGLPVARRVFEQLG--VQVEWLVKDGDRVEPGEVVAEVEG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  109 PARGMLTAERTALNFLGHLSGVATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNH 188
Cdd:TIGR00078  78 PARSLLTAERTALNFLGRLSGIATATRKYVEAARGTNVRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  189 VALAGGVAQALTLARAHIGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRAITEASGRITPETAP 268
Cdd:TIGR00078 158 IAAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLE 237

                         250       260
                  ....*....|....*....|....*..
gi 646375756  269 AIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:TIGR00078 238 EYAETGVDVISSGALTHSVPALDFSLK 264
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 19-294 1.12e-79

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 243.86  E-value: 1.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  19 PALPQVMLEPLVRATLLEDLGRAGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHALLADGARLE 98
Cdd:PLN02716  12 PSHPTYDIEAVIKLALAEDAGDRGDVTCLATIPGDMEAEATFLAKADGVLAGIALADMVFEEVDPSLKVEWAAIDGDFVH 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  99 PGAEIARIDGPARGMLTAERTALNFLGHLSGVATATASIADAIAHTRckVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGL 178
Cdd:PLN02716  92 KGLKFGKVTGPAHSILVAERVVLNFMQRMSGIATLTKAMADAAKPAC--ILETRKTAPGLRLVDKWAVLIGGGKNHRMGL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 179 DDAVLIKDNHVALAGGVAQALTLARAHI---GHMVKIELEVDTLAQLDEALQ------AGVDVLLLDNM---------DN 240
Cdd:PLN02716 170 FDMVMIKDNHIAAAGGITNAVQSADKYLeekGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvplengdvDV 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 646375756 241 DTLREAVRRVAGRAITEASGRITPETAPAIAETGVDLMAIGWLTHSARVLDIGL 294
Cdd:PLN02716 250 SMLKEAVELINGRFETEASGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISL 303
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 43-295 1.97e-71

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: 221.73  E-value: 1.97e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  43 DLTTDAIVPAEARGQTRLVAR------QAGVLAGLDLARLAFRLID-PEIRFHALLADGARLEPGAEIARIDGPARGMLT 115
Cdd:cd00516    1 DLYKLTMIQAYPPPDTRATAEftaredPYGVLAGLEEALELLELLRfPGPLVILAVPEGTVVEPGEPLLTIEGPARELLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 116 AERTALNFLGHLSGVATATASIADAIAH--TRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNHVALAG 193
Cdd:cd00516   81 LERVLLNLLQRLSGIATATARYVEAAKGanTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 194 GVAQALTL------ARAHIG--HMVKIELEVDTLAQLDEALQAG-VDVLLLDNMDNDTLREAVRRVAGRA---------- 254
Cdd:cd00516  161 SIIQAFGElaavkaLRRWLPelFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARAhldgkglprv 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 646375756 255 ITEASGRITPETAPAIAETGVDLMAIGWLTHSARVLDIGLD 295
Cdd:cd00516  241 KIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 130-295 3.50e-70

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: 214.48  E-value: 3.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  130 VATATASIADAIAHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNHVALAGGVAQALTLARAHIGHM 209
Cdd:pfam01729   1 IATATRRMVEAARSVKVRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAPFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  210 VKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAV---RRVAGRAITEASGRITPETAPAIAETGVDLMAIGWLTHS 286
Cdd:pfam01729  81 VKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVeelDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHS 160


                  ....*....
gi 646375756  287 ARVLDIGLD 295
Cdd:pfam01729 161 VPPLDISLD 169
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 34-277 3.21e-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: 153.99  E-value: 3.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  34 LLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIrfHALLADGARLEPGAEIARIDGPARGM 113
Cdd:cd01573    8 LLEDAPY-GDLTTEALGIGEQPGKITFRARDPGVLCGTEEAARILELLGLEV--DLAAASGSRVAAGAVLLEAEGPAAAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 114 LTAERTALNFLGHLSGVATATASIADAIAHTRCK--VTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNHVAL 191
Cdd:cd01573   85 HLGWKVAQTLLEWASGIATATAEMVAAARAVNPDivVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHRAF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 192 AGGVAQALTLA--RAHIGHMvKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRA--ITE-ASGRITPET 266
Cdd:cd01573  165 LGGPEPLKALArlRATAPEK-KIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAppVLLaAAGGINIEN 243

                        250
                 ....*....|.
gi 646375756 267 APAIAETGVDL 277
Cdd:cd01573  244 AAAYAAAGADI 254
QRPTase_N pfam02749
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ...
 39-128 1.16e-26

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: 99.87  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756   39 GRAGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDpeIRFHALLADGARLEPGAEIARIDGPARGMLTAER 118
Cdd:pfam02749   1 IGRGDLTTEALIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLG--LEVEWLVKDGDRVEAGDVILEIEGPARALLTAER 78

                          90
                  ....*....|
gi 646375756  119 TALNFLGHLS 128
Cdd:pfam02749  79 VALNLLQRLS 88
PRK06096 PRK06096
molybdenum transport protein ModD; Provisional
 32-278 4.97e-25

molybdenum transport protein ModD; Provisional


Pssm-ID: 180397 [Multi-domain]  Cd Length: 284  Bit Score: 101.34  E-value: 4.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  32 ATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIrfHALLADGARLEPGAEIARIDGPAR 111
Cdd:PRK06096  11 ALLLEDIQG-GDLTTRALGIGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTI--DDAVSDGSQANAGQRLISAQGNAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 112 GMLTAERTALNFLGHLSGVATATASIAdAIAHTR---CKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIKDNH 188
Cdd:PRK06096  88 ALHQGWKAVQNVLEWSCGVSDYLAQML-ALLRERypdGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAETILLFANH 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 189 VAL-------AGGVAQaltLARAhiGHMVKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVR---RVAGRAITEA 258
Cdd:PRK06096 167 RHFlhdpqdwSGAINQ---LRRH--APEKKIVVEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQiapSLAPHCTLSL 241

                        250       260
                 ....*....|....*....|
gi 646375756 259 SGRITPETAPAIAETGVDLM 278
Cdd:PRK06096 242 AGGINLNTLKNYADCGIRLF 261
modD TIGR01334
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ...
 29-277 5.83e-22

putative molybdenum utilization protein ModD; The gene modD for a member of this family is found with molybdenum transport genes modABC in Rhodobacter capsulatus. However, disruption of modD causes only a 4-fold (rather than 500-fold for modA, modB, modC) change in the external molybdenum concentration required to suppress an alternative nitrogenase. ModD proteins are highly similar to nicotinate-nucleotide pyrophosphorylase (also called quinolinate phosphoribosyltransferase). The function unknown. [Unknown function, General]


Pssm-ID: 130401 [Multi-domain]  Cd Length: 277  Bit Score: 92.66  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756   29 LVRATLLEDLGRaGDLTTDAIVPAEARGQTRLVARQAGVLAGLDLARLAFRLIDPEIRFHalLADGARLEPGAEIARIDG 108
Cdd:TIGR01334   7 LIDNLLLEDIGY-GDLTTRALGIQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYA--VPSGSRALAGTLLLEAKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  109 PARGMLTAERTALNFLGHLSGVATATA---SIADAIaHTRCKVTCTRKTMPGLRAVQKYAVRVGGGSNHRFGLDDAVLIK 185
Cdd:TIGR01334  84 SAGQLHQGWKSAQSVLEWSCGVATYTHkmvTLAKKI-SPMAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756  186 DNHVALAGG---VAQALTLARAHIGHMvKIELEVDTLAQLDEALQAGVDVLLLDNMDNDTLREAVRRVAGRA---ITEAS 259
Cdd:TIGR01334 163 ANHRTFLNDnfdWGGAIGRLKQTAPER-KITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDhipTLAAA 241

                         250
                  ....*....|....*...
gi 646375756  260 GRITPETAPAIAETGVDL 277
Cdd:TIGR01334 242 GGINPENIADYIEAGIDL 259
thiE PRK00043
thiamine phosphate synthase;
198-280 4.33e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 37.47  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646375756 198 ALTLARAHIGHMVKIELEVDTLAQLDEALQAGVD------------------VLLLdnmdnDTLREAVRRVAGRAITeAS 259
Cdd:PRK00043  93 PVADARALLGPDAIIGLSTHTLEEAAAALAAGADyvgvgpifptptkkdakaPQGL-----EGLREIRAAVGDIPIV-AI 166

                         90       100
                 ....*....|....*....|.
gi 646375756 260 GRITPETAPAIAETGVDLMAI 280
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAV 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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