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Conserved domains on  [gi|800907428|gb|AKA79609|]
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carboxylating nicotinate-nucleotide diphosphorylase [Saccharolobus solfataricus]

Protein Classification

nicotinate-nucleotide diphosphorylase( domain architecture ID 11488600)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 9-272 7.77e-139

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: 391.62  E-value: 7.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428    9 RLLDYLEEDVMPEDITT--KFLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDA- 85
Cdd:TIGR00078   1 LLDRWLREDLGSGDITTeaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPAr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   86 DILTVERLILNFLGKLSGIATITNLMVKKAKEVNpyVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHI 165
Cdd:TIGR00078  81 SLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  166 TLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNVID 245
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEE 238

                         250       260
                  ....*....|....*....|....*..
gi 800907428  246 YAKTGVDVISSGYITHSYRSLDFSLDV 272
Cdd:TIGR00078 239 YAETGVDVISSGALTHSVPALDFSLKI 265
 
Name Accession Description Interval E-value
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 9-272 7.77e-139

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: 391.62  E-value: 7.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428    9 RLLDYLEEDVMPEDITT--KFLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDA- 85
Cdd:TIGR00078   1 LLDRWLREDLGSGDITTeaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPAr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   86 DILTVERLILNFLGKLSGIATITNLMVKKAKEVNpyVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHI 165
Cdd:TIGR00078  81 SLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  166 TLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNVID 245
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEE 238

                         250       260
                  ....*....|....*....|....*..
gi 800907428  246 YAKTGVDVISSGYITHSYRSLDFSLDV 272
Cdd:TIGR00078 239 YAETGVDVISSGALTHSVPALDFSLKI 265
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 10-271 4.52e-123

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: 351.78  E-value: 4.52e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTK--FLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGfSNINGE---KDGREVKKGDIVLNFEGD 84
Cdd:cd01572    4 VRLALAEDLGRGDITSEaiIPPDARAEARLIAKEEGVLAGLPVAEEVFELLD-PGIEVEwlvKDGDRVEPGQVLATVEGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  85 A-DILTVERLILNFLGKLSGIATITNLMVKKAKEvnPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDN 163
Cdd:cd01572   83 ArSLLTAERTALNFLQRLSGIATLTRRYVEALAG--TKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 164 HITLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNV 243
Cdd:cd01572  161 HIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENI 240

                        250       260
                 ....*....|....*....|....*...
gi 800907428 244 IDYAKTGVDVISSGYITHSYRSLDFSLD 271
Cdd:cd01572  241 RAYAETGVDYISVGALTHSAPALDISLD 268
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 10-274 1.17e-116

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: 335.45  E-value: 1.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTKFL--EGIRARGIVRCKDSGILAGNRFIVPFLKYLGfSNINGE---KDGREVKKGDIVLNFEGD 84
Cdd:COG0157    5 IRRALAEDLGYGDLTTEALipADARARARLIAREDGVLAGLEVAERVFRLLD-PGLEVEwlvADGDRVEAGDVLLEVEGP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  85 A-DILTVERLILNFLGKLSGIATITNLMVKKAKEvnPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDN 163
Cdd:COG0157   84 ArALLTAERVALNLLQRLSGIATLTRRYVDAVAG--TGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 164 HITLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNV 243
Cdd:COG0157  162 HIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLENI 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 800907428 244 IDYAKTGVDVISSGYITHSYRSLDFSLDVEK 274
Cdd:COG0157  242 RAYAETGVDYISVGALTHSAPALDLSLRIEP 272
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 104-271 4.25e-76

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: 228.73  E-value: 4.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  104 IATITNLMVKKAKEVNpyVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLYGNLEELIKRVKFSVS 183
Cdd:pfam01729   1 IATATRRMVEAARSVK--VRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  184 FTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSK---VLLEASGGITPDNVIDYAKTGVDVISSGYIT 260
Cdd:pfam01729  79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERnprVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158

                         170
                  ....*....|.
gi 800907428  261 HSYRSLDFSLD 271
Cdd:pfam01729 159 HSVPPLDISLD 169
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 40-273 3.33e-59

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 190.70  E-value: 3.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  40 KDSGILAGNRFIVPFLKYLGFS-NIN-GEKDGREVKKGDIVLNFEGDA-DILTVERLILNFLGKLSGIATITNLMVKKAK 116
Cdd:PLN02716  56 KADGVLAGIALADMVFEEVDPSlKVEwAAIDGDFVHKGLKFGKVTGPAhSILVAERVVLNFMQRMSGIATLTKAMADAAK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 117 EVNpyvrIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLYGNLEELIKRVK---FSVSFTKIIEVEVS 193
Cdd:PLN02716 136 PAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVQSADkylEEKGLSMKIEVETR 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 194 SYEDAIRAF------KAGADVILLDNM-KPYEILPI-VNELKSKVLL-------EASGGITPDNVIDYAKTGVDVISSGY 258
Cdd:PLN02716 212 TLEEVKEVLeylsdtKTSLTRVMLDNMvVPLENGDVdVSMLKEAVELingrfetEASGNVTLDTVHKIGQTGVTYISSGA 291

                        250
                 ....*....|....*
gi 800907428 259 ITHSYRSLDFSLDVE 273
Cdd:PLN02716 292 LTHSVKALDISLKID 306
 
Name Accession Description Interval E-value
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 9-272 7.77e-139

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: 391.62  E-value: 7.77e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428    9 RLLDYLEEDVMPEDITT--KFLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDA- 85
Cdd:TIGR00078   1 LLDRWLREDLGSGDITTeaLVPGSTRATASLVAKEDGVLAGLPVARRVFEQLGVQVEWLVKDGDRVEPGEVVAEVEGPAr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   86 DILTVERLILNFLGKLSGIATITNLMVKKAKEVNpyVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHI 165
Cdd:TIGR00078  81 SLLTAERTALNFLGRLSGIATATRKYVEAARGTN--VRIADTRKTTPGLRLLEKYAVRVGGGDNHRLGLSDAVMIKDNHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  166 TLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNVID 245
Cdd:TIGR00078 159 AAAGSIEKAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGRVLLEASGGITLDNLEE 238

                         250       260
                  ....*....|....*....|....*..
gi 800907428  246 YAKTGVDVISSGYITHSYRSLDFSLDV 272
Cdd:TIGR00078 239 YAETGVDVISSGALTHSVPALDFSLKI 265
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 10-271 4.52e-123

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: 351.78  E-value: 4.52e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTK--FLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGfSNINGE---KDGREVKKGDIVLNFEGD 84
Cdd:cd01572    4 VRLALAEDLGRGDITSEaiIPPDARAEARLIAKEEGVLAGLPVAEEVFELLD-PGIEVEwlvKDGDRVEPGQVLATVEGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  85 A-DILTVERLILNFLGKLSGIATITNLMVKKAKEvnPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDN 163
Cdd:cd01572   83 ArSLLTAERTALNFLQRLSGIATLTRRYVEALAG--TKARILDTRKTTPGLRLLEKYAVRCGGGDNHRFGLSDAVLIKDN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 164 HITLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNV 243
Cdd:cd01572  161 HIAAAGSITEAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGRVLLEASGGITLENI 240

                        250       260
                 ....*....|....*....|....*...
gi 800907428 244 IDYAKTGVDVISSGYITHSYRSLDFSLD 271
Cdd:cd01572  241 RAYAETGVDYISVGALTHSAPALDISLD 268
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 10-274 1.17e-116

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: 335.45  E-value: 1.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTKFL--EGIRARGIVRCKDSGILAGNRFIVPFLKYLGfSNINGE---KDGREVKKGDIVLNFEGD 84
Cdd:COG0157    5 IRRALAEDLGYGDLTTEALipADARARARLIAREDGVLAGLEVAERVFRLLD-PGLEVEwlvADGDRVEAGDVLLEVEGP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  85 A-DILTVERLILNFLGKLSGIATITNLMVKKAKEvnPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDN 163
Cdd:COG0157   84 ArALLTAERVALNLLQRLSGIATLTRRYVDAVAG--TGARILDTRKTTPGLRALEKYAVRAGGGVNHRLGLSDAVLIKDN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 164 HITLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSKVLLEASGGITPDNV 243
Cdd:COG0157  162 HIAAAGGIAEAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLRGRALLEASGGITLENI 241

                        250       260       270
                 ....*....|....*....|....*....|.
gi 800907428 244 IDYAKTGVDVISSGYITHSYRSLDFSLDVEK 274
Cdd:COG0157  242 RAYAETGVDYISVGALTHSAPALDLSLRIEP 272
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 10-271 1.35e-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: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 335.21  E-value: 1.35e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTKFL--EGIRARGIVRCKDSGILAGNRFIVPFLKYL-GFSNINGEKDGREVKKGDIVLNFEGDA- 85
Cdd:cd01568    4 LDRALAEDLGYGDLTTEALipGDAPATATLIAKEEGVLAGLEVAEEVFELLdGIEVEWLVKDGDRVEAGQVLLEVEGPAr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  86 DILTVERLILNFLGKLSGIATITNLMVKKAKEvnPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHI 165
Cdd:cd01568   84 SLLTAERVALNLLQRLSGIATATRRYVEAARG--TKARIADTRKTTPGLRLLEKYAVRAGGGDNHRLGLSDAVLIKDNHI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 166 TLYGNLEELIKRVKFSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKS--KVLLEASGGITPDNV 243
Cdd:cd01568  162 AAAGGITEAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLKGlpRVLLEASGGITLENI 241

                        250       260
                 ....*....|....*....|....*...
gi 800907428 244 IDYAKTGVDVISSGYITHSYRSLDFSLD 271
Cdd:cd01568  242 RAYAETGVDVISTGALTHSAPALDISLK 269
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 104-271 4.25e-76

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: 228.73  E-value: 4.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  104 IATITNLMVKKAKEVNpyVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLYGNLEELIKRVKFSVS 183
Cdd:pfam01729   1 IATATRRMVEAARSVK--VRIADTRKTTPGLRPLEKYAVLIGGGDNHRLGLSDMVMIKDNHIAAAGSITEAVRRARQVAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  184 FTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSK---VLLEASGGITPDNVIDYAKTGVDVISSGYIT 260
Cdd:pfam01729  79 FAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERnprVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158

                         170
                  ....*....|.
gi 800907428  261 HSYRSLDFSLD 271
Cdd:pfam01729 159 HSVPPLDISLD 169
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 36-271 1.38e-72

Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.


Pssm-ID: 238286 [Multi-domain]  Cd Length: 281  Bit Score: 224.04  E-value: 1.38e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  36 IVRCKDSGILAGNRFIVPFLKYLGFS---NINGEKDGREVKKGDIVLNFEGDA-DILTVERLILNFLGKLSGIATITNLM 111
Cdd:cd00516   23 TAREDPYGVLAGLEEALELLELLRFPgplVILAVPEGTVVEPGEPLLTIEGPArELLLLERVLLNLLQRLSGIATATARY 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 112 VKKAKEVNPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLYGNLEELIKRVK--------FSVS 183
Cdd:cd00516  103 VEAAKGANTKVHDFGTRKTTPGLRLLEKYAVLIGGGDGHRNGLSDAILIKDNHGTMAHSIIQAFGELAavkalrrwLPEL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 184 FTKIIEVEVSSYEDAIRAFKAG-ADVILLDNMKPYEILPIVNELK----------SKVLLEASGGITPDNVIDYAKTGVD 252
Cdd:cd00516  183 FIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKarahldgkglPRVKIEASGGLDEENIRAYAETGVD 262

                        250
                 ....*....|....*....
gi 800907428 253 VISSGYITHSYRSLDFSLD 271
Cdd:cd00516  263 VFGVGTLLHSAPPLDIVLK 281
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 10-258 1.55e-61

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: 195.21  E-value: 1.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  10 LLDYLEEDVMPEDITTKFLeGIRARG--IV-RCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDAD 86
Cdd:cd01573    4 LERLLLEDAPYGDLTTEAL-GIGEQPgkITfRARDPGVLCGTEEAARILELLGLEVDLAAASGSRVAAGAVLLEAEGPAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  87 ILT-VERLILNFLGKLSGIATITNLMVKKAKEVNPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHI 165
Cdd:cd01573   83 ALHlGWKVAQTLLEWASGIATATAEMVAAARAVNPDIVVATTRKAFPGTRKLALKAILAGGAVPHRLGLSETILVFAEHR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 166 TLYGNLEEL--IKRVKfSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKSK---VLLEASGGITP 240
Cdd:cd01573  163 AFLGGPEPLkaLARLR-ATAPEKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLappVLLAAAGGINI 241

                        250       260
                 ....*....|....*....|
gi 800907428 241 DNVIDYAKTGVDVI--SSGY 258
Cdd:cd01573  242 ENAAAYAAAGADILvtSAPY 261
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 40-273 3.33e-59

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 190.70  E-value: 3.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  40 KDSGILAGNRFIVPFLKYLGFS-NIN-GEKDGREVKKGDIVLNFEGDA-DILTVERLILNFLGKLSGIATITNLMVKKAK 116
Cdd:PLN02716  56 KADGVLAGIALADMVFEEVDPSlKVEwAAIDGDFVHKGLKFGKVTGPAhSILVAERVVLNFMQRMSGIATLTKAMADAAK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 117 EVNpyvrIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLYGNLEELIKRVK---FSVSFTKIIEVEVS 193
Cdd:PLN02716 136 PAC----ILETRKTAPGLRLVDKWAVLIGGGKNHRMGLFDMVMIKDNHIAAAGGITNAVQSADkylEEKGLSMKIEVETR 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 194 SYEDAIRAF------KAGADVILLDNM-KPYEILPI-VNELKSKVLL-------EASGGITPDNVIDYAKTGVDVISSGY 258
Cdd:PLN02716 212 TLEEVKEVLeylsdtKTSLTRVMLDNMvVPLENGDVdVSMLKEAVELingrfetEASGNVTLDTVHKIGQTGVTYISSGA 291

                        250
                 ....*....|....*
gi 800907428 259 ITHSYRSLDFSLDVE 273
Cdd:PLN02716 292 LTHSVKALDISLKID 306
PRK06096 PRK06096
molybdenum transport protein ModD; Provisional
 5-258 2.05e-32

molybdenum transport protein ModD; Provisional


Pssm-ID: 180397 [Multi-domain]  Cd Length: 284  Bit Score: 120.21  E-value: 2.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   5 IYV--KRLLDYLEEDVMPEDITTKFL--EGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLN 80
Cdd:PRK06096   2 IFLsdAQLDALLLEDIQGGDLTTRALgiGHQPGYIEFFHRQGGCVSGISVACKMLTTLGLTIDDAVSDGSQANAGQRLIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  81 FEGDADIL----TVERLILNFLgklSGIATITNLMVKKAKEVNPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSD 156
Cdd:PRK06096  82 AQGNAAALhqgwKAVQNVLEWS---CGVSDYLAQMLALLRERYPDGNIACTRKAIPGTRLLATQAVLAAGGLIHRAGCAE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 157 AVLIKDNHITLYGNLEE---LIKRVKFSVSFTKIIeVEVSSYEDAIRAFKAGADVILLDNMKPYEILPIVNELKS---KV 230
Cdd:PRK06096 159 TILLFANHRHFLHDPQDwsgAINQLRRHAPEKKIV-VEADTPKEAIAALRAQPDVLQLDKFSPQQATEIAQIAPSlapHC 237

                        250       260       270
                 ....*....|....*....|....*....|
gi 800907428 231 LLEASGGITPDNVIDYAKTGVD--VISSGY 258
Cdd:PRK06096 238 TLSLAGGINLNTLKNYADCGIRlfITSAPY 267
modD TIGR01334
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ...
 12-254 3.11e-32

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: 119.62  E-value: 3.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   12 DYLEEDVMPEDITTKFL--EGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDADILT 89
Cdd:TIGR01334  10 NLLLEDIGYGDLTTRALgiQDHPAHITFTARDEGIVSGVSEAAKLLKQLGASIDYAVPSGSRALAGTLLLEAKGSAGQLH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   90 VE-RLILNFLGKLSGIATITNLMVKKAKEVNPYVRIAGTRKTTPGFRLFEKYAIEVGGGDPHRYNLSDAVLIKDNHITLY 168
Cdd:TIGR01334  90 QGwKSAQSVLEWSCGVATYTHKMVTLAKKISPMAVVACTRKAIPLTRPLAVKAVLAAGGVIHRIGLSETLLVFANHRTFL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  169 GNLEE---LIKRVKFSVSFTKIIeVEVSSYEDAIRAFKAGADVILLDNMKP---YEILPIVNELKSKVLLEASGGITPDN 242
Cdd:TIGR01334 170 NDNFDwggAIGRLKQTAPERKIT-VEADTIEQALTVLQASPDILQLDKFTPqqlHHLHERLKFFDHIPTLAAAGGINPEN 248

                         250
                  ....*....|..
gi 800907428  243 VIDYAKTGVDVI 254
Cdd:TIGR01334 249 IADYIEAGIDLF 260
QRPTase_N pfam02749
Quinolinate phosphoribosyl transferase, N-terminal domain; Quinolinate phosphoribosyl ...
 18-102 7.36e-21

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: 84.08  E-value: 7.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428   18 VMPEDITTK--FLEGIRARGIVRCKDSGILAGNRFIVPFLKYLGFSNINGEKDGREVKKGDIVLNFEGDA-DILTVERLI 94
Cdd:pfam02749   1 IGRGDLTTEalIPGDKKAKAVIIAKEEGVVAGLEEAERVFELLGLEVEWLVKDGDRVEAGDVILEIEGPArALLTAERVA 80


                  ....*...
gi 800907428   95 LNFLGKLS 102
Cdd:pfam02749  81 LNLLQRLS 88
TrpF COG0135
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ...
 167-257 1.08e-05

Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439905  Cd Length: 208  Bit Score: 45.13  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 167 LYGNL-EELIKRVK--FSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKP-----------YEILPIVNeLKSKVLL 232
Cdd:COG0135   82 LHGDEsPEYCAALRerLGLPVIKAIRVGDGADLEEAAAYAPVADALLLDAKVPglyggtgktfdWSLLAGLA-LPKPVIL 160

                         90       100
                 ....*....|....*....|....*....
gi 800907428 233 eaSGGITPDNVIDYAKT----GVDViSSG 257
Cdd:COG0135  161 --AGGLTPENVAEAIRLvrpyGVDV-SSG 186
PRAI cd00405
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ...
 163-257 3.67e-05

Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.


Pssm-ID: 238237  Cd Length: 203  Bit Score: 43.72  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 163 NHITLYGNL-EELIKRVK--FSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKP-----------YEILPIVNeLKS 228
Cdd:cd00405   75 DVVQLHGDEsPEYCAQLRarLGLPVIKAIRVKDEEDLEKAAAYAGEVDAILLDSKSGgggggtgktfdWSLLRGLA-SRK 153

                         90       100       110
                 ....*....|....*....|....*....|...
gi 800907428 229 KVLLeaSGGITPDNVIDYAKT----GVDViSSG 257
Cdd:cd00405  154 PVIL--AGGLTPDNVAEAIRLvrpyGVDV-SSG 183
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 115-254 2.85e-04

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 41.55  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  115 AKEVNPYvrIAGTRKTTPGfrlfekyaieVGGGDPHR----YNLSD-AVLIKDnhitlygnLEELIKRVKFSVsftKIIE 189
Cdd:pfam01645 155 GEKVSPE--IARIRGSPPG----------VGLISPPPhhdiYSIEDlAQLIYD--------LKEINPKAPISV---KLVS 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  190 VEVssyEDAIRAF--KAGADVILLDNMK------PYEI-----------LPIV------NELKSKVLLEASGGItpdnvi 244
Cdd:pfam01645 212 GHG---VGTIAAGvaKAGADIILIDGYDggtgasPKTSikhaglpwelaLAEAhqtlkeNGLRDRVSLIADGGL------ 282

                         170
                  ....*....|
gi 800907428  245 dyaKTGVDVI 254
Cdd:pfam01645 283 ---RTGADVA 289
PRK01222 PRK01222
phosphoribosylanthranilate isomerase;
173-257 1.23e-03

phosphoribosylanthranilate isomerase;


Pssm-ID: 234923  Cd Length: 210  Bit Score: 39.02  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 173 ELIKRVK--FSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDNMKPY----------EILPIvnELKSKVLLeaSGGITP 240
Cdd:PRK01222  90 EFCRQLKrrYGLPVIKALRVRSAGDLEAAAAYYGDADGLLLDAYVGLpggtgktfdwSLLPA--GLAKPWIL--AGGLNP 165

                         90       100
                 ....*....|....*....|.
gi 800907428 241 DNV---IDYAK-TGVDViSSG 257
Cdd:PRK01222 166 DNVaeaIRQVRpYGVDV-SSG 185
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
 173-220 1.53e-03

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 38.86  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 800907428 173 ELIKRVKFSVSFTKIIEVEVSSYE-DAIRAFKAGADVILLDNMKPYEIL 220
Cdd:PRK10651  69 ETLDKLREKSLSGRIVVFSVSNHEeDVVTALKRGADGYLLKDMEPEDLL 117
PRK07695 PRK07695
thiazole tautomerase TenI;
175-262 1.54e-03

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 38.85  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 175 IKRVKFSVSFTKIiEVEVSSYEDAIRAFKAGADVILLDNMKPYEILP--------IVNELKSKVLLE--ASGGITPDNVI 244
Cdd:PRK07695  86 VRSVREKFPYLHV-GYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgvpargleELSDIARALSIPviAIGGITPENTR 164

                         90       100
                 ....*....|....*....|
gi 800907428 245 DYAKTGVDVIS--SGYITHS 262
Cdd:PRK07695 165 DVLAAGVSGIAvmSGIFSSA 184
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 186-256 1.74e-03

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes 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. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428  186 KIIEVEVSSYEDAIRAFKAGADVILL---------DNMKPYEiLPIVNELKSKVLLE--ASGGITPDNVIDYAKTGVD-- 252
Cdd:pfam02581  96 LIIGVSTHTLEEALEAEALGADYIGFgpifptptkPDAPPLG-LEGLKAIAEAVEIPvvAIGGITPENVPEVIEAGADgv 174


                  ....*
gi 800907428  253 -VISS 256
Cdd:pfam02581 175 aVVSA 179
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 186-255 2.44e-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: 38.27  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 186 KIIEVEVSSYEDAIRAFKAGADVILL---------DNMKPYEILPIVNELKSKVLLE--ASGGITPDNVIDYAKTGVD-- 252
Cdd:cd00564   96 LIIGVSTHSLEEALRAEELGADYVGFgpvfptptkPGAGPPLGLELLREIAELVEIPvvAIGGITPENAAEVLAAGADgv 175


                 ....
gi 800907428 253 -VIS 255
Cdd:cd00564  176 aVIS 179
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 151-257 5.46e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 37.18  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 800907428 151 RYNLSDAVLIKDNHITLYGNLEELIKRVK-FSVSFTKIIEVEVSSYEDAIRAFKAGADVILLDN------MKPYEILPIV 223
Cdd:cd04722   81 RAAGADGVEIHGAVGYLAREDLELIRELReAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNggggggGRDAVPIADL 160

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 800907428 224 NE----LKSKVLLEASGGI-TPDNVIDYAKTGVDVISSG 257
Cdd:cd04722  161 LLilakRGSKVPVIAGGGInDPEDAAEALALGADGVIVG 199
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 197-251 9.85e-03

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: 36.34  E-value: 9.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 800907428 197 DAIRAFKAGADVILLDNMKPYEIlPIVNELKSK---VLLEASGGITPDNVIDYAKTGV 251
Cdd:cd00452  109 EIMQALELGADIVKLFPAEAVGP-AYIKALKGPfpqVRFMPTGGVSLDNAAEWLAAGV 165
 
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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