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Conserved domains on  [gi|970949423|ref|NP_001305178|]
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nicotinate-nucleotide pyrophosphorylase [carboxylating] isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nadC super family cl36584
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 38-140 3.22e-49

nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase (decarboxylating) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


The actual alignment was detected with superfamily member TIGR00078:

Pssm-ID: 272894 [Multi-domain]  Cd Length: 265  Bit Score: 158.96  E-value: 3.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGP 117
Cdd:TIGR00078 166 KAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEEYAET 242

                          90       100
                  ....*....|....*....|...
gi 970949423  118 HIDVISMGMLTQAAPALDFSLKL 140
Cdd:TIGR00078 243 GVDVISSGALTHSVPALDFSLKI 265
 
Name Accession Description Interval E-value
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 38-140 3.22e-49

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: 158.96  E-value: 3.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGP 117
Cdd:TIGR00078 166 KAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEEYAET 242

                          90       100
                  ....*....|....*....|...
gi 970949423  118 HIDVISMGMLTQAAPALDFSLKL 140
Cdd:TIGR00078 243 GVDVISSGALTHSVPALDFSLKI 265
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 38-139 5.84e-49

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: 155.16  E-value: 5.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGP 117
Cdd:pfam01729  68 EAVRRARQVAPFAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKT 147

                          90       100
                  ....*....|....*....|..
gi 970949423  118 HIDVISMGMLTQAAPALDFSLK 139
Cdd:pfam01729 148 GVDVISVGALTHSVPPLDISLD 169
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 38-139 4.22e-46

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: 150.70  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGP 117
Cdd:cd01572  170 EAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGITLENIRAYAET 246

                         90       100
                 ....*....|....*....|..
gi 970949423 118 HIDVISMGMLTQAAPALDFSLK 139
Cdd:cd01572  247 GVDYISVGALTHSAPALDISLD 268
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 38-140 1.04e-37

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: 129.37  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaqfPSVAVEASGGITLDNLPQFCGP 117
Cdd:COG0157  171 EAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR---GRALLEASGGITLENIRAYAET 247

                         90       100
                 ....*....|....*....|...
gi 970949423 118 HIDVISMGMLTQAAPALDFSLKL 140
Cdd:COG0157  248 GVDYISVGALTHSAPALDLSLRI 270
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 38-140 1.85e-20

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 85.15  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQ---AADFALKVEVECSSLQEAVQAAE------AGADLVLLDNFK--PEELHPTATVLKAQFPSVA----VEA 102
Cdd:PLN02716 188 NAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVvpLENGDVDVSMLKEAVELINgrfeTEA 267

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 970949423 103 SGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 140
Cdd:PLN02716 268 SGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
 
Name Accession Description Interval E-value
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 38-140 3.22e-49

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: 158.96  E-value: 3.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGP 117
Cdd:TIGR00078 166 KAVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEEYAET 242

                          90       100
                  ....*....|....*....|...
gi 970949423  118 HIDVISMGMLTQAAPALDFSLKL 140
Cdd:TIGR00078 243 GVDVISSGALTHSVPALDFSLKI 265
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 38-139 5.84e-49

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: 155.16  E-value: 5.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGP 117
Cdd:pfam01729  68 EAVRRARQVAPFAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKT 147

                          90       100
                  ....*....|....*....|..
gi 970949423  118 HIDVISMGMLTQAAPALDFSLK 139
Cdd:pfam01729 148 GVDVISVGALTHSVPPLDISLD 169
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 38-139 4.22e-46

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: 150.70  E-value: 4.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGP 117
Cdd:cd01572  170 EAVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGITLENIRAYAET 246

                         90       100
                 ....*....|....*....|..
gi 970949423 118 HIDVISMGMLTQAAPALDFSLK 139
Cdd:cd01572  247 GVDYISVGALTHSAPALDISLD 268
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 38-139 2.61e-44

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: 146.47  E-value: 2.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaQFPSVAVEASGGITLDNLPQFCGP 117
Cdd:cd01568  169 EAVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLK-GLPRVLLEASGGITLENIRAYAET 247

                         90       100
                 ....*....|....*....|..
gi 970949423 118 HIDVISMGMLTQAAPALDFSLK 139
Cdd:cd01568  248 GVDVISTGALTHSAPALDISLK 269
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 38-140 1.04e-37

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: 129.37  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaqfPSVAVEASGGITLDNLPQFCGP 117
Cdd:COG0157  171 EAVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR---GRALLEASGGITLENIRAYAET 247

                         90       100
                 ....*....|....*....|...
gi 970949423 118 HIDVISMGMLTQAAPALDFSLKL 140
Cdd:COG0157  248 GVDYISVGALTHSAPALDLSLRI 270
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 37-139 3.45e-28

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: 105.01  E-value: 3.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  37 LKAVRAARQAA--DFALKVEVECSSLQEAVQAAEAG-ADLVLLDNFKPEELHPTATVLKAQ-------FPSVAVEASGGI 106
Cdd:cd00516  169 LAAVKALRRWLpeLFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARahldgkgLPRVKIEASGGL 248

                         90       100       110
                 ....*....|....*....|....*....|...
gi 970949423 107 TLDNLPQFCGPHIDVISMGMLTQAAPALDFSLK 139
Cdd:cd00516  249 DEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 38-140 1.85e-20

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 85.15  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  38 KAVRAARQ---AADFALKVEVECSSLQEAVQAAE------AGADLVLLDNFK--PEELHPTATVLKAQFPSVA----VEA 102
Cdd:PLN02716 188 NAVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMVvpLENGDVDVSMLKEAVELINgrfeTEA 267

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 970949423 103 SGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 140
Cdd:PLN02716 268 SGNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 37-140 5.96e-16

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: 72.33  E-value: 5.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  37 LKAVRAARQAADfALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCG 116
Cdd:cd01573  171 LKALARLRATAP-EKKIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPVLLAAAGGINIENAAAYAA 249

                         90       100
                 ....*....|....*....|....
gi 970949423 117 PHIDVISMGMLTQAAPAlDFSLKL 140
Cdd:cd01573  250 AGADILVTSAPYYAKPA-DIKVKI 272
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 33-134 1.32e-09

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: 54.06  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  33 SP-WTLKAVRAARQAADFALkveVECSSLQEAVQAAEAGADLVLLDNFKPEeLHPTATVLKAQFPSVAVEASGGITLDNL 111
Cdd:cd00452   82 SPgLDPEVVKAANRAGIPLL---PGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNA 157

                         90       100
                 ....*....|....*....|...
gi 970949423 112 PQFCGphIDVISMGMLTQAAPAL 134
Cdd:cd00452  158 AEWLA--AGVVAVGGGSLLPKDA 178
modD TIGR01334
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ...
 52-140 5.44e-08

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: 50.28  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423   52 KVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAA 131
Cdd:TIGR01334 190 KITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGGINPENIADYIEAGIDLFITSAPYYAA 269


                  ....*....
gi 970949423  132 PAlDFSLKL 140
Cdd:TIGR01334 270 PC-DIKVKL 277
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 57-138 9.34e-05

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 180618  Cd Length: 213  Bit Score: 40.75  E-value: 9.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  57 CSSLQEAVQAAEAGADLVlldnfkpeELHPTATV-------LKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMG-MLT 128
Cdd:PRK06552 116 CMTVTEIVTALEAGSEIV--------KLFPGSTLgpsfikaIKGPLPQVNVMVTGGVNLDNVKDWFAAGADAVGIGgELN 187

                         90
                 ....*....|
gi 970949423 129 QAAPALDFSL 138
Cdd:PRK06552 188 KLASQGDFDL 197
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 40-113 3.44e-04

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: 39.04  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  40 VRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNF-----KPEELHP------TATVLKAQFPSVAVeasGGITL 108
Cdd:cd00564   85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVfptptKPGAGPPlglellREIAELVEIPVVAI---GGITP 161


                 ....*
gi 970949423 109 DNLPQ 113
Cdd:cd00564  162 ENAAE 166
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 35-125 2.12e-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: 36.80  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  35 WTLKAVRAARQAA-DFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTA-------TVLKAQFPSVAVEASGGI 106
Cdd:cd04722  100 EDLELIRELREAVpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAvpiadllLILAKRGSKVPVIAGGGI 179

                         90       100
                 ....*....|....*....|
gi 970949423 107 TL-DNLPQFCGPHIDVISMG 125
Cdd:cd04722  180 NDpEDAAEALALGADGVIVG 199
PRK07695 PRK07695
thiazole tautomerase TenI;
51-132 7.32e-03

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 35.38  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  51 LKVEVECSSLQEAVQAAEAGADLVLLDN---------FKPEELHPTATVlkAQFPSVAVEASGGITLDNLPQF--CGPH- 118
Cdd:PRK07695  96 LHVGYSVHSLEEAIQAEKNGADYVVYGHvfptdckkgVPARGLEELSDI--ARALSIPVIAIGGITPENTRDVlaAGVSg 173

                         90
                 ....*....|....
gi 970949423 119 IDVISmGMLTQAAP 132
Cdd:PRK07695 174 IAVMS-GIFSSANP 186
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 39-113 7.82e-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: 35.16  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949423  39 AVRAARQAADFALKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATV---------LKAQF--PSVAVeasGGIT 107
Cdd:COG0352   89 PVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPplgleglawWAELVeiPVVAI---GGIT 165


                 ....*.
gi 970949423 108 LDNLPQ 113
Cdd:COG0352  166 PENAAE 171
 
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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