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Conserved domains on  [gi|1844084043|ref|NP_001305179|]
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nicotinate-nucleotide pyrophosphorylase [carboxylating] isoform 3 [Homo sapiens]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 36-136 2.62e-46

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member pfam01729:

Pssm-ID: 473867  Cd Length: 169  Bit Score: 148.23  E-value: 2.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPH 115
Cdd:pfam01729  69 AVRRARQVAPFAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTG 148

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:pfam01729 149 VDVISVGALTHSVPPLDISLD 169
 
Name Accession Description Interval E-value
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 36-136 2.62e-46

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: 148.23  E-value: 2.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPH 115
Cdd:pfam01729  69 AVRRARQVAPFAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTG 148

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:pfam01729 149 VDVISVGALTHSVPPLDISLD 169
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 36-137 2.73e-46

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: 151.25  E-value: 2.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGPH 115
Cdd:TIGR00078 167 AVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEEYAETG 243

                          90       100
                  ....*....|....*....|..
gi 1844084043 116 IDVISMGMLTQAAPALDFSLKL 137
Cdd:TIGR00078 244 VDVISSGALTHSVPALDFSLKI 265
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 36-136 2.53e-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: 238806 [Multi-domain]  Cd Length: 268  Bit Score: 146.08  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGPH 115
Cdd:cd01572   171 AVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGITLENIRAYAETG 247

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:cd01572   248 VDYISVGALTHSAPALDISLD 268
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 36-137 1.24e-35

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: 123.98  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaqfPSVAVEASGGITLDNLPQFCGPH 115
Cdd:COG0157   172 AVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR---GRALLEASGGITLENIRAYAETG 248

                          90       100
                  ....*....|....*....|..
gi 1844084043 116 IDVISMGMLTQAAPALDFSLKL 137
Cdd:COG0157   249 VDYISVGALTHSAPALDLSLRI 270
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 36-137 8.45e-20

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 83.23  E-value: 8.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQ---AADFTLKVEVECSSLQEAVQAAE------AGADLVLLDNF--KPEELHPTATVLKAQFPSVA----VEAS 100
Cdd:PLN02716  189 AVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVDVSMLKEAVELINgrfeTEAS 268

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1844084043 101 GGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 137
Cdd:PLN02716  269 GNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
 
Name Accession Description Interval E-value
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 36-136 2.62e-46

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: 148.23  E-value: 2.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPH 115
Cdd:pfam01729  69 AVRRARQVAPFAVKIEVEVESLEEAEEALEAGADIIMLDNFSPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTG 148

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:pfam01729 149 VDVISVGALTHSVPPLDISLD 169
nadC TIGR00078
nicotinate-nucleotide pyrophosphorylase; Synonym: quinolinate phosphoribosyltransferase ...
 36-137 2.73e-46

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: 151.25  E-value: 2.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGPH 115
Cdd:TIGR00078 167 AVKRARAAAPFTLKIEVEVESLEEAEEAAEAGADIIMLDNMKPEEIKEAVQLLKGR---VLLEASGGITLDNLEEYAETG 243

                          90       100
                  ....*....|....*....|..
gi 1844084043 116 IDVISMGMLTQAAPALDFSLKL 137
Cdd:TIGR00078 244 VDVISSGALTHSVPALDFSLKI 265
QPRTase cd01572
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 36-136 2.53e-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: 238806 [Multi-domain]  Cd Length: 268  Bit Score: 146.08  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQfpsVAVEASGGITLDNLPQFCGPH 115
Cdd:cd01572   171 AVRRARAAAPFTLKIEVEVETLEQLKEALEAGADIIMLDNMSPEELREAVALLKGR---VLLEASGGITLENIRAYAETG 247

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:cd01572   248 VDYISVGALTHSAPALDISLD 268
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 36-136 4.21e-42

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: 140.69  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaQFPSVAVEASGGITLDNLPQFCGPH 115
Cdd:cd01568   170 AVKRARAAAPFEKKIEVEVETLEEAEEALEAGADIIMLDNMSPEELKEAVKLLK-GLPRVLLEASGGITLENIRAYAETG 248

                          90       100
                  ....*....|....*....|.
gi 1844084043 116 IDVISMGMLTQAAPALDFSLK 136
Cdd:cd01568   249 VDVISTGALTHSAPALDISLK 269
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 36-137 1.24e-35

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: 123.98  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKaqfPSVAVEASGGITLDNLPQFCGPH 115
Cdd:COG0157   172 AVARARARAPPEKKIEVEVETLEELEEALAAGADIIMLDNMSPEELREAVALLR---GRALLEASGGITLENIRAYAETG 248

                          90       100
                  ....*....|....*....|..
gi 1844084043 116 IDVISMGMLTQAAPALDFSLKL 137
Cdd:COG0157   249 VDYISVGALTHSAPALDLSLRI 270
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
 36-136 1.79e-26

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: 100.39  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQAA--DFTLKVEVECSSLQEAVQAAEAG-ADLVLLDNFKPEELHPTATVLKAQ-------FPSVAVEASGGITL 105
Cdd:cd00516   171 AVKALRRWLpeLFIALIDVEVDTLEEALEAAKAGgADGIRLDSGSPEELDPAVLILKARahldgkgLPRVKIEASGGLDE 250

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1844084043 106 DNLPQFCGPHIDVISMGMLTQAAPALDFSLK 136
Cdd:cd00516   251 ENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
PLN02716 PLN02716
nicotinate-nucleotide diphosphorylase (carboxylating)
 36-137 8.45e-20

nicotinate-nucleotide diphosphorylase (carboxylating)


Pssm-ID: 178318 [Multi-domain]  Cd Length: 308  Bit Score: 83.23  E-value: 8.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  36 AVRAARQ---AADFTLKVEVECSSLQEAVQAAE------AGADLVLLDNF--KPEELHPTATVLKAQFPSVA----VEAS 100
Cdd:PLN02716  189 AVQSADKyleEKGLSMKIEVETRTLEEVKEVLEylsdtkTSLTRVMLDNMvvPLENGDVDVSMLKEAVELINgrfeTEAS 268

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1844084043 101 GGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKL 137
Cdd:PLN02716  269 GNVTLDTVHKIGQTGVTYISSGALTHSVKALDISLKI 305
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 49-137 8.34e-15

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: 69.25  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  49 KVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAA 128
Cdd:cd01573   185 KIVVEVDSLEEALAAAEAGADILQLDKFSPEELAELVPKLRSLAPPVLLAAAGGINIENAAAYAAAGADILVTSAPYYAK 264


                  ....*....
gi 1844084043 129 PAlDFSLKL 137
Cdd:cd01573   265 PA-DIKVKI 272
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 37-131 4.65e-08

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: 49.82  E-value: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  37 VRAARQAADFTLkveVECSSLQEAVQAAEAGADLVLLDNFKPEeLHPTATVLKAQFPSVAVEASGGITLDNLPQFCGphI 116
Cdd:cd00452    90 VKAANRAGIPLL---PGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEWLA--A 163

                          90
                  ....*....|....*
gi 1844084043 117 DVISMGMLTQAAPAL 131
Cdd:cd00452   164 GVVAVGGGSLLPKDA 178
modD TIGR01334
putative molybdenum utilization protein ModD; The gene modD for a member of this family is ...
 49-137 7.84e-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: 49.90  E-value: 7.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  49 KVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAA 128
Cdd:TIGR01334 190 KITVEADTIEQALTVLQASPDILQLDKFTPQQLHHLHERLKFFDHIPTLAAAGGINPENIADYIEAGIDLFITSAPYYAA 269


                  ....*....
gi 1844084043 129 PAlDFSLKL 137
Cdd:TIGR01334 270 PC-DIKVKL 277
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 54-135 1.72e-04

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 39.98  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  54 CSSLQEAVQAAEAGADLVlldnfkpeELHPTATV-------LKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMG-MLT 125
Cdd:PRK06552  116 CMTVTEIVTALEAGSEIV--------KLFPGSTLgpsfikaIKGPLPQVNVMVTGGVNLDNVKDWFAAGADAVGIGgELN 187

                          90
                  ....*....|
gi 1844084043 126 QAAPALDFSL 135
Cdd:PRK06552  188 KLASQGDFDL 197
PRK07695 PRK07695
thiazole tautomerase TenI;
30-129 5.64e-04

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 38.46  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  30 LNYAALAVRAARQAADFtLKVEVECSSLQEAVQAAEAGADLVLLDN---------FKPEELHPTATVlkAQFPSVAVEAS 100
Cdd:PRK07695   79 LGYRSFSVRSVREKFPY-LHVGYSVHSLEEAIQAEKNGADYVVYGHvfptdckkgVPARGLEELSDI--ARALSIPVIAI 155

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1844084043 101 GGITLDNLPQF--CGPH-IDVISmGMLTQAAP 129
Cdd:PRK07695  156 GGITPENTRDVlaAGVSgIAVMS-GIFSSANP 186
PRK08999 PRK08999
Nudix family hydrolase;
30-108 9.32e-04

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 37.93  E-value: 9.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  30 LNYAALAVRAARQAADFTLkVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVL--------KAQFPsVAVEASG 101
Cdd:PRK08999  210 LTSAQLAALAARPLPAGRW-VAASCHDAEELARAQRLGVDFAVLSPVQPTASHPGAAPLgwegfaalIAGVP-LPVYALG 287


                  ....*..
gi 1844084043 102 GITLDNL 108
Cdd:PRK08999  288 GLGPGDL 294
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 35-110 2.61e-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: 36.34  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084043  35 LAVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNF-----KPEELHP------TATVLKAQFPSVAVeasGGI 103
Cdd:cd00564    83 LPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVfptptKPGAGPPlglellREIAELVEIPVVAI---GGI 159


                  ....*..
gi 1844084043 104 TLDNLPQ 110
Cdd:cd00564   160 TPENAAE 166
 
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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