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Conserved domains on  [gi|523632025|ref|WP_020769314|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [unclassified Leptospira]

Protein Classification

pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)

pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway

CATH:  3.40.50.620
EC:  2.7.7.3
Gene Ontology:  GO:0005524|GO:0015937|GO:0004595
PubMed:  33271445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-158 1.22e-99

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440433  Cd Length: 159  Bit Score: 283.43  E-value: 1.22e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   2 TRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKR 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025  82 GAKSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLKKL 158
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-158 1.22e-99

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 283.43  E-value: 1.22e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   2 TRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKR 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025  82 GAKSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLKKL 158
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 1.03e-93

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 268.18  E-value: 1.03e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKRGA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523632025  84 KSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLK 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 1.04e-73

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 217.53  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025    4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKRGA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523632025   84 KSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLKKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 5.88e-27

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 98.16  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025    6 VYPGSFDPLTRGHLDILQRSVGLFDK-VIIGVA----VNSNKSLLFSIEERIEFIREAtKGWENLEIDTFEGLTVDYCKK 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPsdepPHKLKRPLFSAEERLEMLELA-KWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523632025   81 RGAKSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEV 135
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-161 5.51e-09

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 52.53  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   1 MTRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSL-----LFSIEERIEFIREATKGWENLEIDTFE---- 71
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHkpqkpLAPLEHRLAMLELAIADNPRFSVSDIElerp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025  72 GL-----TVDYCKKRGAKS----IIrGLRAVTDF----DYEYAISLMN-----------KKLAPEVETIFLMSSNDYSFV 127
Cdd:PRK00071  83 GPsytidTLRELRARYPDVelvfII-GADALAQLprwkRWEEILDLVHfvvvprpgyplEALALPALQQLLEAAGAITLL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 523632025 128 -------SSTIVKEVARHGRDVSAQVPEHVSKALLK-KLYHK 161
Cdd:PRK00071 162 dvpllaiSSTAIRERIKEGRPIRYLLPEAVLDYIEKhGLYRS 203
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 2-158 1.22e-99

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 283.43  E-value: 1.22e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   2 TRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKR 81
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025  82 GAKSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLKKL 158
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 1.03e-93

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 268.18  E-value: 1.03e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKRGA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523632025  84 KSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLK 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 1.04e-73

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 217.53  E-value: 1.04e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025    4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFEGLTVDYCKKRGA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523632025   84 KSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEVARHGRDVSAQVPEHVSKALLKKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 5.88e-27

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 98.16  E-value: 5.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025    6 VYPGSFDPLTRGHLDILQRSVGLFDK-VIIGVA----VNSNKSLLFSIEERIEFIREAtKGWENLEIDTFEGLTVDYCKK 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPsdepPHKLKRPLFSAEERLEMLELA-KWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523632025   81 RGAKSIIRGLRAVTDFDYEYAISLMNKKLAPEVETIFLMSSNDYSFVSSTIVKEV 135
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-64 5.29e-13

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 60.40  E-value: 5.29e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523632025    4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGV----AVNSNKSL-LFSIEERIEFIREATKGWEN 64
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVgsdqFVNPLKGEpVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-134 2.72e-11

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 57.84  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVG-LFDKVIIGVAVNSNKSL----LFSIEERIEFIREATKGWENLEIDTFEG----LT 74
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEeALDEVIIIIVSNPPKKKrnkdPFSLHERVEMLKEILKDRLKVVPVDFPEvkilLA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523632025  75 VD----YCKKRGAKSIIRGLRAVTDFDYEYaiSLMNKKLAPEVETIFLMSSNDYSFVSSTIVKE 134
Cdd:cd02039   81 VVfilkILLKVGPDKVVVGEDFAFGKNASY--NKDLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-159 1.38e-10

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 56.87  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVGLF--DKVIIGVAVNS--NKSLLFSIEERIEFIREATKGWENLEIDTFEGL------ 73
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPphKPPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKrdgpsy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025  74 TVD---YCKKR----------GAKSIIR--------------GLRAVTDFDYEYAISLMNKKLAPEVETIFLmsSNDYSF 126
Cdd:cd02165   81 TIDtleELRERypnaelyfiiGSDNLIRlpkwydweellslvHLVVAPRPGYPIEDASLEKLLLPGGRIILL--DNPLLN 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 523632025 127 VSSTIVKEVARHGRDVSAQVPEHVSKALLK-KLY 159
Cdd:cd02165  159 ISSTEIRERLKNGKSIRYLLPPAVADYIKEhGLY 192
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 5-130 3.30e-09

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 51.39  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   5 AVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNS---NKSLLFSIEERIEFIREatkgwenleidtfegltvdyckkr 81
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPpvkVWQDPHELEERKESIEE------------------------ 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 523632025  82 gaKSIIRGLRAVTDFDYeYAISLMNKKLAPEVETIFLMSSN-DYSFVSST 130
Cdd:cd02156   58 --DISVCGEDFQQNREL-YRWVKDNITLPVDPEQVELPRLNlETTVMSKR 104
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-161 5.51e-09

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 52.53  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   1 MTRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSNKSL-----LFSIEERIEFIREATKGWENLEIDTFE---- 71
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHkpqkpLAPLEHRLAMLELAIADNPRFSVSDIElerp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025  72 GL-----TVDYCKKRGAKS----IIrGLRAVTDF----DYEYAISLMN-----------KKLAPEVETIFLMSSNDYSFV 127
Cdd:PRK00071  83 GPsytidTLRELRARYPDVelvfII-GADALAQLprwkRWEEILDLVHfvvvprpgyplEALALPALQQLLEAAGAITLL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 523632025 128 -------SSTIVKEVARHGRDVSAQVPEHVSKALLK-KLYHK 161
Cdd:PRK00071 162 dvpllaiSSTAIRERIKEGRPIRYLLPEAVLDYIEKhGLYRS 203
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-66 6.08e-09

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 52.12  E-value: 6.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   1 MTRIAVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAvNSNKSLL----FSIEERIEFIREATKgWENLE 66
Cdd:COG1056    1 MMKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIG-SAQESHTprnpFTAGERIEMIRAALK-EEGLS 68
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-71 1.39e-07

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 48.58  E-value: 1.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025   1 MTRIAVYPGSFDPLTRGHLDI---LQRSVGLfDKVIIGVAVNS---NKSLLFSIEERIEFIREATKGWENLEIDTFE 71
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALaeeAAEQLGL-DEVIFVPAGQPphkKHKPLASAEHRLAMLRLAIADNPRFEVSDIE 76
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
3-81 2.46e-06

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 46.09  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   3 RIAVYPGSFDPLTRGHLDILQRSVGL--FDKVIIGVAVNS---NKSLLFSIEERIEFIREATKGWENLEIDTFE------ 71
Cdd:PRK07152   2 KIAIFGGSFDPIHKGHINIAKKAIKKlkLDKLFFVPTYINpfkKKQKASNGEHRLNMLKLALKNLPKMEVSDFEikrqnv 81

                         90
                 ....*....|...
gi 523632025  72 ---GLTVDYCKKR 81
Cdd:PRK07152  82 sytIDTIKYFKKK 94
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
4-61 8.57e-06

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 44.23  E-value: 8.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVI--IGVAvNSNKSLL--FSIEERIEFIREATKG 61
Cdd:PRK05379   8 YLVFIGRFQPFHNGHLAVIREALSRAKKVIvlIGSA-DLARSIKnpFSFEERAQMIRAALAG 68
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 5-60 1.49e-05

Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present.


Pssm-ID: 173917  Cd Length: 163  Bit Score: 42.67  E-value: 1.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   5 AVYPGSFDPLTRGHLDILQRSVGLFDKVIIGVAvNSNKSLL----FSIEERIEFIREATK 60
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIG-SAQESHTlenpFTAGERVLMIRRALE 60
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-152 2.03e-04

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 39.99  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025    6 VYPGSFDPLTRGHLDILQRSVGLF--DKVI-IGVAVNSNKSL--LFSIEERIEFIREATKGWENLEIDTFEGL------- 73
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLdlDKVIfVPTANPPHKKTyeAASSHHRLAMLKLAIEDNPKFEVDDFEIKrggpsyt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523632025   74 --TVDYCKKRGAKS----IIrGLRAVTDFDYEYAI-SLMNK--------------KLAPEVETIFLMSSNDYSF------ 126
Cdd:TIGR00482  81 idTLKHLKKKYPDVelyfII-GADALRSFPLWKDWqELLELvhlvivprpgytldKALLEKAILRMHHGNLTLLhnprvp 159

                         170       180
                  ....*....|....*....|....*.
gi 523632025  127 VSSTIVKEVARHGRDVSAQVPEHVSK 152
Cdd:TIGR00482 160 ISSTEIRQRIRQGKSIEYLLPDPVIK 185
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 5-58 5.73e-04

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 38.32  E-value: 5.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025   5 AVYPGSFDPLTRGHLDILQRSVGLFDKVIIGV-AVNSNKSLL--FSIEERIEFIREA 58
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIgSAQESHTLKnpFTAGERILMIRKA 59
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-57 3.16e-03

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 35.73  E-value: 3.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523632025   1 MTRIAVYpGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSN-----KSLLFSIEERIEFIRE 57
Cdd:cd02170    1 MKRVYAA-GTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETvakikRRPILPEEQRAEVVEA 61
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 6-56 3.58e-03

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 35.46  E-value: 3.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 523632025   6 VY-PGSFDPLTRGHLDILQRSVGLFDKVIIGVAVNSN-----KSLLFSIEERIEFIR 56
Cdd:COG0615    3 VItYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFvaskgRKPIIPEEQRKEIVE 59
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 4-71 4.02e-03

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase


Pssm-ID: 173918  Cd Length: 158  Bit Score: 35.93  E-value: 4.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523632025   4 IAVYPGSFDPLTRGHLDILQRSVGLFDKVII---GVAVNSNKSLLFSIEERIEFIREATKGWENLEIDTFE 71
Cdd:cd02167    1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIivgSDDTRDDARTGLPLEKRLRWLREIFPDQENIVVHTLN 71
 
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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