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Conserved domains on  [gi|556486067|ref|WP_023334018|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [Enterobacter]

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 ...
 3-159 1.34e-104

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: 295.76  E-value: 1.34e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   3 TKAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQ 82
Cdd:COG0669    2 RIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556486067  83 ANILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALMEKLK 159
Cdd:COG0669   82 ANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 3-159 1.34e-104

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: 295.76  E-value: 1.34e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   3 TKAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQ 82
Cdd:COG0669    2 RIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556486067  83 ANILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALMEKLK 159
Cdd:COG0669   82 ANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 9.42e-99

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: 280.89  E-value: 9.42e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556486067  84 NILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALME 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 8.29e-78

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: 227.93  E-value: 8.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067    4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556486067   84 NILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALMEKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 1.84e-32

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: 112.03  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067    6 IYPGTFDPITNGHLDIITRAACMFDK-VILAIAASPS----KKPMFDLNERVQLATdAISHLPNVEVVGFSDLMANFARA 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPphklKRPLFSAEERLEMLE-LAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 556486067   81 QQANILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEV 135
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-67 6.48e-10

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 55.23  E-value: 6.48e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556486067   1 MSTKAIYPGTFDPITNGHLDIITRAACMF--DKVILAIAASP---SKKPMFDLNERVQLATDAISHLPNVEV 67
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPNPGPphkPQKPLAPLEHRLAMLELAIADNPRFSV 74
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 3-159 1.34e-104

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: 295.76  E-value: 1.34e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   3 TKAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQ 82
Cdd:COG0669    2 RIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556486067  83 ANILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALMEKLK 159
Cdd:COG0669   82 ANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFA 158
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 9.42e-99

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: 280.89  E-value: 9.42e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556486067  84 NILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALME 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 8.29e-78

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: 227.93  E-value: 8.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067    4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKPMFDLNERVQLATDAISHLPNVEVVGFSDLMANFARAQQA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556486067   84 NILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEVARHHGDVTHFLPTNVHQALMEKL 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 1.84e-32

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: 112.03  E-value: 1.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067    6 IYPGTFDPITNGHLDIITRAACMFDK-VILAIAASPS----KKPMFDLNERVQLATdAISHLPNVEVVGFSDLMANFARA 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPphklKRPLFSAEERLEMLE-LAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 556486067   81 QQANILIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSTLVKEV 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 5.32e-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: 5.32e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556486067    4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAI----AASPSKK-PMFDLNERVQLATDAISHLPN 64
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVgsdqFVNPLKGePVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-134 6.15e-12

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: 59.38  E-value: 6.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKKP-----MFDLNERVQLATDAISHLPNVEVVGF---SDLMA 75
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKkrnkdPFSLHERVEMLKEILKDRLKVVPVDFpevKILLA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556486067  76 NFARAQQAN-----ILIRGLRAVADFEYEMQlaHMNRHLMPELESVFLMPSKEWSFISSTLVKE 134
Cdd:cd02039   81 VVFILKILLkvgpdKVVVGEDFAFGKNASYN--KDLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 5-152 1.53e-10

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: 56.67  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   5 AIYPGTFDPITNGHLDIITRAA--CMFDKVILAIAASP---SKKPMFDLNERVQLATDAISHLPNVEV-------VGFS- 71
Cdd:COG1057    5 GIFGGTFDPIHIGHLALAEEAAeqLGLDEVIFVPAGQPphkKHKPLASAEHRLAMLRLAIADNPRFEVsdielerPGPSy 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067  72 --DLMANFaRAQQAN---ILIRGLRAVADF----EYE--MQLAH---MNR--HLMPELESV-FLMPSKEWSF-------I 127
Cdd:COG1057   85 tiDTLREL-REEYPDaelYFIIGADALLQLpkwkRWEelLELAHlvvVPRpgYELDELEELeALKPGGRIILldvplldI 163

                        170       180
                 ....*....|....*....|....*
gi 556486067 128 SSTLVKEVARHHGDVTHFLPTNVHQ 152
Cdd:COG1057  164 SSTEIRERLAEGKSIRYLVPDAVED 188
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-67 6.48e-10

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 55.23  E-value: 6.48e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556486067   1 MSTKAIYPGTFDPITNGHLDIITRAACMF--DKVILAIAASP---SKKPMFDLNERVQLATDAISHLPNVEV 67
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPNPGPphkPQKPLAPLEHRLAMLELAIADNPRFSV 74
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 5-152 1.85e-09

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: 53.79  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   5 AIYPGTFDPITNGHLDIITRAACMF--DKVILAIAASPSKKP--MFDLNERVQLATDAISHLPNVEV------------- 67
Cdd:cd02165    2 ALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPPHKPpkPASFEHRLEMLKLAIEDNPKFEVsdieikrdgpsyt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067  68 -------------------VGfSDLMANFAR-------AQQANILIrGLRAVADFEYEMQLAHMNRHLMPELESVFLMPs 121
Cdd:cd02165   82 idtleelrerypnaelyfiIG-SDNLIRLPKwydweelLSLVHLVV-APRPGYPIEDASLEKLLLPGGRIILLDNPLLN- 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 556486067 122 kewsfISSTLVKEVARHHGDVTHFLPTNVHQ 152
Cdd:cd02165  159 -----ISSTEIRERLKNGKSIRYLLPPAVAD 184
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-131 2.31e-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: 51.77  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556486067   4 KAIYPGTFDPITNGHLDIITRAACMFDKVILAIAASPSKK---PMFDLNERVQLAtdaishlpnvevvgfsdlmanfara 80
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKvwqDPHELEERKESI------------------------- 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556486067  81 qQANILIRGLRAVADFEYEMQlAHMNRHLMPELESVFLMPS-KEWSFISSTL 131
Cdd:cd02156   56 -EEDISVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRLnLETTVMSKRK 105
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 6-67 2.93e-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: 39.22  E-value: 2.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556486067    6 IYPGTFDPITNGHLDIITRAACMF--DKVILAIAASPSKKPMF---DLNERVQLATDAISHLPNVEV 67
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLdlDKVIFVPTANPPHKKTYeaaSSHHRLAMLKLAIEDNPKFEV 67
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 3-68 8.50e-04

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: 37.39  E-value: 8.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556486067   3 TKAIYPGTFDPITNGHLDIITRAACMFDKVILAIA-----ASPSKKPMFDLNERVQLatdaISHLPNV-EVV 68
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVAtdefvASKGRKPIIPEEQRKEI----VEALKYVdEVI 68
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
5-70 8.64e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 38.39  E-value: 8.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556486067   5 AIYPGTFDPITNGHLDIITRA--ACMFDKVILAIAA-SPSKKP--MFDLNERVQLATDAISHLPNVEVVGF 70
Cdd:PRK07152   4 AIFGGSFDPIHKGHINIAKKAikKLKLDKLFFVPTYiNPFKKKqkASNGEHRLNMLKLALKNLPKMEVSDF 74
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 9-54 1.46e-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: 36.89  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556486067   9 GTFDPITNGHLDIITRAACMFDKVILAIA-----ASPSKKPMFDLNERVQL 54
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVArdetvAKIKRRPILPEEQRAEV 58
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 3-36 4.35e-03

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 36.00  E-value: 4.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 556486067   3 TKAIYPGTFDPITNGHLDIITRAACMFDKVILAI 36
Cdd:PRK01153   1 MRALFIGRFQPFHKGHLEVIKWILEEVDELIIGI 34
 
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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