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Conserved domains on  [gi|518932890|ref|WP_020088765|]
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pantetheine-phosphate adenylyltransferase [Levilactobacillus parabrevis]

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 ...
 1-159 5.65e-91

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: 261.47  E-value: 5.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSV 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518932890  81 NATVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRDRLER 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-159 5.65e-91

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: 261.47  E-value: 5.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSV 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518932890  81 NATVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRDRLER 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 2.67e-86

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: 249.30  E-value: 2.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSVNA 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518932890  83 TVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRD 155
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-157 1.05e-71

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: 212.52  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890    3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSVNA 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518932890   83 TVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRDRL 157
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 5.17e-23

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: 88.15  E-value: 5.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890    5 VFPGSFDPLTNGHLDLIQRASRMFDH-LIVAVGQNTS----KRGVFTASERVAFIEagtQALANVSVQVEA--GLTVDFM 77
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPphklKRPLFSAEERLEMLE---LAKWVDEVIVVApwELTRELL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518932890   78 RSVNATVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEV 134
Cdd:pfam01467  78 KELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-63 2.06e-07

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 47.95  E-value: 2.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518932890   4 AVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSKRGVFTASERVAFIeagTQALAN 63
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGsaqESHTLKNPFTAGERILMI---RKALEE 62
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-66 2.22e-07

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 48.01  E-value: 2.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 518932890    12 PLTNGHLDLIQRASRMFDHLIV-AVGQNTSkrgVFTASERVAFIEAGTQALANVSV 66
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLfVVSEDAS---LFSFDERFALVKKGTKDLDNVTV 62
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-159 5.65e-91

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: 261.47  E-value: 5.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSV 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518932890  81 NATVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRDRLER 159
Cdd:COG0669   81 GANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-155 2.67e-86

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: 249.30  E-value: 2.67e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSVNA 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518932890  83 TVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRD 155
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-157 1.05e-71

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: 212.52  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890    3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQVEAGLTVDFMRSVNA 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518932890   83 TVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEVAQFGGDLTQLVPPAVAQGLRDRL 157
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-134 5.17e-23

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: 88.15  E-value: 5.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890    5 VFPGSFDPLTNGHLDLIQRASRMFDH-LIVAVGQNTS----KRGVFTASERVAFIEagtQALANVSVQVEA--GLTVDFM 77
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPphklKRPLFSAEERLEMLE---LAKWVDEVIVVApwELTRELL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518932890   78 RSVNATVLVRGLRNSTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKEV 134
Cdd:pfam01467  78 KELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-61 1.94e-16

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: 69.26  E-value: 1.94e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518932890    3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG-----QNTSKRGVFTASERVAFIEAGTQAL 61
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGsdqfvNPLKGEPVFSLEERLEMLKALKYVD 64
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-133 9.72e-13

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: 61.69  E-value: 9.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRA-SRMFDHLIVAVGQNT----SKRGVFTASERVAFIEAGTQALANVSV----QVEAGLT 73
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEAlEEALDEVIIIIVSNPpkkkRNKDPFSLHERVEMLKEILKDRLKVVPvdfpEVKILLA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518932890  74 VDFMRS----VNATVLVRGLRnsTDFEFEQGIAGMNRSLDDQIDTVCLMAAPKYQFVSSSLLKE 133
Cdd:cd02039   81 VVFILKillkVGPDKVVVGED--FAFGKNASYNKDLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-61 4.03e-12

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: 60.59  E-value: 4.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSKRGVFTASERVAFIeagTQAL 61
Cdd:COG1056    2 MKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGsaqESHTPRNPFTAGERIEMI---RAAL 62
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-151 2.53e-08

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: 50.70  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMF--DHLI-VAVGQNTSK-RGVFTASERVAFIEAGTQALANVSV-QVEAGL----- 72
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLlLPSANPPHKpPKPASFEHRLEMLKLAIEDNPKFEVsDIEIKRdgpsy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890  73 TVDFMRSVNAT------VLVRG----LRNSTDFEFEQ-----GIAGMNRSLDDQIDT----------VCLMAAPKYQFVS 127
Cdd:cd02165   81 TIDTLEELRERypnaelYFIIGsdnlIRLPKWYDWEEllslvHLVVAPRPGYPIEDAsleklllpggRIILLDNPLLNIS 160

                        170       180
                 ....*....|....*....|....
gi 518932890 128 SSLLKEVAQFGGDLTQLVPPAVAQ 151
Cdd:cd02165  161 STEIRERLKNGKSIRYLLPPAVAD 184
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-130 7.36e-08

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: 47.92  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   4 AVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQN---TSKRGVFTASERVafieagtqalanvsvqveagltvdfmRSV 80
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNppvKVWQDPHELEERK--------------------------ESI 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518932890  81 NATVLVRGLRNSTDFEFEQGiAGMNRSLDDQIDTVCLMA-APKYQFVSSSL 130
Cdd:cd02156   56 EEDISVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRlNLETTVMSKRK 105
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-63 2.06e-07

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 47.95  E-value: 2.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518932890   4 AVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSKRGVFTASERVAFIeagTQALAN 63
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGsaqESHTLKNPFTAGERILMI---RKALEE 62
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-66 2.22e-07

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 48.01  E-value: 2.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 518932890    12 PLTNGHLDLIQRASRMFDHLIV-AVGQNTSkrgVFTASERVAFIEAGTQALANVSV 66
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLfVVSEDAS---LFSFDERFALVKKGTKDLDNVTV 62
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
2-56 8.80e-07

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 47.31  E-value: 8.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518932890   2 TIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSKRGVFTASERVAFIEA 56
Cdd:PRK05379   7 DYLVFIGRFQPFHNGHLAVIREALSRAKKVIVLIGsadLARSIKNPFSFEERAQMIRA 64
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 12-79 3.02e-06

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 45.72  E-value: 3.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518932890  12 PLTNGHLDLIQRASRMFDHLIVAVGQNTSKRgvFTASERVAFIEAGTQALANVSVqVEAGltvDFMRS 79
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLFVVSEDKSL--FSFADRFKLVKKGTKHLKNVTV-HSGG---DYIIS 186
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-66 3.31e-06

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: 44.59  E-value: 3.31e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518932890   4 AVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSKRGVFTASERVAFIeagTQALANVSV 66
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIGsaqESHTLENPFTAGERVLMI---RRALEEEGI 64
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
 3-60 4.81e-06

Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also containing a Nudix hydrolase domain; N-terminal NMNAT (Nicotinamide/nicotinate mononucleotide adenylyltransferase) domain of a novel bifunctional enzyme endowed with NMN adenylyltransferase and Nudix hydrolase activities. This domain is highly homologous to the archeal NMN adenyltransferase that catalyzes NAD synthesis from NMN and ATP. NMNAT is an essential 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. The C-terminal domain of this enzyme shares homology with the archaeal ADP-ribose pyrophosphatase, a member of the 'Nudix' hydrolase family.


Pssm-ID: 173919  Cd Length: 181  Bit Score: 44.29  E-value: 4.81e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRGV---FTASERVAFIEAGTQA 60
Cdd:cd02168    1 YLVYIGRFQPFHNGHLAVVLIALEKAKKVIILIGSARTARNIknpWTSEEREVMIEAALSD 61
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-151 1.08e-05

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: 43.57  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMFD----HLIVAvGQN--TSKRGVFTASERVAFIEAGTQALANVSV-QVEAGL- 72
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLGldevIFVPA-GQPphKKHKPLASAEHRLAMLRLAIADNPRFEVsDIELERp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890  73 ----TVDFMRSvnatvlVRGLRNSTDF----------------EFEQ-----GIAGMNR---SLDDQIDTVCLMAAPKYQ 124
Cdd:COG1057   81 gpsyTIDTLRE------LREEYPDAELyfiigadallqlpkwkRWEEllelaHLVVVPRpgyELDELEELEALKPGGRII 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 518932890 125 F-------VSSSLLKEVAQFGGDLTQLVPPAVAQ 151
Cdd:COG1057  155 LldvplldISSTEIRERLAEGKSIRYLVPDAVED 188
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 7-56 1.75e-05

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: 42.01  E-value: 1.75e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518932890   7 PGSFDPLTNGHLDLIQRASRMFDHLIVAVG---QNTSK--RGVFTASERVAFIEA 56
Cdd:COG0615    6 YGTFDLLHPGHINLLKRAKALGDELIVGVAtdeFVASKgrKPIIPEEQRKEIVEA 60
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-151 3.20e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 42.13  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRASRMF--DHLIVAV-GQN--TSKRGVFTASERVAFIEAGTQALANVSV-QVEAGL-- 72
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLglDEVWFLPnPGPphKPQKPLAPLEHRLAMLELAIADNPRFSVsDIELERpg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518932890  73 ---TVDFMRSVNAT------VLVRGLRNSTDF----EFEQ-----GIAGMNR------SLDDQIDTVCLMAAPKYQFV-- 126
Cdd:PRK00071  84 psyTIDTLRELRARypdvelVFIIGADALAQLprwkRWEEildlvHFVVVPRpgypleALALPALQQLLEAAGAITLLdv 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 518932890 127 -----SSSLLKEVAQFGGDLTQLVPPAVAQ 151
Cdd:PRK00071 164 pllaiSSTAIRERIKEGRPIRYLLPEAVLD 193
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 8-56 5.81e-04

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: 38.04  E-value: 5.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518932890   8 GSFDPLTNGHLDLIQRASRMFDHLIVAVG-----QNTSKRGVFTASERVAFIEA 56
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVArdetvAKIKRRPILPEEQRAEVVEA 61
PRK08099 PRK08099
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ...
 2-41 8.21e-04

multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;


Pssm-ID: 236151 [Multi-domain]  Cd Length: 399  Bit Score: 38.48  E-value: 8.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 518932890   2 TIAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSK 41
Cdd:PRK08099  53 KIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIICYDDER 92
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 8-35 1.40e-03

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 36.69  E-value: 1.40e-03
                         10        20
                 ....*....|....*....|....*...
gi 518932890   8 GSFDPLTNGHLDLIQRASRMFDHLIVAV 35
Cdd:cd02171    8 GTFDLLHIGHLNLLERAKALGDKLIVAV 35
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
3-68 1.82e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 37.46  E-value: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMFDH---LIVAVGQNTSKRGVFTASERVAFIEAGTQALANVSVQV 68
Cdd:PRK06973  24 IGILGGTFDPIHDGHLALARRFADVLDLtelVLIPAGQPWQKADVSAAEHRLAMTRAAAASLVLPGVTV 92
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-24 3.02e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 36.85  E-value: 3.02e-03
                         10        20
                 ....*....|....*....|....
gi 518932890   1 MTIAVFPGSFDPLTNGHLDLIQRA 24
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKA 24
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 3-43 7.71e-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: 35.16  E-value: 7.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 518932890   3 IAVFPGSFDPLTNGHLDLIQRASRMFDHLIVAVGQNTSKRG 43
Cdd:cd02167    1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDD 41
 
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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