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Conserved domains on  [gi|523533230|ref|WP_020751560|]
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pantetheine-phosphate adenylyltransferase [Lacticaseibacillus paracasei]

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 ...
3-162 1.62e-86

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: 250.30  E-value: 1.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   3 KKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARS 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSF-DGLLVDFARE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  83 IGARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYAKLGD 162
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
3-162 1.62e-86

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: 250.30  E-value: 1.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   3 KKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARS 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSF-DGLLVDFARE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  83 IGARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYAKLGD 162
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
5-158 1.75e-81

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: 237.36  E-value: 1.75e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARSIG 84
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGF-DGLLVDFARKHG 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523533230  85 ARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYA 158
Cdd:cd02163   80 ANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
5-160 3.48e-69

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: 206.36  E-value: 3.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230    5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARSIG 84
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVF-DGLLVDYAKELG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523533230   85 ARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYAKL 160
Cdd:TIGR01510  80 ATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
7-137 1.53e-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: 100.09  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230    7 VFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTN-----TSKKPLFSSEEKLALISEStAGLPNVKaMAAPKRLTVEFAR 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSdepphKLKRPLFSAEERLEMLELA-KWVDEVI-VVAPWELTRELLK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 523533230   82 SIGARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEV 137
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-154 1.95e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.68  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   1 MTKKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNT-----SKKPLFSSEEKLALIsestaglpnVKAMAAPKRL 75
Cdd:PRK00071   2 MMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPgpphkPQKPLAPLEHRLAML---------ELAIADNPRF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  76 TV---EFARSiGARFMIRGIR------------------NVADF---------------------GY--EADIATVNHDL 111
Cdd:PRK00071  73 SVsdiELERP-GPSYTIDTLRelrarypdvelvfiigadALAQLprwkrweeildlvhfvvvprpGYplEALALPALQQL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 523533230 112 DPEIETVFLLADKQYdALSSTIIKEVAAFGGDVHRFVPAPVEA 154
Cdd:PRK00071 152 LEAAGAITLLDVPLL-AISSTAIRERIKEGRPIRYLLPEAVLD 193
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
14-67 8.49e-04

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: 37.99  E-value: 8.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 523533230    14 PFTNGHLDTLKRASRLFDEVVVAAMTNtsKKPLFSSEEKLALISESTAGLPNVK 67
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSE--DASLFSFDERFALVKKGTKDLDNVT 61
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
3-162 1.62e-86

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: 250.30  E-value: 1.62e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   3 KKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARS 82
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSF-DGLLVDFARE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  83 IGARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYAKLGD 162
Cdd:COG0669   80 VGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
5-158 1.75e-81

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: 237.36  E-value: 1.75e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARSIG 84
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGF-DGLLVDFARKHG 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523533230  85 ARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYA 158
Cdd:cd02163   80 ANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
5-160 3.48e-69

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: 206.36  E-value: 3.48e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230    5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKKPLFSSEEKLALISESTAGLPNVKAMAApKRLTVEFARSIG 84
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVF-DGLLVDYAKELG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523533230   85 ARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEVAAFGGDVHRFVPAPVEAALYAKL 160
Cdd:TIGR01510  80 ATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
7-137 1.53e-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: 100.09  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230    7 VFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTN-----TSKKPLFSSEEKLALISEStAGLPNVKaMAAPKRLTVEFAR 81
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSdepphKLKRPLFSAEERLEMLELA-KWVDEVI-VVAPWELTRELLK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 523533230   82 SIGARFMIRGIRNVADFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKEV 137
Cdd:pfam01467  79 ELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
5-65 1.16e-14

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: 64.64  E-value: 1.16e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523533230    5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVVA----AMTNTSKK-PLFSSEEKLALISESTAGLPN 65
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGvgsdQFVNPLKGePVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
5-136 2.75e-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: 58.22  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   5 IAVFPGSFDPFTNGHLDTLKRA-SRLFDEVVV----AAMTNTSKKPLFSSEEKLALISESTAGLPNV---KAMAAPKRLT 76
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEAlEEALDEVIIiivsNPPKKKRNKDPFSLHERVEMLKEILKDRLKVvpvDFPEVKILLA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523533230  77 VEFARSI----GARFMIRGiRNVAdFGYEADIATVNHDLDPEIETVFLLADKQYDALSSTIIKE 136
Cdd:cd02039   81 VVFILKIllkvGPDKVVVG-EDFA-FGKNASYNKDLKELFLDIEIVEVPRVRDGKKISSTLIRE 142
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-154 1.95e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.68  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   1 MTKKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNT-----SKKPLFSSEEKLALIsestaglpnVKAMAAPKRL 75
Cdd:PRK00071   2 MMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPgpphkPQKPLAPLEHRLAML---------ELAIADNPRF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  76 TV---EFARSiGARFMIRGIR------------------NVADF---------------------GY--EADIATVNHDL 111
Cdd:PRK00071  73 SVsdiELERP-GPSYTIDTLRelrarypdvelvfiigadALAQLprwkrweeildlvhfvvvprpGYplEALALPALQQL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 523533230 112 DPEIETVFLLADKQYdALSSTIIKEVAAFGGDVHRFVPAPVEA 154
Cdd:PRK00071 152 LEAAGAITLLDVPLL-AISSTAIRERIKEGRPIRYLLPEAVLD 193
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
1-156 2.28e-07

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 49.24  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   1 MTKKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVV----AAMTNTSKKPlFSSEEKLALISESTAGlpnvkamAAPKRLT 76
Cdd:PRK05379   4 RRYDYLVFIGRFQPFHNGHLAVIREALSRAKKVIVligsADLARSIKNP-FSFEERAQMIRAALAG-------IDLARVT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  77 VE------FARSIGARFMIRGIRNVadFGYEADIATVNHDLD---------PEIEtvFLLADkQYDALSSTIIKEvAAFG 141
Cdd:PRK05379  76 IRplrdslYNDSLWLAEVQAAVAEH--AGADARIGLIGHEKDassyylrsfPQWE--LVDVP-NTEDLSATEIRD-AYFE 149
                        170
                 ....*....|....*....
gi 523533230 142 GD----VHRFVPAPVEAAL 156
Cdd:PRK05379 150 GRissfYGWAVPAPVYAFL 168
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
3-154 7.26e-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: 47.04  E-value: 7.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   3 KKIAVFPGSFDPFTNGHLDTLKRASRLF--DEVV-VAAMTN--TSKKPLFSSEEKLALISESTAGLPNVKAmaapkrLTV 77
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLglDEVIfVPAGQPphKKHKPLASAEHRLAMLRLAIADNPRFEV------SDI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  78 EFARSiGARFMI---RGIR---------------NVADF---------------------GYEADIATVNHDLDPEiETV 118
Cdd:COG1057   76 ELERP-GPSYTIdtlRELReeypdaelyfiigadALLQLpkwkrweellelahlvvvprpGYELDELEELEALKPG-GRI 153
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 523533230 119 FLLADKQYDaLSSTIIKEVAAFGGDVHRFVPAPVEA 154
Cdd:COG1057  154 ILLDVPLLD-ISSTEIRERLAEGKSIRYLVPDAVED 188
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
2-59 1.56e-06

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: 45.57  E-value: 1.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523533230   2 TKKIAVFPGSFDPFTNGHLDTLKRASRLFDEVVV----AAMTNTSKKPlFSSEEKLALISES 59
Cdd:COG1056    1 MMKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIgigsAQESHTPRNP-FTAGERIEMIRAA 61
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
6-132 1.61e-06

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: 44.45  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   6 AVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNtskkplfsseeklalisestaglPNVKAMAAPKRLtVEFARSIGA 85
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDN-----------------------PPVKVWQDPHEL-EERKESIEE 57
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 523533230  86 RFMIRGIRNVADFGYEADiATVNHDLDPEIETVFLLA-DKQYDALSST 132
Cdd:cd02156   58 DISVCGEDFQQNRELYRW-VKDNITLPVDPEQVELPRlNLETTVMSKR 104
NMNAT_Nudix cd02168
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional proteins, also ...
5-156 3.26e-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: 45.06  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   5 IAVFPGSFDPFTNGHLDTLKRASRLFDEVVV----AAMTNTSKKPlFSSEEKLALISestAGLPNvkAMAAPKRLTVEFA 80
Cdd:cd02168    1 YLVYIGRFQPFHNGHLAVVLIALEKAKKVIIligsARTARNIKNP-WTSEEREVMIE---AALSD--AGADLARVHFRPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  81 RSI--GARFMIRGIRNV--ADFGYEADIATVNHDLD---------PEIEtvfLLADKQYDALSSTIIKEvAAF---GGDV 144
Cdd:cd02168   75 RDHlySDNLWLAEVQQQvlEIAGGSASVGLVGHRKDassyylrsfPQWD---YLEVPNYPDLNATDIRR-AYFegkEAMY 150
                        170
                 ....*....|..
gi 523533230 145 HRFVPAPVEAAL 156
Cdd:cd02168  151 RAALPAGVYDFL 162
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
5-154 3.73e-06

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: 44.93  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   5 IAVFPGSFDPFTNGHLDTLKRASRLF--DEVVVAAMTNTSKKP--LFSSEEKLALISESTAGLPNVKAMAAPKRL----- 75
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPPHKPpkPASFEHRLEMLKLAIEDNPKFEVSDIEIKRdgpsy 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230  76 ---TVEFARS----------IGA----RFM----IRGIRNVADF------GYeaDIATVNHDLDPEIETVFLLADKQYDA 128
Cdd:cd02165   81 tidTLEELRErypnaelyfiIGSdnliRLPkwydWEELLSLVHLvvaprpGY--PIEDASLEKLLLPGGRIILLDNPLLN 158
                        170       180
                 ....*....|....*....|....*.
gi 523533230 129 LSSTIIKEVAAFGGDVHRFVPAPVEA 154
Cdd:cd02165  159 ISSTEIRERLKNGKSIRYLLPPAVAD 184
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
6-72 2.15e-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: 42.28  E-value: 2.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523533230   6 AVFPGSFDPFTNGHLDTLKRASRLFDEVVV----AAMTNTSKKPlFSSEEKLALISES--TAGLPNVKAMAAP 72
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIgigsAQESHTLENP-FTAGERVLMIRRAleEEGIDLSRYYIIP 73
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
4-57 3.26e-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: 41.24  E-value: 3.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 523533230   4 KIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMT---NTSKK--PLFSSEEKLALIS 57
Cdd:COG0615    1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATdefVASKGrkPIIPEEQRKEIVE 59
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
6-59 1.03e-04

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 40.63  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 523533230   6 AVFPGSFDPFTNGHLDTLKRASRLFDEVVV----AAMTNTSKKPlFSSEEKLALISES 59
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIgigsAQESHTLKNP-FTAGERILMIRKA 59
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
3-67 2.21e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 40.31  E-value: 2.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523533230   3 KKIAVFPGSFDPFTNGHLDTLKRASRL--FDEV-VVAAMTNTSKKP--LFSSEEKLALISESTAGLPNVK 67
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKlkLDKLfFVPTYINPFKKKqkASNGEHRLNMLKLALKNLPKME 70
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
14-67 4.08e-04

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: 39.56  E-value: 4.08e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523533230  14 PFTNGHLDTLKRASRLFDEVVVAAMTNTSKkpLFSSEEKLALISESTAGLPNVK 67
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLFVVSEDKS--LFSFADRFKLVKKGTKHLKNVT 176
Citrate_ly_lig pfam08218
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ...
13-67 4.43e-04

Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 429870  Cd Length: 182  Bit Score: 38.85  E-value: 4.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 523533230   13 DPFTNGHLDTLKRASRLFDEVVVAAMTNTSKkpLFSSEEKLALISESTAGLPNVK 67
Cdd:pfam08218   9 NPFTLGHRYLVEQAAAECDWLHLFVVSEDKS--LFSYEDRFALVKKGTKHLKNVT 61
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
14-67 8.49e-04

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: 37.99  E-value: 8.49e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 523533230    14 PFTNGHLDTLKRASRLFDEVVVAAMTNtsKKPLFSSEEKLALISESTAGLPNVK 67
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSE--DASLFSFDERFALVKKGTKDLDNVT 61
cit_ly_ligase TIGR00124
[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. ...
4-66 2.49e-03

[citrate (pro-3S)-lyase] ligase; ATP is cleaved to AMP and pyrophosphate during the reaction. The carboxyl end is homologous to a number of cytidyltransferases that also release pyrophosphate. [Energy metabolism, Fermentation, Protein fate, Protein modification and repair]


Pssm-ID: 129230 [Multi-domain]  Cd Length: 332  Bit Score: 37.11  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523533230    4 KIAVFPGSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTSKkpLFSSEEKLALISESTAGLPNV 66
Cdd:TIGR00124 140 KIGSIVMNANPFTNGHRYLIEQAARQCDWLHLFVVKEDAS--LFSYDERFALVKQGIQDLSNV 200
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
10-58 7.65e-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: 34.96  E-value: 7.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523533230  10 GSFDPFTNGHLDTLKRASRLFDEVVVAAMTNTS-----KKPLFSSEEKLALISE 58
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETvakikRRPILPEEQRAEVVEA 61
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
3-59 8.62e-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: 34.77  E-value: 8.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523533230   3 KKIAVFpGSFDPFTNGHLDTLKRASRLFDEVVVAAMTN-----TSKKPLFSSEEKlALISES 59
Cdd:cd02171    2 KVVITY-GTFDLLHIGHLNLLERAKALGDKLIVAVSTDefnagKGKKAVIPYEQR-AEILES 61
 
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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