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Conserved domains on  [gi|489713365|ref|WP_003617502|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [Lactobacillus]

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 ...
 1-162 1.87e-78

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: 229.89  E-value: 1.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLA 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALAD--LPNVEVDSFDG-LLVDFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365  81 KELGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKEKL 160
Cdd:COG0669   78 REVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157


                 ..
gi 489713365 161 QS 162
Cdd:COG0669  158 AK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-162 1.87e-78

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: 229.89  E-value: 1.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLA 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALAD--LPNVEVDSFDG-LLVDFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365  81 KELGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKEKL 160
Cdd:COG0669   78 REVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157


                 ..
gi 489713365 161 QS 162
Cdd:COG0669  158 AK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-158 3.28e-74

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: 218.87  E-value: 3.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   3 TALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLAKE 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKH--LPNVEVDGFDG-LLVDFARK 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489713365  83 LGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKE 158
Cdd:cd02163   78 HGANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-160 3.44e-62

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: 188.64  E-value: 3.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365    3 TALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLAKE 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKH--LPNVRVDVFDG-LLVDYAKE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   83 LGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKEKL 160
Cdd:TIGR01510  78 LGATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-137 4.72e-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: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365    5 LFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSS-----KKALFTPDERVDLIKDAVkehGLANVeILARPGQLTVDL 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEpphklKRPLFSAEERLEMLELAK---WVDEV-IVVAPWELTREL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   80 AKELGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEI 137
Cdd:pfam01467  77 LKELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-87 1.91e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.68  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNS-----SKKALFTPDERVDLIKDAVKEHGLANVE--ILARPG 73
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPgpphkPQKPLAPLEHRLAMLELAIADNPRFSVSdiELERPG 83

                         90
                 ....*....|....*...
gi 489713365  74 -QLTVD---LAKELGAGV 87
Cdd:PRK00071  84 pSYTIDtlrELRARYPDV 101
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-69 1.05e-05

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: 43.39  E-value: 1.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 489713365    12 PITNGHMDTIEQAAKVFDRL-LVVVMTNSSkkaLFTPDERVDLIKDAVKEhgLANVEIL 69
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVhLFVVSEDAS---LFSFDERFALVKKGTKD--LDNVTVH 63
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 1-162 1.87e-78

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: 229.89  E-value: 1.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLA 80
Cdd:COG0669    1 MRIAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALAD--LPNVEVDSFDG-LLVDFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365  81 KELGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKEKL 160
Cdd:COG0669   78 REVGANVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKF 157


                 ..
gi 489713365 161 QS 162
Cdd:COG0669  158 AK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 3-158 3.28e-74

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: 218.87  E-value: 3.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   3 TALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLAKE 82
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKH--LPNVEVDGFDG-LLVDFARK 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489713365  83 LGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKE 158
Cdd:cd02163   78 HGANVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 3-160 3.44e-62

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: 188.64  E-value: 3.44e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365    3 TALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKKALFTPDERVDLIKDAVKEhgLANVEILARPGqLTVDLAKE 82
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKH--LPNVRVDVFDG-LLVDYAKE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   83 LGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEIAMFGGELDRFLPKKAARALKEKL 160
Cdd:TIGR01510  78 LGATFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-137 4.72e-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: 4.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365    5 LFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSS-----KKALFTPDERVDLIKDAVkehGLANVeILARPGQLTVDL 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEpphklKRPLFSAEERLEMLELAK---WVDEV-IVVAPWELTREL 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   80 AKELGAGVLVRGVRNSSDFLYEQQIAQLNRDLAPDLPTVLFMAEAANSALASSMLKEI 137
Cdd:pfam01467  77 LKELNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-59 5.64e-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: 63.09  E-value: 5.64e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489713365    4 ALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVM----TNSSKKALFTP-DERVDLIKDAVK 59
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVGVGsdqfVNPLKGEPVFSlEERLEMLKALKY 62
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 3-83 6.10e-10

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


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 55.33  E-value: 6.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   3 TALFPGSFDPITNGHMDTIEQAAKVF--DRLLVVVMTNSSKKA--LFTPDERVDLIKDAVKehGLANVEI----LARPGQ 74
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPPHKPpkPASFEHRLEMLKLAIE--DNPKFEVsdieIKRDGP 78

                         90
                 ....*....|
gi 489713365  75 L-TVDLAKEL 83
Cdd:cd02165   79 SyTIDTLEEL 88
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-59 3.31e-08

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: 49.75  E-value: 3.31e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489713365   4 ALFPGSFDPITNGHMDTIEQA-AKVFDRLLVVVMTNS----SKKALFTPDERVDLIKDAVK 59
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEAlEEALDEVIIIIVSNPpkkkRNKDPFSLHERVEMLKEILK 62
NMNAT_Archaea cd02166
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ...
 4-72 4.05e-08

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: 49.99  E-value: 4.05e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489713365   4 ALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVmtNSSKKAL-----FTPDERVDLIKDAVKEHGLANVEILARP 72
Cdd:cd02166    2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGI--GSAQESHtlenpFTAGERVLMIRRALEEEGIDLSRYYIIP 73
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-83 1.88e-07

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


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 48.58  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVF--DRLLVVVmTNSS---KKALFTPDE-RVDLIKDAVKEH---GLANVEIlAR 71
Cdd:COG1057    2 MRIGIFGGTFDPIHIGHLALAEEAAEQLglDEVIFVP-AGQPphkKHKPLASAEhRLAMLRLAIADNprfEVSDIEL-ER 79

                         90
                 ....*....|...
gi 489713365  72 PGQ-LTVDLAKEL 83
Cdd:COG1057   80 PGPsYTIDTLREL 92
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-87 1.91e-07

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 48.68  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNS-----SKKALFTPDERVDLIKDAVKEHGLANVE--ILARPG 73
Cdd:PRK00071   4 KRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPgpphkPQKPLAPLEHRLAMLELAIADNPRFSVSdiELERPG 83

                         90
                 ....*....|....*...
gi 489713365  74 -QLTVD---LAKELGAGV 87
Cdd:PRK00071  84 pSYTIDtlrELRARYPDV 101
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 3-58 4.22e-07

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: 45.99  E-value: 4.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489713365   3 TALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSSKK---ALFTPDERVDLIKDAV 58
Cdd:cd02156    1 KARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKvwqDPHELEERKESIEEDI 59
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 12-70 4.20e-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: 45.33  E-value: 4.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365  12 PITNGHMDTIEQAAKVFDRLLV-VVMTNSSkkaLFTPDERVDLIKDAVKEhgLANVEILA 70
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLfVVSEDKS---LFSFADRFKLVKKGTKH--LKNVTVHS 179
PRK01153 PRK01153
nicotinamide-nucleotide adenylyltransferase; Provisional
 4-63 7.62e-06

nicotinamide-nucleotide adenylyltransferase; Provisional


Pssm-ID: 179235  Cd Length: 174  Bit Score: 43.71  E-value: 7.62e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489713365   4 ALFPGSFDPITNGHMDTIEQAAKVFDRLLVVVMT---NSSKKALFTPDERVDLIKDAVKEHGL 63
Cdd:PRK01153   3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIGSaqeSHTLKNPFTAGERILMIRKALEEEGI 65
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 12-69 1.05e-05

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: 43.39  E-value: 1.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 489713365    12 PITNGHMDTIEQAAKVFDRL-LVVVMTNSSkkaLFTPDERVDLIKDAVKEhgLANVEIL 69
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVhLFVVSEDAS---LFSFDERFALVKKGTKD--LDNVTVH 63
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 5-83 1.51e-05

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: 43.08  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365    5 LFPGSFDPITNGHMDTIEQAAKVF--DRLLVVVMTNSSKKALFTP---DERVDLIKDAVKEHGLANVE--ILARPGQL-T 76
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLdlDKVIFVPTANPPHKKTYEAassHHRLAMLKLAIEDNPKFEVDdfEIKRGGPSyT 80


                  ....*..
gi 489713365   77 VDLAKEL 83
Cdd:TIGR00482  81 IDTLKHL 87
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 8-55 1.15e-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: 39.97  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489713365   8 GSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSS-----KKALFTPDERVDLIK 55
Cdd:cd02170    8 GTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETvakikRRPILPEEQRAEVVE 60
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-68 1.78e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 40.70  E-value: 1.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKV--FDRLLVVVMTNS---SKKALFTPDERVDLIKDAVKEhgLANVEI 68
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKlkLDKLFFVPTYINpfkKKQKASNGEHRLNMLKLALKN--LPKMEV 71
Citrate_ly_lig pfam08218
Citrate lyase ligase C-terminal domain; This family is composed of the C-terminal domain of ...
 11-68 1.91e-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: 40.01  E-value: 1.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489713365   11 DPITNGHMDTIEQAAKVFDRL-LVVVMTNSSkkaLFTPDERVDLIKDAVKehGLANVEI 68
Cdd:pfam08218   9 NPFTLGHRYLVEQAAAECDWLhLFVVSEDKS---LFSYEDRFALVKKGTK--HLKNVTV 62
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
4-68 3.94e-04

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 39.61  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   4 ALFPGSFDPITNGHMDTIEQAAKVFDRLLVVV---MTNSSKKALFTPDERVDLIKDAVKEHGLANVEI 68
Cdd:PRK05379   9 LVFIGRFQPFHNGHLAVIREALSRAKKVIVLIgsaDLARSIKNPFSFEERAQMIRAALAGIDLARVTI 76
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 7-63 3.51e-03

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


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 35.85  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489713365   7 PGSFDPITNGHMDTIEQAAKVFDRLLVVVMTNSS-----KKALFTPDERVDLIK------DAVKEHGL 63
Cdd:COG0615    6 YGTFDLLHPGHINLLKRAKALGDELIVGVATDEFvaskgRKPIIPEEQRKEIVEalkyvdEVILGEEW 73
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
1-74 4.00e-03

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 36.24  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489713365   1 MTTALFPGSFDPITNGHMDTIEQAAKvFDR-LLVVVMTNSSKKALFTPDERVDLIKDAVKEHGLANVEI------LARPG 73
Cdd:PRK08887   2 KKIAVFGSAFNPPSLGHKSVIESLSH-FDLvLLVPSIAHAWGKTMLDYETRCQLVDAFIQDLGLSNVQRsdieqeLYAPD 80


                 .
gi 489713365  74 Q 74
Cdd:PRK08887  81 E 81
 
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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