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Conserved domains on  [gi|15224138|ref|NP_179417|]
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4-phosphopantetheine adenylyltransferase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 1-173 7.72e-117

phosphopantetheine adenylyltransferase


:

Pssm-ID: 215218  Cd Length: 177  Bit Score: 328.06  E-value: 7.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138    1 MAAPEDSKMSPANSFGAVVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVK 80
Cdd:PLN02388   5 KDSVADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138   81 SIKPELVVQAEPITDPYGPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKME 160
Cdd:PLN02388  85 SIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPEESTGNKLSSTTLRRLE 164

                        170
                 ....*....|...
gi 15224138  161 AEKASKQKQPAEE 173
Cdd:PLN02388 165 AEKAVKQKQPAEE 177
 
Name Accession Description Interval E-value
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 1-173 7.72e-117

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 328.06  E-value: 7.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138    1 MAAPEDSKMSPANSFGAVVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVK 80
Cdd:PLN02388   5 KDSVADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138   81 SIKPELVVQAEPITDPYGPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKME 160
Cdd:PLN02388  85 SIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPEESTGNKLSSTTLRRLE 164

                        170
                 ....*....|...
gi 15224138  161 AEKASKQKQPAEE 173
Cdd:PLN02388 165 AEKAVKQKQPAEE 177
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 18-159 9.38e-74

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 217.92  E-value: 9.38e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:cd02164   2 VAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224138  98 GPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKM 159
Cdd:cd02164  82 GPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKADEDGEKISSTRIRRG 143
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 18-160 1.16e-41

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


Pssm-ID: 440642  Cd Length: 154  Bit Score: 136.87  E-value: 1.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELARDrIVVGVCDGPMLTKKQfSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:COG1019   4 VAVGGTFDPLHDGHRALLERAFELGGD-VIIGLTSDELAKKTK-KRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224138  98 GPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVsDGSSGNKISSSTLRKME 160
Cdd:COG1019  82 GPALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHV-LAEDGKPISSTRIRNGE 143
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 19-158 6.77e-10

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: 54.25  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138    19 VLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMltKKQFSDMIQPIEERMRNVEtyvkSIKPELVVQAEPITDPYG 98
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEP--PHKLKRPLFSAEERLEMLE----LAKWVDEVIVVAPWELTR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224138    99 PSIVDENLEAIVVSKETLPGglSVNRKRAERGLSQLKIEVVEIVSDGS-SGNKISSSTLRK 158
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLLD--FWYELDEILGNVKLVVVVRPVFFIPLkPTNGISSTDIRE 133
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 18-84 9.48e-09

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: 49.61  E-value: 9.48e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224138    18 VVLGGTFDRLHDGHRMFLKAAAELArDRIVVGVCdGPMLTKKQFSDMIQPIEERMRNVETYVKSIKP 84
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 1-173 7.72e-117

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 328.06  E-value: 7.72e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138    1 MAAPEDSKMSPANSFGAVVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVK 80
Cdd:PLN02388   5 KDSVADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138   81 SIKPELVVQAEPITDPYGPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKME 160
Cdd:PLN02388  85 SIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPEESTGNKLSSTTLRRLE 164

                        170
                 ....*....|...
gi 15224138  161 AEKASKQKQPAEE 173
Cdd:PLN02388 165 AEKAVKQKQPAEE 177
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 18-159 9.38e-74

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 217.92  E-value: 9.38e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:cd02164   2 VAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224138  98 GPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSSGNKISSSTLRKM 159
Cdd:cd02164  82 GPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKADEDGEKISSTRIRRG 143
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
18-160 1.02e-42

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 139.58  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138   18 VVLGGTFDRLHDGHRMFLKAAAELArDRIVVGVCDGPMLTKKQfSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:PRK00777   4 VAVGGTFDPLHDGHRALLRKAFELG-KRVTIGLTSDEFAKSYK-KHKVRPYEVRLKNLKKFLKAVEYDREYEIVKIDDPY 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224138   98 GPSIvDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGsSGNKISSSTLRKME 160
Cdd:PRK00777  82 GPAL-EDDFDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLAE-DGKPISSTRIRRGE 142
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 18-160 1.16e-41

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


Pssm-ID: 440642  Cd Length: 154  Bit Score: 136.87  E-value: 1.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELARDrIVVGVCDGPMLTKKQfSDMIQPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:COG1019   4 VAVGGTFDPLHDGHRALLERAFELGGD-VIIGLTSDELAKKTK-KRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224138  98 GPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVsDGSSGNKISSSTLRKME 160
Cdd:COG1019  82 GPALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHV-LAEDGKPISSTRIRNGE 143
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
18-170 2.67e-22

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 91.03  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138   18 VVLGGTFDRLHDGHRMFLKAAAELArDRIVVGVCDGPmLTKKQFSDMIqPIEERMRNVETYVKSIKPELVVQaePITDPY 97
Cdd:PRK01170   3 TVVGGTFSKLHKGHKALLKKAIETG-DEVVIGLTSDE-YVRKNKVYPI-PYEDRKRKLENFIKKFTNKFRIR--PIDDRY 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15224138   98 GPSIVDENLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSdGSSGNKISSSTLRKMEAEKASKQKQP 170
Cdd:PRK01170  78 GNTLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRVPYVL-AEDLFPISSTRIINGEIDGNGKRLKP 149
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 18-159 3.06e-15

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: 68.62  E-value: 3.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMLTKKQFSDMiqPIEERMRNVETYVKSIKPELVVQAEPITDPY 97
Cdd:cd02039   2 GIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKKRNKDPF--SLHERVEMLKEILKDRLKVVPVDFPEVKILL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224138  98 GPSIVDE-----NLEAIVVSKETLPGGLSVNRKRAERGLSQLKIEVVEIVSDGSsgnKISSSTLRKM 159
Cdd:cd02039  80 AVVFILKillkvGPDKVVVGEDFAFGKNASYNKDLKELFLDIEIVEVPRVRDGK---KISSTLIREL 143
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 19-158 6.77e-10

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: 54.25  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224138    19 VLGGTFDRLHDGHRMFLKAAAELARDRIVVGVCDGPMltKKQFSDMIQPIEERMRNVEtyvkSIKPELVVQAEPITDPYG 98
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEP--PHKLKRPLFSAEERLEMLE----LAKWVDEVIVVAPWELTR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224138    99 PSIVDENLEAIVVSKETLPGglSVNRKRAERGLSQLKIEVVEIVSDGS-SGNKISSSTLRK 158
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLLD--FWYELDEILGNVKLVVVVRPVFFIPLkPTNGISSTDIRE 133
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 18-84 9.48e-09

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: 49.61  E-value: 9.48e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224138    18 VVLGGTFDRLHDGHRMFLKAAAELArDRIVVGVCdGPMLTKKQFSDMIQPIEERMRNVETYVKSIKP 84
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 18-92 1.49e-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: 1.49e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224138  18 VVLGGTFDRLHDGHRMFLKAAAELArDRIVVGVCDGPMLTKKQfSDMIQPIEERMRNVEtyvkSIKP--ELVVQAEP 92
Cdd:cd02170   4 VYAAGTFDIIHPGHIRFLEEAKKLG-DYLIVGVARDETVAKIK-RRPILPEEQRAEVVE----ALKYvdEVILGHPW 74
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
19-88 7.47e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 38.66  E-value: 7.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15224138   19 VLGGTFDRLHDGHRMFLKAAAE-LARDRIVVGVCDGPMLtkKQFSDMIqPIEERMRNVETYVKSIkPELVV 88
Cdd:PRK00071   8 LFGGTFDPPHYGHLAIAEEAAErLGLDEVWFLPNPGPPH--KPQKPLA-PLEHRLAMLELAIADN-PRFSV 74
 
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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