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Conserved domains on  [gi|2462557985|ref|XP_054173387|]
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bifunctional coenzyme A synthase isoform X2 [Homo sapiens]

Protein Classification

dephospho-CoA kinase( domain architecture ID 10114910)

dephospho-CoA kinase catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 193-339 9.98e-68

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: 212.91  E-value: 9.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 272
Cdd:cd02164     1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462557985 273 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 339
Cdd:cd02164    81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 360-466 8.96e-39

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


:

Pssm-ID: 238980  Cd Length: 179  Bit Score: 138.42  E-value: 8.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:cd02022     1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                          90       100
                  ....*....|....*....|....*..
gi 2462557985 440 LTDIMWPIIAKLAREEMDRAVAEDPIL 466
Cdd:cd02022    81 LEAITHPLIRKEIEEQLAEARKEKVVV 107
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 193-339 9.98e-68

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: 212.91  E-value: 9.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 272
Cdd:cd02164     1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462557985 273 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 339
Cdd:cd02164    81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 360-466 8.96e-39

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 138.42  E-value: 8.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:cd02022     1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                          90       100
                  ....*....|....*....|....*..
gi 2462557985 440 LTDIMWPIIAKLAREEMDRAVAEDPIL 466
Cdd:cd02022    81 LEAITHPLIRKEIEEQLAEARKEKVVV 107
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 359-466 3.91e-36

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 132.11  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:COG0237     2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                          90       100
                  ....*....|....*....|....*...
gi 2462557985 439 ILTDIMWPIIAKLAREEMDRAVAEDPIL 466
Cdd:COG0237    82 KLEAIVHPLVREEIERRLAAARGAPYVV 109
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 180-338 1.23e-33

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 124.68  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 180 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 259
Cdd:PLN02388    8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462557985 260 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 338
Cdd:PLN02388   88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 195-347 1.04e-30

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: 116.07  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 195 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 274
Cdd:COG1019     5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462557985 275 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 347
Cdd:COG1019    83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 360-462 3.23e-24

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 99.39  E-value: 3.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100
                  ....*....|....*....|....
gi 2462557985 439 ILTDIMWPIIaklaREEMDRAVAE 462
Cdd:TIGR00152  81 WLNALTHPLI----RQWMKKLIAQ 100
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 359-462 7.32e-22

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 92.38  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100
                  ....*....|....*....|....
gi 2462557985 439 ILTDIMWPIIAKLAREEMDRAVAE 462
Cdd:pfam01121  81 WLNGILHPLIRREIFKQIATLTAA 104
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 361-466 2.24e-21

dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 95.46  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 361 IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKIL 440
Cdd:PRK03333    4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                          90       100
                  ....*....|....*....|....*.
gi 2462557985 441 TDIMWPIIAKLAREEMDrAVAEDPIL 466
Cdd:PRK03333   84 NGIVHPLVGARRAELIA-AAPEDAVV 108
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 197-339 1.13e-09

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: 56.17  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 197 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 276
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462557985 277 GSDPSLEFLVVSEETYRGgmAINRFRLENDLEELAlyqIQLLKDLRHTENEEDKVSSSSFRQR 339
Cdd:pfam01467  77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 193-260 5.08e-05

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: 41.14  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAqEQLVVGVAdKDLLKSKLLPELLQPYTERVEHLSEFLVDIKP 260
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 193-339 9.98e-68

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: 212.91  E-value: 9.98e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 272
Cdd:cd02164     1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462557985 273 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 339
Cdd:cd02164    81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 360-466 8.96e-39

Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.


Pssm-ID: 238980  Cd Length: 179  Bit Score: 138.42  E-value: 8.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:cd02022     1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                          90       100
                  ....*....|....*....|....*..
gi 2462557985 440 LTDIMWPIIAKLAREEMDRAVAEDPIL 466
Cdd:cd02022    81 LEAITHPLIRKEIEEQLAEARKEKVVV 107
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 359-466 3.91e-36

Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440007  Cd Length: 193  Bit Score: 132.11  E-value: 3.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:COG0237     2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                          90       100
                  ....*....|....*....|....*...
gi 2462557985 439 ILTDIMWPIIAKLAREEMDRAVAEDPIL 466
Cdd:COG0237    82 KLEAIVHPLVREEIERRLAAARGAPYVV 109
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 180-338 1.23e-33

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 124.68  E-value: 1.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 180 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 259
Cdd:PLN02388    8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462557985 260 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 338
Cdd:PLN02388   88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 195-347 1.04e-30

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: 116.07  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 195 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 274
Cdd:COG1019     5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462557985 275 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 347
Cdd:COG1019    83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
191-348 6.99e-26

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 102.60  E-value: 6.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 191 YYRGAVGGTFDRLHNAHKVLLSVACILAQEqLVVGVADKDLLKSKLlPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLL 270
Cdd:PRK00777    1 MMKVAVGGTFDPLHDGHRALLRKAFELGKR-VTIGLTSDEFAKSYK-KHKVRPYEVRLKNLKKFLKAVEYDREYEIVKID 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 271 DPYGPAGSDPsLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhteneEDKVSSSSFRQR-----MLGNLL 345
Cdd:PRK00777   79 DPYGPALEDD-FDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLA-------EDGKPISSTRIRrgeidEHGNLI 150


                  ...
gi 2462557985 346 RPP 348
Cdd:PRK00777  151 KER 153
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 360-462 3.23e-24

dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, guanylate, uridine, and thymidylate kinases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272931  Cd Length: 190  Bit Score: 99.39  E-value: 3.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100
                  ....*....|....*....|....
gi 2462557985 439 ILTDIMWPIIaklaREEMDRAVAE 462
Cdd:TIGR00152  81 WLNALTHPLI----RQWMKKLIAQ 100
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 359-462 7.32e-22

Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form Coenzyme A EC:2.7.1.24. This enzyme uses ATP in its reaction.


Pssm-ID: 426062  Cd Length: 180  Bit Score: 92.38  E-value: 7.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100
                  ....*....|....*....|....
gi 2462557985 439 ILTDIMWPIIAKLAREEMDRAVAE 462
Cdd:pfam01121  81 WLNGILHPLIRREIFKQIATLTAA 104
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 361-466 2.24e-21

dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 95.46  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 361 IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKIL 440
Cdd:PRK03333    4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                          90       100
                  ....*....|....*....|....*.
gi 2462557985 441 TDIMWPIIAKLAREEMDrAVAEDPIL 466
Cdd:PRK03333   84 NGIVHPLVGARRAELIA-AAPEDAVV 108
coaE PRK14734
dephospho-CoA kinase; Provisional
 358-462 5.71e-21

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 90.67  E-value: 5.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 358 LYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQL 437
Cdd:PRK14734    1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                          90       100
                  ....*....|....*....|....*
gi 2462557985 438 KILTDIMWPIIAKLAREEMDRAVAE 462
Cdd:PRK14734   81 ALLNAITHPRIAEETARRFNEARAQ 105
PLN02422 PLN02422
dephospho-CoA kinase
 360-454 1.46e-14

dephospho-CoA kinase


Pssm-ID: 215232  Cd Length: 232  Bit Score: 72.86  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:PLN02422    3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82

                          90
                  ....*....|....*.
gi 2462557985 440 LTDIMWPIIAK-LARE 454
Cdd:PLN02422   83 LNRLLAPYISSgIFWE 98
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
196-315 7.00e-13

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 69.46  E-value: 7.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 196 VGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPellQPYTERVEHLSEFLvdIKPSLTFDVIPLLDPYGP 275
Cdd:PRK01170    5 VGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYP---IPYEDRKRKLENFI--KKFTNKFRIRPIDDRYGN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462557985 276 AGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQI 315
Cdd:PRK01170   80 TLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRV 119
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 197-339 1.13e-09

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: 56.17  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 197 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 276
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462557985 277 GSDPSLEFLVVSEETYRGgmAINRFRLENDLEELAlyqIQLLKDLRHTENEEDKVSSSSFRQR 339
Cdd:pfam01467  77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 193-339 6.50e-07

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: 48.59  E-value: 6.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVadKDLLKSKLLPELLQPYTERVEHLSEFLVD-----------IKPS 261
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIII--VSNPPKKKRNKDPFSLHERVEMLKEILKDrlkvvpvdfpeVKIL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 262 LTFD-VIPLLDPYGPagsdpslEFLVVSEETYRGGMAINRFRL---ENDLEELALYQIqllkdlrhteNEEDKVSSSSFR 337
Cdd:cd02039    79 LAVVfILKILLKVGP-------DKVVVGEDFAFGKNASYNKDLkelFLDIEIVEVPRV----------RDGKKISSTLIR 141


                  ..
gi 2462557985 338 QR 339
Cdd:cd02039   142 EL 143
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 193-260 5.08e-05

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: 41.14  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462557985 193 RGAVGGTFDRLHNAHKVLLSVACILAqEQLVVGVAdKDLLKSKLLPELLQPYTERVEHLSEFLVDIKP 260
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
358-409 4.59e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 40.67  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462557985 358 LYVIGltGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRAYAPGGPAYQPVVEA 409
Cdd:COG0645     1 LILVC--GLPGSGKSTLARALaERLGAVRLRSDVVRKRLFGAGLAPLERSPEA 51
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 360-389 8.34e-04

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 40.46  E-value: 8.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462557985 360 VIGLTGISGSGKSSIA----QRLKGLG--AFVIDSD 389
Cdd:COG0529    18 VVWFTGLSGSGKSTLAnaleRRLFERGrhVYLLDGD 53
aroK PRK00131
shikimate kinase; Reviewed
 363-391 1.05e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.79  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462557985 363 LTGISGSGKSSIAQRL-KGLGAFVIDSDHL 391
Cdd:PRK00131    9 LIGFMGAGKSTIGRLLaKRLGYDFIDTDHL 38
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 360-393 1.62e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 41.07  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIA----QRLKGLG--AFVIDSDHLGH 393
Cdd:PRK05506  462 TVWFTGLSGSGKSTIAnlveRRLHALGrhTYLLDGDNVRH 501
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 361-391 2.94e-03

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 38.31  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462557985 361 IGLTGISGSGKSSIAQRL-KGLGAFVIDSDHL 391
Cdd:cd00464     2 IVLIGMMGAGKTTVGRLLaKALGLPFVDLDEL 33
PTZ00451 PTZ00451
dephospho-CoA kinase; Provisional
 360-450 3.40e-03

dephospho-CoA kinase; Provisional


Pssm-ID: 185630  Cd Length: 244  Bit Score: 39.09  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRLK-GLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:PTZ00451    3 LIGLTGGIACGKSTVSRILReEHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQARR 82

                          90
                  ....*....|..
gi 2462557985 439 ILTDIMWPIIAK 450
Cdd:PTZ00451   83 ALGRIMNPPIFR 94
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 360-393 3.82e-03

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 37.84  E-value: 3.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 393
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALeeklfqRGRPVYVLDGDNVRH 40
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 358-395 4.60e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 37.62  E-value: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462557985 358 LYVIglTGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRA 395
Cdd:cd02021     1 IIVV--MGVSGSGKSTVGKALaERLGAPFIDGDDLHPPA 37
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 360-393 4.77e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 37.68  E-value: 4.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462557985 360 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 393
Cdd:pfam01583   4 TIWLTGLSGAGKSTIANALerklfeQGRSVYVLDGDNVRH 43
 
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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