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Conserved domains on  [gi|205277394|ref|NP_001035997|]
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bifunctional coenzyme A synthase isoform c [Homo sapiens]

Protein Classification

PPAT_CoAS and DPCK domain-containing protein( domain architecture ID 10114910)

PPAT_CoAS and DPCK domain-containing protein

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; ...
 222-368 4.64e-67

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: 214.45  E-value: 4.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 222 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 301
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277394 302 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 368
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 389-565 1.15e-63

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: 206.99  E-value: 1.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 468
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 469 LTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQM 548
Cdd:cd02022   81 LEAITHPLIRKEIEEQLAE--ARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 205277394 549 SGQQLVEQSHVVLSTLW 565
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 222-368 4.64e-67

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: 214.45  E-value: 4.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 222 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 301
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277394 302 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 368
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 389-565 1.15e-63

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: 206.99  E-value: 1.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 468
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 469 LTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQM 548
Cdd:cd02022   81 LEAITHPLIRKEIEEQLAE--ARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 205277394 549 SGQQLVEQSHVVLSTLW 565
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 388-581 1.31e-62

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: 204.53  E-value: 1.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 388 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 468 ILTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 547
Cdd:COG0237   82 KLEAIVHPLVREEIERRLAA--ARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 205277394 548 MSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALL 581
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 388-561 3.97e-39

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: 141.69  E-value: 3.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  388 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  468 ILTDIMWPIIAKLAREEMdrAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 547
Cdd:pfam01121  81 WLNGILHPLIRREIFKQI--ATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 205277394  548 MSGQQLVEQSHVVL 561
Cdd:pfam01121 159 ASREERLALADDVL 172
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 389-561 7.16e-34

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: 127.51  E-value: 7.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  389 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  468 ILTDIMWPIIaklaREEMDRAVAE---GKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRL 544
Cdd:TIGR00152  81 WLNALTHPLI----RQWMKKLIAQfqsKYALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRL 156

                         170
                  ....*....|....*..
gi 205277394  545 QSQMSGQQLVEQSHVVL 561
Cdd:TIGR00152 157 ASQMDIEEKLARIDTVI 173
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 209-367 5.02e-33

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 124.68  E-value: 5.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 209 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 288
Cdd:PLN02388   8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277394 289 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 367
Cdd:PLN02388  88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
coaE PRK14734
dephospho-CoA kinase; Provisional
 387-585 1.06e-32

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 124.57  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 387 LYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQL 466
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 467 KILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQS 546
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 205277394 547 QMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRI 585
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 224-376 1.20e-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: 117.22  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 224 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 303
Cdd:COG1019    5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277394 304 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 376
Cdd:COG1019   83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 226-368 1.16e-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: 56.56  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  226 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 305
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277394  306 GSDPSLEFLVVSEETYRGgmAINRFRLENDLEELAlyqIQLLKDLRHTENEEDKVSSSSFRQR 368
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 ...
 222-289 5.06e-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: 41.52  E-value: 5.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277394  222 RGAVGGTFDRLHNAHKVLLSVACILAqEQLVVGVAdKDLLKSKLLPELLQPYTERVEHLSEFLVDIKP 289
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; ...
 222-368 4.64e-67

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: 214.45  E-value: 4.64e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 222 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 301
Cdd:cd02164    1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277394 302 YGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQR 368
Cdd:cd02164   81 YGPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVKA----DEDGEKISSTRIRRG 143
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 389-565 1.15e-63

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: 206.99  E-value: 1.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 468
Cdd:cd02022    1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 469 LTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQM 548
Cdd:cd02022   81 LEAITHPLIRKEIEEQLAE--ARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158

                        170
                 ....*....|....*..
gi 205277394 549 SGQQLVEQSHVVLSTLW 565
Cdd:cd02022  159 PLEEKRARADFVIDNSG 175
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 388-581 1.31e-62

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: 204.53  E-value: 1.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 388 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:COG0237    2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 468 ILTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 547
Cdd:COG0237   82 KLEAIVHPLVREEIERRLAA--ARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159

                        170       180       190
                 ....*....|....*....|....*....|....
gi 205277394 548 MSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALL 581
Cdd:COG0237  160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 388-561 3.97e-39

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: 141.69  E-value: 3.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  388 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  468 ILTDIMWPIIAKLAREEMdrAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 547
Cdd:pfam01121  81 WLNGILHPLIRREIFKQI--ATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158

                         170
                  ....*....|....
gi 205277394  548 MSGQQLVEQSHVVL 561
Cdd:pfam01121 159 ASREERLALADDVL 172
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 389-561 7.16e-34

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: 127.51  E-value: 7.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  389 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  468 ILTDIMWPIIaklaREEMDRAVAE---GKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRL 544
Cdd:TIGR00152  81 WLNALTHPLI----RQWMKKLIAQfqsKYALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRL 156

                         170
                  ....*....|....*..
gi 205277394  545 QSQMSGQQLVEQSHVVL 561
Cdd:TIGR00152 157 ASQMDIEEKLARIDTVI 173
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 209-367 5.02e-33

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 124.68  E-value: 5.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 209 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 288
Cdd:PLN02388   8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277394 289 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 367
Cdd:PLN02388  88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
coaE PRK14734
dephospho-CoA kinase; Provisional
 387-585 1.06e-32

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 124.57  E-value: 1.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 387 LYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQL 466
Cdd:PRK14734   1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 467 KILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQS 546
Cdd:PRK14734  81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 205277394 547 QMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRI 585
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 224-376 1.20e-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: 117.22  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 224 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 303
Cdd:COG1019    5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277394 304 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 376
Cdd:COG1019   83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 390-579 3.07e-30

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


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 122.81  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 390 IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKIL 469
Cdd:PRK03333   4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 470 TDIMWPIIAKLAREEMDRAVAEGkrVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMS 549
Cdd:PRK03333  84 NGIVHPLVGARRAELIAAAPEDA--VVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRRLVEQRGMAEADARARIAAQAS 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 205277394 550 GQQLVEQSHVVLSTLWEPHITQRQVEKAWA 579
Cdd:PRK03333 162 DEQRRAVADVWLDNSGTPDELVEAVRALWA 191
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
220-377 4.38e-26

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 104.14  E-value: 4.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 220 YYRGAVGGTFDRLHNAHKVLLSVACILAQEqLVVGVADKDLLKSKLlPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLL 299
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFELGKR-VTIGLTSDEFAKSYK-KHKVRPYEVRLKNLKKFLKAVEYDREYEIVKID 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 300 DPYGPAGSDPsLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhteneEDKVSSSSFRQR-----MLGNLL 374
Cdd:PRK00777  79 DPYGPALEDD-FDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLA-------EDGKPISSTRIRrgeidEHGNLI 150


                 ...
gi 205277394 375 RPP 377
Cdd:PRK00777 151 KER 153
PLN02422 PLN02422
dephospho-CoA kinase
 389-549 6.25e-26

dephospho-CoA kinase


Pssm-ID: 215232  Cd Length: 232  Bit Score: 106.37  E-value: 6.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 468
Cdd:PLN02422   3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 469 LTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAG---WQNLVHEVWtaVIPETEaVRRIVERDGLSEAAAQSRLQ 545
Cdd:PLN02422  83 LNRLLAPYISSGIFWEILKLWLKGCKVIVLDIPLLFETKmdkWTKPVVVVW--VDPETQ-LERLMARDGLSEEQARNRIN 159


                 ....
gi 205277394 546 SQMS 549
Cdd:PLN02422 160 AQMP 163
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
225-344 1.05e-12

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 69.46  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 225 VGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPellQPYTERVEHLSEFLvdIKPSLTFDVIPLLDPYGP 304
Cdd:PRK01170   5 VGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYP---IPYEDRKRKLENFI--KKFTNKFRIRPIDDRYGN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 205277394 305 AGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQI 344
Cdd:PRK01170  80 TLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRV 119
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 226-368 1.16e-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: 56.56  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394  226 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 305
Cdd:pfam01467   3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277394  306 GSDPSLEFLVVSEETYRGgmAINRFRLENDLEELAlyqIQLLKDLRHTENEEDKVSSSSFRQR 368
Cdd:pfam01467  77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
PTZ00451 PTZ00451
dephospho-CoA kinase; Provisional
 389-549 3.83e-09

dephospho-CoA kinase; Provisional


Pssm-ID: 185630  Cd Length: 244  Bit Score: 57.58  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRLK-GLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 467
Cdd:PTZ00451   3 LIGLTGGIACGKSTVSRILReEHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 468 ILTDIMWPII--------AKLAREEMDRAVA-EGKRVCVIDAAVLLEAG-WQNLVHEVWTAVIPETEAVRRIVERDGLSE 537
Cdd:PTZ00451  83 ALGRIMNPPIfrailkriAAAWWEDLWRSGAgSSPLIVVLDAPTLFETKtFTYFVSASVVVSCSEERQIERLRKRNGFSK 162

                        170
                 ....*....|..
gi 205277394 538 AAAQSRLQSQMS 549
Cdd:PTZ00451 163 EEALQRIGSQMP 174
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 222-368 8.63e-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: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 222 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVadKDLLKSKLLPELLQPYTERVEHLSEFLVD-----------IKPS 290
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIII--VSNPPKKKRNKDPFSLHERVEMLKEILKDrlkvvpvdfpeVKIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277394 291 LTFD-VIPLLDPYGPagsdpslEFLVVSEETYRGGMAINRFRL---ENDLEELALYQIqllkdlrhteNEEDKVSSSSFR 366
Cdd:cd02039   79 LAVVfILKILLKVGP-------DKVVVGEDFAFGKNASYNKDLkelFLDIEIVEVPRV----------RDGKKISSTLIR 141


                 ..
gi 205277394 367 QR 368
Cdd:cd02039  142 EL 143
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 222-289 5.06e-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: 41.52  E-value: 5.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277394  222 RGAVGGTFDRLHNAHKVLLSVACILAqEQLVVGVAdKDLLKSKLLPELLQPYTERVEHLSEFLVDIKP 289
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 389-418 1.13e-03

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: 1.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 205277394 389 VIGLTGISGSGKSSIA----QRLKGLG--AFVIDSD 418
Cdd:COG0529   18 VVWFTGLSGSGKSTLAnaleRRLFERGrhVYLLDGD 53
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
387-438 1.15e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.90  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 205277394 387 LYVIGltGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRAYAPGGPAYQPVVEA 438
Cdd:COG0645    1 LILVC--GLPGSGKSTLARALaERLGAVRLRSDVVRKRLFGAGLAPLERSPEA 51
aroK PRK00131
shikimate kinase; Reviewed
 392-420 1.41e-03

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 39.79  E-value: 1.41e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 205277394 392 LTGISGSGKSSIAQRL-KGLGAFVIDSDHL 420
Cdd:PRK00131   9 LIGFMGAGKSTIGRLLaKRLGYDFIDTDHL 38
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 389-422 2.50e-03

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 40.68  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIA----QRLKGLG--AFVIDSDHLGH 422
Cdd:PRK05506 462 TVWFTGLSGSGKSTIAnlveRRLHALGrhTYLLDGDNVRH 501
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 390-420 3.73e-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: 3.73e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 205277394 390 IGLTGISGSGKSSIAQRL-KGLGAFVIDSDHL 420
Cdd:cd00464    2 IVLIGMMGAGKTTVGRLLaKALGLPFVDLDEL 33
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 389-422 4.52e-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: 4.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 205277394 389 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 422
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALeeklfqRGRPVYVLDGDNVRH 40
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 389-422 6.34e-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: 6.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 205277394  389 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 422
Cdd:pfam01583   4 TIWLTGLSGAGKSTIANALerklfeQGRSVYVLDGDNVRH 43
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 387-424 7.88e-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: 37.23  E-value: 7.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 205277394 387 LYVIglTGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRA 424
Cdd:cd02021    1 IIVV--MGVSGSGKSTVGKALaERLGAPFIDGDDLHPPA 37
 
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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