|
Name |
Accession |
Description |
Interval |
E-value |
| PPAT_CoAS |
cd02164 |
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ... |
193-339 |
3.05e-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: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 272
Cdd:cd02164 1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996043 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 ... |
360-536 |
1.69e-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: 205.83 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:cd02022 1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 440 LTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQM 519
Cdd:cd02022 81 LEAITHPLIRKEIEEQLAE--ARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158
|
170
....*....|....*..
gi 767996043 520 SGQQLVEQSHVVLSTLW 536
Cdd:cd02022 159 PLEEKRARADFVIDNSG 175
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
359-552 |
1.13e-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: 204.15 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:COG0237 2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 518
Cdd:COG0237 82 KLEAIVHPLVREEIERRLAA--ARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159
|
170 180 190
....*....|....*....|....*....|....
gi 767996043 519 MSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALL 552
Cdd:COG0237 160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
|
|
| CoaE |
pfam01121 |
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ... |
359-532 |
3.29e-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: 141.31 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:pfam01121 1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIAKLAREEMdrAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 518
Cdd:pfam01121 81 WLNGILHPLIRREIFKQI--ATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158
|
170
....*....|....
gi 767996043 519 MSGQQLVEQSHVVL 532
Cdd:pfam01121 159 ASREERLALADDVL 172
|
|
| TIGR00152 |
TIGR00152 |
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ... |
360-532 |
1.49e-33 |
|
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: 126.35 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:TIGR00152 1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIaklaREEMDRAVAE---GKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRL 515
Cdd:TIGR00152 81 WLNALTHPLI----RQWMKKLIAQfqsKYALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRL 156
|
170
....*....|....*..
gi 767996043 516 QSQMSGQQLVEQSHVVL 532
Cdd:TIGR00152 157 ASQMDIEEKLARIDTVI 173
|
|
| PLN02388 |
PLN02388 |
phosphopantetheine adenylyltransferase |
180-338 |
3.13e-33 |
|
phosphopantetheine adenylyltransferase
Pssm-ID: 215218 Cd Length: 177 Bit Score: 125.06 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 180 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 259
Cdd:PLN02388 8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996043 260 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 338
Cdd:PLN02388 88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
|
|
| coaE |
PRK14734 |
dephospho-CoA kinase; Provisional |
358-556 |
7.97e-33 |
|
dephospho-CoA kinase; Provisional
Pssm-ID: 237808 Cd Length: 200 Bit Score: 124.57 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 358 LYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQL 437
Cdd:PRK14734 1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 438 KILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQS 517
Cdd:PRK14734 81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 767996043 518 QMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRI 556
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
|
|
| CAB4 |
COG1019 |
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
195-347 |
1.51e-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: 116.45 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 195 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 274
Cdd:COG1019 5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996043 275 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 347
Cdd:COG1019 83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
197-339 |
1.44e-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: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 197 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 276
Cdd:pfam01467 3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767996043 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 |
5.51e-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: 5.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996043 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 |
3.05e-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: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDP 272
Cdd:cd02164 1 KVAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996043 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 ... |
360-536 |
1.69e-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: 205.83 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:cd02022 1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 440 LTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQM 519
Cdd:cd02022 81 LEAITHPLIRKEIEEQLAE--ARKEKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIASQM 158
|
170
....*....|....*..
gi 767996043 520 SGQQLVEQSHVVLSTLW 536
Cdd:cd02022 159 PLEEKRARADFVIDNSG 175
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
359-552 |
1.13e-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: 204.15 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:COG0237 2 LIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIAKLAREEMDRavAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 518
Cdd:COG0237 82 KLEAIVHPLVREEIERRLAA--ARGAPYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARIAAQ 159
|
170 180 190
....*....|....*....|....*....|....
gi 767996043 519 MSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALL 552
Cdd:COG0237 160 MPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
|
|
| CoaE |
pfam01121 |
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ... |
359-532 |
3.29e-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: 141.31 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 359 YVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:pfam01121 1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIAKLAREEMdrAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQ 518
Cdd:pfam01121 81 WLNGILHPLIRREIFKQI--ATLTAAPYVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIAAQ 158
|
170
....*....|....
gi 767996043 519 MSGQQLVEQSHVVL 532
Cdd:pfam01121 159 ASREERLALADDVL 172
|
|
| TIGR00152 |
TIGR00152 |
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ... |
360-532 |
1.49e-33 |
|
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: 126.35 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLKGLGAF-VIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:TIGR00152 1 LIALTGGIGSGKSTVLQYLADKYHFpVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPIIaklaREEMDRAVAE---GKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRL 515
Cdd:TIGR00152 81 WLNALTHPLI----RQWMKKLIAQfqsKYALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRL 156
|
170
....*....|....*..
gi 767996043 516 QSQMSGQQLVEQSHVVL 532
Cdd:TIGR00152 157 ASQMDIEEKLARIDTVI 173
|
|
| PLN02388 |
PLN02388 |
phosphopantetheine adenylyltransferase |
180-338 |
3.13e-33 |
|
phosphopantetheine adenylyltransferase
Pssm-ID: 215218 Cd Length: 177 Bit Score: 125.06 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 180 VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIK 259
Cdd:PLN02388 8 VADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEYIKSIK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996043 260 PSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhtENEEDKVSSSSFRQ 338
Cdd:PLN02388 88 PELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVPE----ESTGNKLSSTTLRR 162
|
|
| coaE |
PRK14734 |
dephospho-CoA kinase; Provisional |
358-556 |
7.97e-33 |
|
dephospho-CoA kinase; Provisional
Pssm-ID: 237808 Cd Length: 200 Bit Score: 124.57 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 358 LYVIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQL 437
Cdd:PRK14734 1 MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 438 KILTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQS 517
Cdd:PRK14734 81 ALLNAITHPRIAEETARRFNEARAQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 767996043 518 QMSGQQLVEQSHVVLSTLWEPHITQRQVEKAWALLQKRI 556
Cdd:PRK14734 161 QIPDDVRLKAADIVVDNNGTREQLLAQVDGLIAEILSRV 199
|
|
| coaE |
PRK03333 |
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional |
361-550 |
1.07e-30 |
|
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
Pssm-ID: 179560 [Multi-domain] Cd Length: 395 Bit Score: 123.58 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 361 IGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKIL 440
Cdd:PRK03333 4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 441 TDIMWPIIAKLAREEMDRAVAEGkrVCVIDAAVLLEAGWQNLVHEVWTAVIPETEAVRRIVERDGLSEAAAQSRLQSQMS 520
Cdd:PRK03333 84 NGIVHPLVGARRAELIAAAPEDA--VVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRRLVEQRGMAEADARARIAAQAS 161
|
170 180 190
....*....|....*....|....*....|
gi 767996043 521 GQQLVEQSHVVLSTLWEPHITQRQVEKAWA 550
Cdd:PRK03333 162 DEQRRAVADVWLDNSGTPDELVEAVRALWA 191
|
|
| CAB4 |
COG1019 |
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
195-347 |
1.51e-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: 116.45 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 195 AVGGTFDRLHNAHKVLLSVACILAqEQLVVGVADKDLLKsKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYG 274
Cdd:COG1019 5 AVGGTFDPLHDGHRALLERAFELG-GDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLDDPYG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996043 275 PAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKdlrhtenEEDKVSSSSFRQRM-----LGNLLRP 347
Cdd:COG1019 83 PALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVL-------AEDGKPISSTRIRNgeideHGRLLKD 153
|
|
| PRK00777 |
PRK00777 |
pantetheine-phosphate adenylyltransferase; |
191-348 |
5.68e-26 |
|
pantetheine-phosphate adenylyltransferase;
Pssm-ID: 234834 Cd Length: 153 Bit Score: 103.76 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 191 YYRGAVGGTFDRLHNAHKVLLSVACILAQEqLVVGVADKDLLKSKLlPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLL 270
Cdd:PRK00777 1 MMKVAVGGTFDPLHDGHRALLRKAFELGKR-VTIGLTSDEFAKSYK-KHKVRPYEVRLKNLKKFLKAVEYDREYEIVKID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 271 DPYGPAGSDPsLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDlrhteneEDKVSSSSFRQR-----MLGNLL 345
Cdd:PRK00777 79 DPYGPALEDD-FDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLA-------EDGKPISSTRIRrgeidEHGNLI 150
|
...
gi 767996043 346 RPP 348
Cdd:PRK00777 151 KER 153
|
|
| PLN02422 |
PLN02422 |
dephospho-CoA kinase |
360-520 |
6.45e-26 |
|
dephospho-CoA kinase
Pssm-ID: 215232 Cd Length: 232 Bit Score: 105.98 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLKGLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLKI 439
Cdd:PLN02422 3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 440 LTDIMWPIIAKLAREEMDRAVAEGKRVCVIDAAVLLEAG---WQNLVHEVWtaVIPETEaVRRIVERDGLSEAAAQSRLQ 516
Cdd:PLN02422 83 LNRLLAPYISSGIFWEILKLWLKGCKVIVLDIPLLFETKmdkWTKPVVVVW--VDPETQ-LERLMARDGLSEEQARNRIN 159
|
....
gi 767996043 517 SQMS 520
Cdd:PLN02422 160 AQMP 163
|
|
| PRK01170 |
PRK01170 |
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase; |
196-315 |
9.70e-13 |
|
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
Pssm-ID: 234912 [Multi-domain] Cd Length: 322 Bit Score: 69.46 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 196 VGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPellQPYTERVEHLSEFLvdIKPSLTFDVIPLLDPYGP 275
Cdd:PRK01170 5 VGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYP---IPYEDRKRKLENFI--KKFTNKFRIRPIDDRYGN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767996043 276 AGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQI 315
Cdd:PRK01170 80 TLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRV 119
|
|
| CTP_transf_like |
pfam01467 |
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
197-339 |
1.44e-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: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 197 GGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPelLQPYTERVEHLSEflvdIKPSLTFDVIPLLDPYGPA 276
Cdd:pfam01467 3 GGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTREL 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767996043 277 GSDPSLEFLVVSEETYRGgmAINRFRLENDLEELAlyqIQLLKDLRHTENEEDKVSSSSFRQR 339
Cdd:pfam01467 77 LKELNPDVLVIGADSLLD--FWYELDEILGNVKLV---VVVRPVFFIPLKPTNGISSTDIRER 134
|
|
| PTZ00451 |
PTZ00451 |
dephospho-CoA kinase; Provisional |
360-520 |
2.87e-09 |
|
dephospho-CoA kinase; Provisional
Pssm-ID: 185630 Cd Length: 244 Bit Score: 57.96 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRLK-GLGAFVIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGIINRKVLGSRVFGNKKQLK 438
Cdd:PTZ00451 3 LIGLTGGIACGKSTVSRILReEHHIEVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 439 ILTDIMWPII--------AKLAREEMDRAVA-EGKRVCVIDAAVLLEAG-WQNLVHEVWTAVIPETEAVRRIVERDGLSE 508
Cdd:PTZ00451 83 ALGRIMNPPIfrailkriAAAWWEDLWRSGAgSSPLIVVLDAPTLFETKtFTYFVSASVVVSCSEERQIERLRKRNGFSK 162
|
170
....*....|..
gi 767996043 509 AAAQSRLQSQMS 520
Cdd:PTZ00451 163 EEALQRIGSQMP 174
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
193-339 |
8.14e-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: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 193 RGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVadKDLLKSKLLPELLQPYTERVEHLSEFLVD-----------IKPS 261
Cdd:cd02039 1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIII--VSNPPKKKRNKDPFSLHERVEMLKEILKDrlkvvpvdfpeVKIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996043 262 LTFD-VIPLLDPYGPagsdpslEFLVVSEETYRGGMAINRFRL---ENDLEELALYQIqllkdlrhteNEEDKVSSSSFR 337
Cdd:cd02039 79 LAVVfILKILLKVGP-------DKVVVGEDFAFGKNASYNKDLkelFLDIEIVEVPRV----------RDGKKISSTLIR 141
|
..
gi 767996043 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 |
5.51e-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: 5.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996043 193 RGAVGGTFDRLHNAHKVLLSVACILAqEQLVVGVAdKDLLKSKLLPELLQPYTERVEHLSEFLVDIKP 260
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELF-DELIVGVG-SDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
360-389 |
1.07e-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: 1.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 767996043 360 VIGLTGISGSGKSSIA----QRLKGLG--AFVIDSD 389
Cdd:COG0529 18 VVWFTGLSGSGKSTLAnaleRRLFERGrhVYLLDGD 53
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
358-409 |
1.08e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 39.90 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767996043 358 LYVIGltGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRAYAPGGPAYQPVVEA 409
Cdd:COG0645 1 LILVC--GLPGSGKSTLARALaERLGAVRLRSDVVRKRLFGAGLAPLERSPEA 51
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
363-391 |
1.48e-03 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 39.79 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|
gi 767996043 363 LTGISGSGKSSIAQRL-KGLGAFVIDSDHL 391
Cdd:PRK00131 9 LIGFMGAGKSTIGRLLaKRLGYDFIDTDHL 38
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
360-393 |
2.20e-03 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 40.68 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767996043 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 |
3.87e-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: 3.87e-03
10 20 30
....*....|....*....|....*....|..
gi 767996043 361 IGLTGISGSGKSSIAQRL-KGLGAFVIDSDHL 391
Cdd:cd00464 2 IVLIGMMGAGKTTVGRLLaKALGLPFVDLDEL 33
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
360-393 |
4.26e-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: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 393
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALeeklfqRGRPVYVLDGDNVRH 40
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
360-393 |
5.98e-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: 5.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767996043 360 VIGLTGISGSGKSSIAQRL------KGLGAFVIDSDHLGH 393
Cdd:pfam01583 4 TIWLTGLSGAGKSTIANALerklfeQGRSVYVLDGDNVRH 43
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
358-395 |
7.44e-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: 7.44e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767996043 358 LYVIglTGISGSGKSSIAQRL-KGLGAFVIDSDHLGHRA 395
Cdd:cd02021 1 IIVV--MGVSGSGKSTVGKALaERLGAPFIDGDDLHPPA 37
|
|
|