NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24658602|ref|NP_647985|]
View 

bifunctional phosphopantetheine adenylyltransferase - Dephospho-CoA kinase [Drosophila melanogaster]

Protein Classification

dephospho-CoA kinase; nucleoside/nucleotide kinase family protein( 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| nucleoside/nucleotide kinase family protein may catalyze the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 147-290 3.46e-66

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: 210.60  E-value: 3.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 147 VVLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPIDDPF 226
Cdd:cd02164   2 VAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658602 227 GPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVEsnvhDGIHETKVSSSNTR 290
Cdd:cd02164  82 GPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVK----ADEDGEKISSTRIR 141
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 313-494 5.21e-66

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: 211.22  E-value: 5.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 313 IIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQA 392
Cdd:cd02022   1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 393 LNGIVWPELIAEVNRRLDALRSqadvPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLAS 472
Cdd:cd02022  81 LEAITHPLIRKEIEEQLAEARK----EKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIAS 156

                       170       180
                ....*....|....*....|..
gi 24658602 473 QVPNSEIVAKSHVIFSSQWDHE 494
Cdd:cd02022 157 QMPLEEKRARADFVIDNSGSLE 178
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 147-290 3.46e-66

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: 210.60  E-value: 3.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 147 VVLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPIDDPF 226
Cdd:cd02164   2 VAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658602 227 GPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVEsnvhDGIHETKVSSSNTR 290
Cdd:cd02164  82 GPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVK----ADEDGEKISSTRIR 141
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 313-494 5.21e-66

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: 211.22  E-value: 5.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 313 IIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQA 392
Cdd:cd02022   1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 393 LNGIVWPELIAEVNRRLDALRSqadvPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLAS 472
Cdd:cd02022  81 LEAITHPLIRKEIEEQLAEARK----EKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIAS 156

                       170       180
                ....*....|....*....|..
gi 24658602 473 QVPNSEIVAKSHVIFSSQWDHE 494
Cdd:cd02022 157 QMPLEEKRARADFVIDNSGSLE 178
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 311-507 1.30e-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: 202.99  E-value: 1.30e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 311 PYIIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQL 390
Cdd:COG0237   1 MLIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 391 QALNGIVWPELIAEVNRRLDALRSQadvpRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRL 470
Cdd:COG0237  81 KKLEAIVHPLVREEIERRLAAARGA----PYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARI 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24658602 471 ASQVPNSEIVAKSHVIFSSQWDHEFTQKQAERAWKML 507
Cdd:COG0237 157 AAQMPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 312-486 2.52e-47

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: 162.49  E-value: 2.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   312 YIIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQ 391
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   392 ALNGIVWPELIAEVNRRLDALRSQAdvprVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLA 471
Cdd:pfam01121  81 WLNGILHPLIRREIFKQIATLTAAP----YVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIA 156

                         170
                  ....*....|....*
gi 24658602   472 SQVPNSEIVAKSHVI 486
Cdd:pfam01121 157 AQASREERLALADDV 171
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 313-487 4.44e-40

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: 143.30  E-value: 4.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   313 IIGLTGGIASGKSKMGERLANMGA-HVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQ 391
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHfPVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   392 ALNGIVWPELIAEVNRRLDALRSQAdvpRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLA 471
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSKY---ALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLA 157

                         170
                  ....*....|....*.
gi 24658602   472 SQVPNSEIVAKSHVIF 487
Cdd:TIGR00152 158 SQMDIEEKLARIDTVI 173
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
144-291 7.30e-37

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 133.42  E-value: 7.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  144 YPSVVLGGTFDRIHLGHKIFLTQAVLrTCKRLVVGVTTSAM-TKGKTLPdlILPVEERIARLREFLVDIDDTLQYEIVPI 222
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFE-LGKRVTIGLTSDEFaKSYKKHK--VRPYEVRLKNLKKFLKAVEYDREYEIVKI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658602  223 DDPFGPTqVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNvhDGIhetKVSSsnTRI 291
Cdd:PRK00777  78 DDPYGPA-LEDDFDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLAE--DGK---PISS--TRI 138
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 144-291 2.38e-36

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: 131.86  E-value: 2.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 144 YPSVVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKgKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPID 223
Cdd:COG1019   1 YMKVAVGGTFDPLHDGHRALLERA-FELGGDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24658602 224 DPFGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNvhDGiheTKVSSsnTRI 291
Cdd:COG1019  79 DPYGPALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVLAE--DG---KPISS--TRI 139
coaE PRK14734
dephospho-CoA kinase; Provisional
 314-504 4.22e-33

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 124.96  E-value: 4.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  314 IGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQAL 393
Cdd:PRK14734   4 IGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQTALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  394 NGIVWPELIAEVNRRLDALRSQAdvPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLASQ 473
Cdd:PRK14734  84 NAITHPRIAEETARRFNEARAQG--AKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAAQ 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24658602  474 VPNSEIVAKSHVIFSSQWDHEFTQKQAERAW 504
Cdd:PRK14734 162 IPDDVRLKAADIVVDNNGTREQLLAQVDGLI 192
CoaD_Thcocales NF041124
phosphopantetheine adenylyltransferase;
142-300 6.23e-23

phosphopantetheine adenylyltransferase;


Pssm-ID: 469047  Cd Length: 156  Bit Score: 95.24  E-value: 6.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  142 KVYPSVVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREFLvDIDDTLQYEIVP 221
Cdd:NF041124   2 KKYRKVVVGGTFDRLHLGHKALLRKA-FEVGEYVYIGLTSDEMIRDKPYAEKILPYELRLRDLIKFF-EVNGYSNYRIIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  222 IDDPFGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNVHDgihetKVSSSNTR---IDLLGTRW 298
Cdd:NF041124  80 IHTAIGFADEMKSLEAIVVSEETYKGALVVNRAREENGLKPLEIVTIGLVKSSLGP-----KISSSLIRaglIDPFGRPL 154


                 ..
gi 24658602  299 RR 300
Cdd:NF041124 155 SR 156
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 148-270 2.55e-10

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 58.49  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   148 VLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPdlILPVEERIARLREflvdIDDTLQYEIVPIDDPFG 227
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24658602   228 PTQVDPDLDMIVVSAETLRggQKVNEVRSAKQLRELEIFVIDI 270
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLL--DFWYELDEILGNVKLVVVVRPV 115
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 147-212 2.20e-07

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: 48.07  E-value: 2.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658602   147 VVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKG-KTLPdlILPVEERIARLREFLVDID 212
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERA-KELFDELIVGVGSDQFVNPlKGEP--VFSLEERLEMLKALKYVDE 65
 
Name Accession Description Interval E-value
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 147-290 3.46e-66

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: 210.60  E-value: 3.46e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 147 VVLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPIDDPF 226
Cdd:cd02164   2 VAVGGTFDRLHDGHKILLSVAFLLAGEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEFLVDLKPTLKYEIVPIDDPY 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658602 227 GPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVEsnvhDGIHETKVSSSNTR 290
Cdd:cd02164  82 GPTGTDPDLEAIVVSPETYPGALKINRKREENGLSPLEIVVVPLVK----ADEDGEKISSTRIR 141
DPCK cd02022
Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of ...
 313-494 5.21e-66

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: 211.22  E-value: 5.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 313 IIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQA 392
Cdd:cd02022   1 IIGLTGGIGSGKSTVAKLLKELGIPVIDADKIAHEVYEPGGPALQAIVEAFGPDILLEDGELDRKKLGEIVFADPEKRKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 393 LNGIVWPELIAEVNRRLDALRSqadvPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLAS 472
Cdd:cd02022  81 LEAITHPLIRKEIEEQLAEARK----EKVVVLDIPLLFETGLEKLVDRVIVVDAPPEIQIERLMKRDGLSEEEAEARIAS 156

                       170       180
                ....*....|....*....|..
gi 24658602 473 QVPNSEIVAKSHVIFSSQWDHE 494
Cdd:cd02022 157 QMPLEEKRARADFVIDNSGSLE 178
CoaE COG0237
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ...
 311-507 1.30e-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: 202.99  E-value: 1.30e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 311 PYIIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQL 390
Cdd:COG0237   1 MLIIGLTGGIGSGKSTVARMFAELGAPVIDADAIARELVEPGGPALAAIVEAFGEEILDADGSLDRKALAEIVFADPEAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 391 QALNGIVWPELIAEVNRRLDALRSQadvpRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRL 470
Cdd:COG0237  81 KKLEAIVHPLVREEIERRLAAARGA----PYVVLDIPLLFETGLEKLVDRVIVVDAPEEVQIERLMARDGLSEEEAEARI 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24658602 471 ASQVPNSEIVAKSHVIFSSQWDHEFTQKQAERAWKML 507
Cdd:COG0237 157 AAQMPDEEKRARADFVIDNDGSLEELRAQVDALLEKL 193
CoaE pfam01121
Dephospho-CoA kinase; This family catalyzes the phosphorylation of the 3'-hydroxyl group of ...
 312-486 2.52e-47

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: 162.49  E-value: 2.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   312 YIIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQ 391
Cdd:pfam01121   1 LIVGLTGGIGSGKSTVANYFRDLGVPIIDADAIARQVVEPGGPALSRIVRHFGPTILDADGQLDRRALRELVFSNPERKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   392 ALNGIVWPELIAEVNRRLDALRSQAdvprVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLA 471
Cdd:pfam01121  81 WLNGILHPLIRREIFKQIATLTAAP----YVVLDIPLLFESGLHKLCHRVLVVDAPPELQVERLVARDGLSREEAQARIA 156

                         170
                  ....*....|....*
gi 24658602   472 SQVPNSEIVAKSHVI 486
Cdd:pfam01121 157 AQASREERLALADDV 171
TIGR00152 TIGR00152
dephospho-CoA kinase; This model produces scores in the range of 0-25 bits against adenylate, ...
 313-487 4.44e-40

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: 143.30  E-value: 4.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   313 IIGLTGGIASGKSKMGERLANMGA-HVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQ 391
Cdd:TIGR00152   1 LIALTGGIGSGKSTVLQYLADKYHfPVIDADKIAHQVVEPGQPAYHAIADHFGANILNQDGELDRKALGNYVFNDPEELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   392 ALNGIVWPELIAEVNRRLDALRSQAdvpRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLA 471
Cdd:TIGR00152  81 WLNALTHPLIRQWMKKLIAQFQSKY---ALVLLDVPLLFENNLRSLVDYVIVVERSPELQLERLMQRNDLTEEEVKKRLA 157

                         170
                  ....*....|....*.
gi 24658602   472 SQVPNSEIVAKSHVIF 487
Cdd:TIGR00152 158 SQMDIEEKLARIDTVI 173
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
144-291 7.30e-37

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 133.42  E-value: 7.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  144 YPSVVLGGTFDRIHLGHKIFLTQAVLrTCKRLVVGVTTSAM-TKGKTLPdlILPVEERIARLREFLVDIDDTLQYEIVPI 222
Cdd:PRK00777   1 MMKVAVGGTFDPLHDGHRALLRKAFE-LGKRVTIGLTSDEFaKSYKKHK--VRPYEVRLKNLKKFLKAVEYDREYEIVKI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658602  223 DDPFGPTqVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNvhDGIhetKVSSsnTRI 291
Cdd:PRK00777  78 DDPYGPA-LEDDFDAIVVSPETYPGALKINEIRRERGLKPLEIVVIDFVLAE--DGK---PISS--TRI 138
CAB4 COG1019
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 144-291 2.38e-36

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: 131.86  E-value: 2.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 144 YPSVVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKgKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPID 223
Cdd:COG1019   1 YMKVAVGGTFDPLHDGHRALLERA-FELGGDVIIGLTSDELAK-KTKKRPVRPYEERRENLEAFLEKLAPDREYEIRKLD 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24658602 224 DPFGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNvhDGiheTKVSSsnTRI 291
Cdd:COG1019  79 DPYGPALEDEDFDALVVSPETEPGAEKINEIRRERGLKPLEIVVVPHVLAE--DG---KPISS--TRI 139
PLN02388 PLN02388
phosphopantetheine adenylyltransferase
 128-290 1.24e-35

phosphopantetheine adenylyltransferase


Pssm-ID: 215218  Cd Length: 177  Bit Score: 130.84  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  128 ISDLSAQQDDTQPPKVYPSVVLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREF 207
Cdd:PLN02388   3 TVKDSVADSKLSPPNSYGAVVLGGTFDRLHDGHRLFLKAAAELARDRIVIGVCDGPMLSKKQFAELIQPIEERMHNVEEY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  208 LVDIDDTLQYEIVPIDDPFGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVEsnvhDGIHETKVSSS 287
Cdd:PLN02388  83 IKSIKPELVVQAEPIIDPYGPSIVDENLEAIVVSKETLPGGLSVNKKRAERGLSQLKIEVVDIVP----EESTGNKLSST 158


                 ...
gi 24658602  288 NTR 290
Cdd:PLN02388 159 TLR 161
coaE PRK14734
dephospho-CoA kinase; Provisional
 314-504 4.22e-33

dephospho-CoA kinase; Provisional


Pssm-ID: 237808  Cd Length: 200  Bit Score: 124.96  E-value: 4.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  314 IGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQAL 393
Cdd:PRK14734   4 IGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGDDILNPDGTLDRAGLAAKAFASPEQTALL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  394 NGIVWPELIAEVNRRLDALRSQAdvPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLASQ 473
Cdd:PRK14734  84 NAITHPRIAEETARRFNEARAQG--AKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLDEDDARRRIAAQ 161

                        170       180       190
                 ....*....|....*....|....*....|.
gi 24658602  474 VPNSEIVAKSHVIFSSQWDHEFTQKQAERAW 504
Cdd:PRK14734 162 IPDDVRLKAADIVVDNNGTREQLLAQVDGLI 192
coaE PRK03333
dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional
 314-473 4.09e-31

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


Pssm-ID: 179560 [Multi-domain]  Cd Length: 395  Bit Score: 124.35  E-value: 4.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  314 IGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQAL 393
Cdd:PRK03333   4 IGLTGGIGAGKSTVAARLAELGAVVVDADVLAREVVEPGTEGLAALVAAFGDDILLADGALDRPALAAKAFADDEARAVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  394 NGIVWPeliaEVNRRLDALRSQADVPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLASQ 473
Cdd:PRK03333  84 NGIVHP----LVGARRAELIAAAPEDAVVVEDIPLLVESGMAPLFHLVVVVDADVEVRVRRLVEQRGMAEADARARIAAQ 159
PLN02422 PLN02422
dephospho-CoA kinase
 313-475 2.33e-28

dephospho-CoA kinase


Pssm-ID: 215232  Cd Length: 232  Bit Score: 112.53  E-value: 2.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  313 IIGLTGGIASGKSKMGERLANMGAHVIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQLQA 392
Cdd:PLN02422   3 VVGLTGGIASGKSTVSNLFKSSGIPVVDADKVARDVLKKGSGGWKRVVAAFGEDILLPDGEVDREKLGQIVFSDPSKRQL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  393 LNGIVWPELIAEVNRRLdaLRSQADVPRVVVLEAAVLLRAGWETNCHEVWSMIVPPDEAVRRIIERNKLSEVEAQKRLAS 472
Cdd:PLN02422  83 LNRLLAPYISSGIFWEI--LKLWLKGCKVIVLDIPLLFETKMDKWTKPVVVVWVDPETQLERLMARDGLSEEQARNRINA 160


                 ...
gi 24658602  473 QVP 475
Cdd:PLN02422 161 QMP 163
CoaD_Thcocales NF041124
phosphopantetheine adenylyltransferase;
142-300 6.23e-23

phosphopantetheine adenylyltransferase;


Pssm-ID: 469047  Cd Length: 156  Bit Score: 95.24  E-value: 6.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  142 KVYPSVVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKGKTLPDLILPVEERIARLREFLvDIDDTLQYEIVP 221
Cdd:NF041124   2 KKYRKVVVGGTFDRLHLGHKALLRKA-FEVGEYVYIGLTSDEMIRDKPYAEKILPYELRLRDLIKFF-EVNGYSNYRIIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  222 IDDPFGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNVHDgihetKVSSSNTR---IDLLGTRW 298
Cdd:NF041124  80 IHTAIGFADEMKSLEAIVVSEETYKGALVVNRAREENGLKPLEIVTIGLVKSSLGP-----KISSSLIRaglIDPFGRPL 154


                 ..
gi 24658602  299 RR 300
Cdd:NF041124 155 SR 156
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
147-271 1.14e-19

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 89.88  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  147 VVLGGTFDRIHLGHKIFLTQAVlRTCKRLVVGVTTSAMTK-GKTLPdliLPVEERIARLREFLVDIddTLQYEIVPIDDP 225
Cdd:PRK01170   3 TVVGGTFSKLHKGHKALLKKAI-ETGDEVVIGLTSDEYVRkNKVYP---IPYEDRKRKLENFIKKF--TNKFRIRPIDDR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24658602  226 FGPTQVDPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIV 271
Cdd:PRK01170  77 YGNTLYEEDYEIIVVSPETYQRALKINEIRIKNGLPPLKIVRVPYV 122
PTZ00451 PTZ00451
dephospho-CoA kinase; Provisional
 313-497 3.45e-16

dephospho-CoA kinase; Provisional


Pssm-ID: 185630  Cd Length: 244  Bit Score: 77.99  E-value: 3.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  313 IIGLTGGIASGKSKMgERLANMGAH--VIDCDKVAHDVYEPGQLCYTRIVQHFGQGIVSDDGRIDRSKLGPLVFADPKQL 390
Cdd:PTZ00451   3 LIGLTGGIACGKSTV-SRILREEHHieVIDADLVVRELQAPNMACTRKIAARWPLCVHPETGELNRAELGKIIFSDAQAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602  391 QALNGIVWPELIAEVNRRLDAL-------RSQADVPRVVVLEAAVLlragWETNCHeVW----SMIV--PPDEAVRRIIE 457
Cdd:PTZ00451  82 RALGRIMNPPIFRAILKRIAAAwwedlwrSGAGSSPLIVVLDAPTL----FETKTF-TYfvsaSVVVscSEERQIERLRK 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 24658602  458 RNKLSEVEAQKRLASQVPNSEIVAKSHVIFSSQWDHEFTQ 497
Cdd:PTZ00451 157 RNGFSKEEALQRIGSQMPLEEKRRLADYIIENDSADDLDE 196
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 148-270 2.55e-10

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 58.49  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602   148 VLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMTKGKTLPdlILPVEERIARLREflvdIDDTLQYEIVPIDDPFG 227
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRP--LFSAEERLEMLEL----AKWVDEVIVVAPWELTR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24658602   228 PTQVDPDLDMIVVSAETLRggQKVNEVRSAKQLRELEIFVIDI 270
Cdd:pfam01467  75 ELLKELNPDVLVIGADSLL--DFWYELDEILGNVKLVVVVRPV 115
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 147-212 2.20e-07

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: 48.07  E-value: 2.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658602   147 VVLGGTFDRIHLGHKIFLTQAvLRTCKRLVVGVTTSAMTKG-KTLPdlILPVEERIARLREFLVDID 212
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERA-KELFDELIVGVGSDQFVNPlKGEP--VFSLEERLEMLKALKYVDE 65
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 147-290 2.51e-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: 50.13  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 147 VVLGGTFDRIHLGHKIFLTQAVLRTCKRLVVGVTTSAMtkGKTLPDLILPVEERIARLREFLVDIDDTLQYEIVPIDDPF 226
Cdd:cd02039   2 GIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPP--KKKRNKDPFSLHERVEMLKEILKDRLKVVPVDFPEVKILL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658602 227 GPTQV-----DPDLDMIVVSAETLRGGQKVNEVRSAKQLRELEIFVIDIVESNvhdgiheTKVSSSNTR 290
Cdd:cd02039  80 AVVFIlkillKVGPDKVVVGEDFAFGKNASYNKDLKELFLDIEIVEVPRVRDG-------KKISSTLIR 141
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 146-211 5.03e-05

FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal domain of the bifunctional riboflavin biosynthesis protein riboflavin kinase/FAD synthetase. These enzymes have both ATP:riboflavin 5'-phosphotransferase and ATP:FMN-adenylyltransferase activities. The N-terminal domain is believed to play a role in the adenylylation reaction of FAD synthetases. The C-terminal domain is thought to have kinase activity. FAD synthetase is present among all kingdoms of life. However, the bifunctional enzyme is not found in mammals, which use separate enzymes for FMN and FAD formation.


Pssm-ID: 185679 [Multi-domain]  Cd Length: 180  Bit Score: 44.07  E-value: 5.03e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658602 146 SVVLGGTFDRIHLGHkifltQAVLRTCKRL--VVGVTTSAMT---------KGKTLPDLILPVEERIARLREFLVDI 211
Cdd:cd02064   1 TVVAIGNFDGVHLGH-----QALIKTLKKIarERGLPSAVLTfdphprevfLPDKAPPRLTTLEEKLELLESLGVDY 72
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 145-211 1.11e-04

FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity. They catalyze the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity.


Pssm-ID: 429011 [Multi-domain]  Cd Length: 158  Bit Score: 42.55  E-value: 1.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24658602   145 PSVVLGGTFDRIHLGHKIFLTQAVLRTCKRlvvGVTTSAMT---------KGKTLPDLILPVEERIARLREFLVDI 211
Cdd:pfam06574   7 GCVVTIGNFDGVHLGHQALIAKAKEIAREL---GLPSVVVTfephprevfNPDSAPFRLTTLEEKIELLAELGVDY 79
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 140-211 1.51e-04

FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439966 [Multi-domain]  Cd Length: 310  Bit Score: 43.88  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658602 140 PPKVYPSVVLGGTFDRIHLGHkifltQAVLRTCKRL--VVGVTTSAMT---------KGKTLPDLILPVEERIARLREFL 208
Cdd:COG0196  11 PADLRGTVVTIGNFDGVHLGH-----QALIARLVELarELGLPSVVLTfephprevfRPDKAPKLLTTLEEKLELLEELG 85


                ...
gi 24658602 209 VDI 211
Cdd:COG0196  86 VDY 88
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 147-200 1.69e-04

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 41.51  E-value: 1.69e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24658602 147 VVLGGTFDRIHLGHKIFLTQAVlRTCKRLVVGVTT-SAMTKGKTLPdlILPVEER 200
Cdd:cd02170   4 VYAAGTFDIIHPGHIRFLEEAK-KLGDYLIVGVARdETVAKIKRRP--ILPEEQR 55
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 143-212 8.25e-03

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


Pssm-ID: 440433  Cd Length: 159  Bit Score: 37.29  E-value: 8.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24658602 143 VYPsvvlgGTFDRIHLGH--------KIFltqavlrtcKRLVVGVTTSAmTKgKTLpdliLPVEERIARLREFLVDID 212
Cdd:COG0669   5 VYP-----GSFDPITNGHldiieraaKLF---------DEVIVAVAVNP-SK-KPL----FSLEERVELIREALADLP 62
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
146-211 9.60e-03

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 38.21  E-value: 9.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24658602  146 SVVLGGtFDRIHLGHKIFLTQAVLRTCKRlvvGVTTSAMT----------KGKTlPDLILPVEERIARLREFLVDI 211
Cdd:PRK05627  16 VLTIGN-FDGVHRGHQALLARAREIARER---GLPSVVMTfephprevfaPDKA-PARLTPLRDKAELLAELGVDY 86
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH