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Conserved domains on  [gi|504265891|ref|WP_014452993|]
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bifunctional riboflavin kinase/FAD synthetase [Caldisericum exile]

Protein Classification

bifunctional riboflavin kinase/FMN adenylyltransferase( domain architecture ID 11415176)

bifunctional riboflavin biosynthesis protein having both ATP-riboflavin kinase and ATP-flavin mononucleotide adenylyltransferase activities

CATH:  3.40.50.620|2.40.30.30
EC:  2.7.1.26|2.7.7.2
Gene Symbol:  ribF
Gene Ontology:  GO:0005524|GO:0006747|GO:0009398|GO:0003919|GO:0008531|GO:0016310|GO:0009231
PubMed:  25801930

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-305 3.40e-133

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: 380.54  E-value: 3.40e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   1 MKIIE-FH--KPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPI----KEAKRKLLTTLNEKLYI 73
Cdd:COG0196    1 MKIIRgLSelPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPRevfrPDKAPKLLTTLEEKLEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  74 FEKLDVENIYIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDG 153
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 154 VAVSSSLIHDLILGGEIEEGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGV 233
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDGRRYPGV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504265891 234 TNVGFNPTFEDKKnVKIESHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFESNP 305
Cdd:COG0196  240 ANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-305 3.40e-133

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: 380.54  E-value: 3.40e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   1 MKIIE-FH--KPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPI----KEAKRKLLTTLNEKLYI 73
Cdd:COG0196    1 MKIIRgLSelPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPRevfrPDKAPKLLTTLEEKLEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  74 FEKLDVENIYIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDG 153
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 154 VAVSSSLIHDLILGGEIEEGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGV 233
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDGRRYPGV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504265891 234 TNVGFNPTFEDKKnVKIESHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFESNP 305
Cdd:COG0196  240 ANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
7-301 2.79e-115

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 334.81  E-value: 2.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   7 HKPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHP----IKEAKRKLLTTLNEKLYIFEKLDVENI 82
Cdd:PRK05627   8 NIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPrevfAPDKAPARLTPLRDKAELLAELGVDYV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  83 YIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSLIH 162
Cdd:PRK05627  88 LVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 163 DLILGGEIEEGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYEngNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTF 242
Cdd:PRK05627 168 QALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGKPYPGVANIGTRPTV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504265891 243 eDKKNVKIESHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFF 301
Cdd:PRK05627 246 -DGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFL 303
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 15-302 3.54e-75

riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase). [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 272898 [Multi-domain]  Cd Length: 288  Bit Score: 232.34  E-value: 3.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   15 AIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPIKEAKRK---LLTTLNEKLYIFEKLDVENIYIANLEEDL 91
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLtapALTPLEDKARQLQIKGVEQLLVVVFDEEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   92 MTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIiVNKVLKDGVAVSSSLIHDLILGGEIE 171
Cdd:TIGR00083  81 ANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVI-VKQLFCQDIRISSSAIRQALKNGDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  172 EGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTFeDKKNVKIE 251
Cdd:TIGR00083 160 LANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKN-QVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTF-IGQQLVIE 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504265891  252 SHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFE 302
Cdd:TIGR00083 238 VHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 14-190 2.63e-64

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: 200.46  E-value: 2.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  14 TAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHP----IKEAKRKLLTTLNEKLYIFEKLDVENIYIANLEE 89
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPrevfLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  90 DLMTMSPEEFVKKELVKtLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSLIHDLILGGE 169
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159

                        170       180
                 ....*....|....*....|.
gi 504265891 170 IEEGNSLLGHPYFVQGIVERG 190
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 7-160 1.82e-52

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: 169.67  E-value: 1.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891    7 HKPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPI----KEAKRKLLTTLNEKLYIFEKLDVENI 82
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPRevfnPDSAPFRLTTLEEKIELLAELGVDYL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504265891   83 YIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSL 160
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 176-302 8.66e-49

Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.


Pssm-ID: 214901 [Multi-domain]  Cd Length: 124  Bit Score: 158.76  E-value: 8.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   176 LLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTFEDKKnvKIESHFL 255
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR--SVEVHIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 504265891   256 DVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFE 302
Cdd:smart00904  78 DFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-305 3.40e-133

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: 380.54  E-value: 3.40e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   1 MKIIE-FH--KPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPI----KEAKRKLLTTLNEKLYI 73
Cdd:COG0196    1 MKIIRgLSelPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPRevfrPDKAPKLLTTLEEKLEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  74 FEKLDVENIYIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDG 153
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 154 VAVSSSLIHDLILGGEIEEGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGV 233
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDGRRYPGV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504265891 234 TNVGFNPTFEDKKnVKIESHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFESNP 305
Cdd:COG0196  240 ANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
7-301 2.79e-115

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 334.81  E-value: 2.79e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   7 HKPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHP----IKEAKRKLLTTLNEKLYIFEKLDVENI 82
Cdd:PRK05627   8 NIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPrevfAPDKAPARLTPLRDKAELLAELGVDYV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  83 YIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSLIH 162
Cdd:PRK05627  88 LVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 163 DLILGGEIEEGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYEngNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTF 242
Cdd:PRK05627 168 QALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGKPYPGVANIGTRPTV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504265891 243 eDKKNVKIESHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFF 301
Cdd:PRK05627 246 -DGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFL 303
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 15-302 3.54e-75

riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase). [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD]


Pssm-ID: 272898 [Multi-domain]  Cd Length: 288  Bit Score: 232.34  E-value: 3.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   15 AIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPIKEAKRK---LLTTLNEKLYIFEKLDVENIYIANLEEDL 91
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLtapALTPLEDKARQLQIKGVEQLLVVVFDEEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   92 MTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIiVNKVLKDGVAVSSSLIHDLILGGEIE 171
Cdd:TIGR00083  81 ANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVI-VKQLFCQDIRISSSAIRQALKNGDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  172 EGNSLLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTFeDKKNVKIE 251
Cdd:TIGR00083 160 LANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKN-QVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTF-IGQQLVIE 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504265891  252 SHFLDVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFE 302
Cdd:TIGR00083 238 VHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 14-190 2.63e-64

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: 200.46  E-value: 2.63e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  14 TAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHP----IKEAKRKLLTTLNEKLYIFEKLDVENIYIANLEE 89
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPrevfLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  90 DLMTMSPEEFVKKELVKtLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSLIHDLILGGE 169
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159

                        170       180
                 ....*....|....*....|.
gi 504265891 170 IEEGNSLLGHPYFVQGIVERG 190
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 7-160 1.82e-52

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: 169.67  E-value: 1.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891    7 HKPVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKNLCPVIYTFSNHPI----KEAKRKLLTTLNEKLYIFEKLDVENI 82
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPRevfnPDSAPFRLTTLEEKIELLAELGVDYL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504265891   83 YIANLEEDLMTMSPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKELGKIFNFEVIIVNKVLKDGVAVSSSL 160
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 176-302 8.66e-49

Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.


Pssm-ID: 214901 [Multi-domain]  Cd Length: 124  Bit Score: 158.76  E-value: 8.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   176 LLGHPYFVQGIVERGKGLGRHLGFPTANLAYENgNKLLPKNGVYITIGNYNGILLKGVTNVGFNPTFEDKKnvKIESHFL 255
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR--SVEVHIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 504265891   256 DVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFFE 302
Cdd:smart00904  78 DFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 177-301 2.06e-48

Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism. This domain is thought to have kinase activity.


Pssm-ID: 460295 [Multi-domain]  Cd Length: 123  Bit Score: 157.92  E-value: 2.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  177 LGHPYFVQGIVERGKGLGRHLGFPTANLAYENgnKLLPKNGVYITIGNYNGI-LLKGVTNVGFNPTFEDKKnVKIESHFL 255
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPE--KLLPANGVYAVWVRVDGGkVYPGVANIGTNPTFGNGK-LTVEVHIL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 504265891  256 DVENDFYGKFLRLYFIKRLRDEIKYEKVQDLRNQVMADIEETRKFF 301
Cdd:pfam01687  78 DFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
PRK07143 PRK07143
hypothetical protein; Provisional
 1-304 1.37e-20

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 89.29  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   1 MKIIEFHK--PVSKKTAIAIGMFDGVHLGHKALISQLLGKSDEKnlcpVIYTFSNhPIKEAK--RKLLTTLNEKLYIFEK 76
Cdd:PRK07143   2 MKVYTFPLknFKFEKPTFVLGGFESFHLGHLELFKKAKESNDEI----VIVIFKN-PENLPKntNKKFSDLNSRLQTLAN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  77 LDVENIYIANLEEDLMTMSPEEFVKKelVKTLNCKLVIVGENFRFGHKKEGNVNTLKElgkiFNFEVIIVNKVLKDGVAV 156
Cdd:PRK07143  77 LGFKNIILLDFNEELQNLSGNDFIEK--LTKNQVSFFVVGKDFRFGKNASWNADDLKE----YFPNVHIVEILKINQQKI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 157 SSSLIHDLILGGEIEEGNSLLGHPYFVQGIVERGKglgrhlgfptaNLAY-ENGNKLlpKNGVYITIGNYNGILLKGVTN 235
Cdd:PRK07143 151 STSLLKEFIEFGDIELLNSLLLYNYSISITINKNF-----------EFTYpQNIIKL--HAGIYLAYVVINNFKYHGILK 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504265891 236 VGFNptfedkKNVKIESHFLDVENDFYGKfLRLYFIKRLRDEIKYEKvQDLRNQvmaDIEETRKFFESN 304
Cdd:PRK07143 218 INFN------NKNKIKFFDFDLIINKYQE-IFIEIVKEIRIISSNED-NNILND---DIEIAKKFFLNN 275
PLN02940 PLN02940
riboflavin kinase
 173-302 5.74e-11

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 62.54  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891 173 GNSLLGHPYFVQGIVERGKGLG-RHLGFPTANLAYENGNKLLPKN--GVYIT-IGNYNGILLKGVTNVGFNPTFEDKKNV 248
Cdd:PLN02940 231 EGTLPIEPWHIGGPVIKGFGRGsKVLGIPTANLSTENYSDVLSEHpsGVYFGwAGLSTRGVYKMVMSIGWNPYFNNTEKT 310

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504265891 249 kIESHFL-DVENDFYGKFLRLYFIKRLRDEIKYEKVQDLrnqvMADIEETRKFFE 302
Cdd:PLN02940 311 -IEPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESL----IAKIHEDRRIAE 360
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 15-161 1.57e-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: 49.75  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891  15 AIAIGMFDGVHLGHKALISQLLGKSDEKNlcpVIYTFSNhPIKEAKRKLLTTLNEKLYIFEKLDVENIYIANLEEDLMTM 94
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEEALDEV---IIIIVSN-PPKKKRNKDPFSLHERVEMLKEILKDRLKVVPVDFPEVKI 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504265891  95 SPEEFVKKELVKTLNCKLVIVGENFRFGHKKEGNVNTLKelgKIFNFEVIIVNKVlKDGVAVSSSLI 161
Cdd:cd02039   78 LLAVVFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKE---LFLDIEIVEVPRV-RDGKKISSTLI 140
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 15-57 3.19e-03

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: 35.36  E-value: 3.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 504265891   15 AIAIGMFDGVHLGHKALISQLLGKSDEKNLCpVIYTFSNHPIK 57
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDELIVG-VGSDQFVNPLK 43
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 16-161 8.20e-03

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: 36.14  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504265891   16 IAIGMFDGVHLGHKALISQLLGKSDEKnlcpVIYTFSNHPIKEAKRKLLTTLNEKlyifekldVENIYIANLEEDLMTMS 95
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED----LIVGVPSDEPPHKLKRPLFSAEER--------LEMLELAKWVDEVIVVA 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504265891   96 PEEfVKKELVKTLNCKLVIVG-ENFRFGHKKEGNVNTLKELgKIFNFEVIIvnKVLKDGVAVSSSLI 161
Cdd:pfam01467  69 PWE-LTRELLKELNPDVLVIGaDSLLDFWYELDEILGNVKL-VVVVRPVFF--IPLKPTNGISSTDI 131
 
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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