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Conserved domains on  [gi|378976889|ref|YP_005225030|]
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bifunctional riboflavin kinase/FMN adenylyltransferase [Klebsiella pneumoniae subsp. pneumoniae HS11286]

Protein Classification

bifunctional riboflavin kinase/FMN adenylyltransferase( domain architecture ID 11481331)

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

EC:  2.7.1.26|2.7.7.2
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
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-291 8.88e-164

bifunctional riboflavin kinase/FAD synthetase;


:

Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 456.92  E-value: 8.88e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:PRK05627  17 LTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPFDEEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:PRK05627  97 AKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAEGDLE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVANIGTRPTVAGVRQQLEVH 241
Cdd:PRK05627 177 LANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVANIGTRPTVDGGRQLLEVH 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 378976889 242 LLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFGL 291
Cdd:PRK05627 256 LLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-291 8.88e-164

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 456.92  E-value: 8.88e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:PRK05627  17 LTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPFDEEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:PRK05627  97 AKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAEGDLE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVANIGTRPTVAGVRQQLEVH 241
Cdd:PRK05627 177 LANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVANIGTRPTVDGGRQLLEVH 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 378976889 242 LLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFGL 291
Cdd:PRK05627 256 LLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 2-290 2.83e-157

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: 440.63  E-value: 2.83e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:COG0196   19 VTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTREF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:COG0196   99 AALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDVE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVTgLGDKPIAGVANIGTRPTVAGVRQQLEV 240
Cdd:COG0196  179 EAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGVANIGTRPTFDGGEPTLEV 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 378976889 241 HLLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFG 290
Cdd:COG0196  258 HLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 2-290 3.32e-137

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: 389.11  E-value: 3.32e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPArLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:TIGR00083   2 LAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGgVRISSTAVRQALADDDLL 161
Cdd:TIGR00083  81 ANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEVH 241
Cdd:TIGR00083 160 LANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEVH 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 378976889  242 LLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFG 290
Cdd:TIGR00083 240 LLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 2-180 5.61e-78

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: 234.74  E-value: 5.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:cd02064    3 VAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKEF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVrRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:cd02064   83 ASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDVE 161

                        170
                 ....*....|....*....
gi 378976889 162 LAETLLGHPFSISGRVVHG 180
Cdd:cd02064  162 LANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 2-150 7.45e-78

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: 233.61  E-value: 7.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:pfam06574  10 VTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKEF 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976889   82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTA 150
Cdd:pfam06574  90 ASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 166-289 1.63e-60

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: 188.42  E-value: 1.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   166 LLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVtGLGDKPIAGVANIGTRPTVAGvRQQLEVHLLD 244
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 378976889   245 VVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELF 289
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-291 8.88e-164

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 456.92  E-value: 8.88e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:PRK05627  17 LTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPFDEEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:PRK05627  97 AKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAEGDLE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVANIGTRPTVAGVRQQLEVH 241
Cdd:PRK05627 177 LANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVANIGTRPTVDGGRQLLEVH 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 378976889 242 LLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFGL 291
Cdd:PRK05627 256 LLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 2-290 2.83e-157

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: 440.63  E-value: 2.83e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:COG0196   19 VTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTREF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:COG0196   99 AALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDVE 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVTgLGDKPIAGVANIGTRPTVAGVRQQLEV 240
Cdd:COG0196  179 EAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGVANIGTRPTFDGGEPTLEV 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 378976889 241 HLLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFG 290
Cdd:COG0196  258 HLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 2-290 3.32e-137

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: 389.11  E-value: 3.32e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPArLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:TIGR00083   2 LAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGgVRISSTAVRQALADDDLL 161
Cdd:TIGR00083  81 ANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  162 LAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEVH 241
Cdd:TIGR00083 160 LANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEVH 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 378976889  242 LLDVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELFG 290
Cdd:TIGR00083 240 LLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 2-180 5.61e-78

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: 234.74  E-value: 5.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:cd02064    3 VAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKEF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  82 AALTAQDFISELLVrRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDDLL 161
Cdd:cd02064   83 ASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDVE 161

                        170
                 ....*....|....*....
gi 378976889 162 LAETLLGHPFSISGRVVHG 180
Cdd:cd02064  162 LANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 2-150 7.45e-78

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: 233.61  E-value: 7.45e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLGYLAESGVDYVLCVRFDRRF 81
Cdd:pfam06574  10 VTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKEF 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976889   82 AALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTA 150
Cdd:pfam06574  90 ASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 167-289 5.73e-61

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: 189.51  E-value: 5.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889  167 LGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEVHLLDVV 246
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPEKLLPANGVYAVWVRVDGGKVYPGVANIGTNPTFGNGKLTVEVHILDFD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 378976889  247 MDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELF 289
Cdd:pfam01687  81 GDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 166-289 1.63e-60

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: 188.42  E-value: 1.63e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   166 LLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVtGLGDKPIAGVANIGTRPTVAGvRQQLEVHLLD 244
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 378976889   245 VVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARDELTARELF 289
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
PRK07143 PRK07143
hypothetical protein; Provisional
 4-124 6.49e-14

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 70.41  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   4 IGNFDGVHRGHQALLQRLREEGRQRglpVVVMIFEPQPLELFAADKaparLTRLREKLGYLAESGVDYVLCVRFDRRFAA 83
Cdd:PRK07143  21 LGGFESFHLGHLELFKKAKESNDEI---VIVIFKNPENLPKNTNKK----FSDLNSRLQTLANLGFKNIILLDFNEELQN 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 378976889  84 LTAQDFISELLvrRLGVQFLAVGDDFRFGAGRQGDFLLLQK 124
Cdd:PRK07143  94 LSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDLKE 132
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 2-153 7.61e-10

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: 56.29  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889   2 LTIGNFDGVHRGHQALLQRLREEGRQRglpVVVMIFEPQPLelfaaDKAPARLTRLREKLGYLAE--SGVDYVLCVRFDR 79
Cdd:cd02039    3 IIIGRFEPFHLGHLKLIKEALEEALDE---VIIIIVSNPPK-----KKRNKDPFSLHERVEMLKEilKDRLKVVPVDFPE 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378976889  80 RFAALTAQDFISELLvrRLGVQFLAVGDDFRFGAGRQGDFLLLQKagaEYGFDVTSTQTFcEGGVRISSTAVRQ 153
Cdd:cd02039   75 VKILLAVVFILKILL--KVGPDKVVVGEDFAFGKNASYNKDLKEL---FLDIEIVEVPRV-RDGKKISSTLIRE 142
PLN02940 PLN02940
riboflavin kinase
 165-281 1.81e-05

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 45.60  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889 165 TLLGHPFSISGRVVHGdeLGR---TIGFPTANLPLRR----QVSPVKGVYaVEVTGLGDKPIAG-VANIGTRPTVAGVRQ 236
Cdd:PLN02940 233 TLPIEPWHIGGPVIKG--FGRgskVLGIPTANLSTENysdvLSEHPSGVY-FGWAGLSTRGVYKmVMSIGWNPYFNNTEK 309

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 378976889 237 QLEVHLL-DVVMDLYGRHINVILRKKIRNEQRFASLDELKAQIARD 281
Cdd:PLN02940 310 TIEPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHED 355
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 2-153 4.30e-04

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: 39.61  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEGrqrGLPVVVMIFEPQPLELFAADKAPA--RLTRLReklgyLAEsGVDYVLCVRFDR 79
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELF---DEDLIVGVPSDEPPHKLKRPLFSAeeRLEMLE-----LAK-WVDEVIVVAPWE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378976889   80 rfaaltaqdfISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKagAEYGFDVTSTQTFCEGGVRISSTAVRQ 153
Cdd:pfam01467  72 ----------LTRELLKELNPDVLVIGADSLLDFWYELDEILGNV--KLVVVVRPVFFIPLKPTNGISSTDIRE 133
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 2-25 4.77e-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: 34.98  E-value: 4.77e-03
                          10        20
                  ....*....|....*....|....
gi 378976889    2 LTIGNFDGVHRGHQALLQRLREEG 25
Cdd:TIGR00125   3 IFVGTFDPFHLGHLDLLERAKELF 26
 
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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