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Conserved domains on  [gi|2090925029|gb|UAD18071|]
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bifunctional riboflavin kinase/FAD synthetase [Klebsiella quasipneumoniae]

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;
2-308 6.64e-171

bifunctional riboflavin kinase/FAD synthetase;


:

Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 475.79  E-value: 6.64e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029   2 KLIRGIHNLSQaPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYL 81
Cdd:PRK05627    1 QLIRGLHNIPQ-PPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  82 AESGVDYVLCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGV 161
Cdd:PRK05627   80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 162 RISSTAVRQALADDDLLLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVAN 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090925029 242 IGTRPTVAGVRQQLEVHLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFGL 308
Cdd:PRK05627  239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-308 6.64e-171

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 475.79  E-value: 6.64e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029   2 KLIRGIHNLSQaPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYL 81
Cdd:PRK05627    1 QLIRGLHNIPQ-PPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  82 AESGVDYVLCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGV 161
Cdd:PRK05627   80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 162 RISSTAVRQALADDDLLLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVAN 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090925029 242 IGTRPTVAGVRQQLEVHLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFGL 308
Cdd:PRK05627  239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-307 9.07e-168

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: 467.98  E-value: 9.07e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029   1 MKLIRGIHNLSQAPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSY 80
Cdd:COG0196     1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  81 LAESGVDYVLCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGG 160
Cdd:COG0196    81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 161 VRISSTAVRQALADDDLLLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVTgLGDKPIAGV 239
Cdd:COG0196   161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGV 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090925029 240 ANIGTRPTVAGVRQQLEVHLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFG 307
Cdd:COG0196   240 ANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 18-307 2.72e-138

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: 392.58  E-value: 2.72e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  18 VLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPArLTRLREKLSYLAESGVDYVLCVRFDRR 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  98 FAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGgVRISSTAVRQALADDDL 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 178 LLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEV 257
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2090925029 258 HLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFG 307
Cdd:TIGR00083 239 HLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 10-167 6.05e-82

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: 244.78  E-value: 6.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  10 LSQAPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYLAESGVDYV 89
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090925029  90 LCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTA 167
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 17-197 4.36e-80

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: 240.90  E-value: 4.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  17 CVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYLAESGVDYVLCVRFDR 96
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  97 RFAALTAQDFISELLVrRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDD 176
Cdd:cd02064    81 EFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159

                         170       180
                  ....*....|....*....|.
gi 2090925029 177 LLLAETLLGHPFSISGRVVHG 197
Cdd:cd02064   160 VELANELLGRPYSIEGRVVHG 180
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 183-306 9.18e-61

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: 189.57  E-value: 9.18e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  183 LLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVtGLGDKPIAGVANIGTRPTVAGvRQQLEVHLLD 261
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2090925029  262 VVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELF 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-308 6.64e-171

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 475.79  E-value: 6.64e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029   2 KLIRGIHNLSQaPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYL 81
Cdd:PRK05627    1 QLIRGLHNIPQ-PPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  82 AESGVDYVLCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGV 161
Cdd:PRK05627   80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 162 RISSTAVRQALADDDLLLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTgLGDKPIAGVAN 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2090925029 242 IGTRPTVAGVRQQLEVHLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFGL 308
Cdd:PRK05627  239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-307 9.07e-168

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: 467.98  E-value: 9.07e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029   1 MKLIRGIHNLSQAPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSY 80
Cdd:COG0196     1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  81 LAESGVDYVLCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGG 160
Cdd:COG0196    81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 161 VRISSTAVRQALADDDLLLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVTgLGDKPIAGV 239
Cdd:COG0196   161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGV 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090925029 240 ANIGTRPTVAGVRQQLEVHLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFG 307
Cdd:COG0196   240 ANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 18-307 2.72e-138

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: 392.58  E-value: 2.72e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  18 VLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPArLTRLREKLSYLAESGVDYVLCVRFDRR 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  98 FAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGgVRISSTAVRQALADDDL 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 178 LLAETLLGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEV 257
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2090925029 258 HLLDVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELFG 307
Cdd:TIGR00083 239 HLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 10-167 6.05e-82

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: 244.78  E-value: 6.05e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  10 LSQAPHGCVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYLAESGVDYV 89
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2090925029  90 LCVRFDRRFAALTAQDFISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTA 167
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 17-197 4.36e-80

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: 240.90  E-value: 4.36e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  17 CVLTIGNFDGVHRGHQALLQRLREEGRQRGLPVVVMIFEPQPLELFAADKAPARLTRLREKLSYLAESGVDYVLCVRFDR 96
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  97 RFAALTAQDFISELLVrRLGVQFLAVGDDFRFGAGRQGDFLLLQKAGAEYGFDVTSTQTFCEGGVRISSTAVRQALADDD 176
Cdd:cd02064    81 EFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159

                         170       180
                  ....*....|....*....|.
gi 2090925029 177 LLLAETLLGHPFSISGRVVHG 197
Cdd:cd02064   160 VELANELLGRPYSIEGRVVHG 180
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 184-306 5.68e-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: 189.90  E-value: 5.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 184 LGHPFSISGRVVHGDELGRTIGFPTANLPLRRQVSPVKGVYAVEVTGLGDKPIAGVANIGTRPTVAGVRQQLEVHLLDVV 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPEKLLPANGVYAVWVRVDGGKVYPGVANIGTNPTFGNGKLTVEVHILDFD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2090925029 264 MDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELF 306
Cdd:pfam01687  81 GDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 183-306 9.18e-61

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: 189.57  E-value: 9.18e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  183 LLGHPFSISGRVVHGDELGRTIGFPTANLPL-RRQVSPVKGVYAVEVtGLGDKPIAGVANIGTRPTVAGvRQQLEVHLLD 261
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2090925029  262 VVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARDELTARELF 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
PRK07143 PRK07143
hypothetical protein; Provisional
 21-141 4.95e-14

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 70.80  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  21 IGNFDGVHRGHQALLQRLREEGRQRglpVVVMIFEPQPLELFAADKaparLTRLREKLSYLAESGVDYVLCVRFDRRFAA 100
Cdd:PRK07143   21 LGGFESFHLGHLELFKKAKESNDEI---VIVIFKNPENLPKNTNKK----FSDLNSRLQTLANLGFKNIILLDFNEELQN 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2090925029 101 LTAQDFISELLvrRLGVQFLAVGDDFRFGAGRQGDFLLLQK 141
Cdd:PRK07143   94 LSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDLKE 132
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 18-170 1.92e-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: 58.22  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  18 VLTIGNFDGVHRGHQALLQRLREEGRQRglpVVVMIFEPQPLelfaaDKAPARLTRLREKLSYLAE--SGVDYVLCVRFD 95
Cdd:cd02039     2 GIIIGRFEPFHLGHLKLIKEALEEALDE---VIIIIVSNPPK-----KKRNKDPFSLHERVEMLKEilKDRLKVVPVDFP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2090925029  96 RRFAALTAQDFISELLvrRLGVQFLAVGDDFRFGAGRQGDFLLLQKagaEYGFDVTSTQTFcEGGVRISSTAVRQ 170
Cdd:cd02039    74 EVKILLAVVFILKILL--KVGPDKVVVGEDFAFGKNASYNKDLKEL---FLDIEIVEVPRV-RDGKKISSTLIRE 142
PLN02940 PLN02940
riboflavin kinase
 182-298 1.69e-05

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 45.98  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029 182 TLLGHPFSISGRVVHGdeLGR---TIGFPTANLPLRR----QVSPVKGVYaVEVTGLGDKPIAG-VANIGTRPTVAGVRQ 253
Cdd:PLN02940  233 TLPIEPWHIGGPVIKG--FGRgskVLGIPTANLSTENysdvLSEHPSGVY-FGWAGLSTRGVYKmVMSIGWNPYFNNTEK 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2090925029 254 QLEVHLL-DVVMDLYGRHINVVLRKKIRNEQRFASLDELKAQIARD 298
Cdd:PLN02940  310 TIEPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHED 355
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 19-170 4.63e-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: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090925029  19 LTIGNFDGVHRGHQALLQRLREEGrqrGLPVVVMIFEPQPLELFAADKAPA--RLTRLReklsyLAEsGVDYVLCVRFDR 96
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELF---DEDLIVGVPSDEPPHKLKRPLFSAeeRLEMLE-----LAK-WVDEVIVVAPWE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090925029  97 rfaaltaqdfISELLVRRLGVQFLAVGDDFRFGAGRQGDFLLLQKagAEYGFDVTSTQTFCEGGVRISSTAVRQ 170
Cdd:pfam01467  72 ----------LTRELLKELNPDVLVIGADSLLDFWYELDEILGNV--KLVVVVRPVFFIPLKPTNGISSTDIRE 133
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 17-42 1.04e-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: 36.90  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*.
gi 2090925029  17 CVLTIGNFDGVHRGHQALLQRLREEG 42
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF 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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