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Conserved domains on  [gi|495139333|ref|WP_007864140|]
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MULTISPECIES: bifunctional riboflavin kinase/FAD synthetase [Cronobacter]

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

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 4.64e-179

bifunctional riboflavin kinase/FAD synthetase;


:

Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 496.59  E-value: 4.64e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   2 KLIRGIHNLTSEHHgCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYL 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  82 ARCGVDYVLCIRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 162 RISSTAVRQALAQDDLSLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLgISDKPLPGVAN 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495139333 242 IGTRPTVAGLRQQLEVHLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFGL 308
Cdd:PRK05627 239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-308 4.64e-179

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 496.59  E-value: 4.64e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   2 KLIRGIHNLTSEHHgCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYL 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  82 ARCGVDYVLCIRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 162 RISSTAVRQALAQDDLSLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLgISDKPLPGVAN 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495139333 242 IGTRPTVAGLRQQLEVHLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFGL 308
Cdd:PRK05627 239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-307 2.20e-177

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: 492.25  E-value: 2.20e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   1 MKLIRGIHNLTSEHHGCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRY 80
Cdd:COG0196    1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  81 LARCGVDYVLCIRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEG 160
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 161 VRISSTAVRQALAQDDLSLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPL-RRQVSPVKGVYAVEVLgISDKPLPGV 239
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGV 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495139333 240 ANIGTRPTVAGLRQQLEVHLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFG 307
Cdd:COG0196  240 ANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-307 1.34e-148

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: 418.77  E-value: 1.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   18 VLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPArLTRLREKLRYLARCGVDYVLCIRFDRR 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   98 FAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEgVRISSTAVRQALAQDDL 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  178 SLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLGISDKPLPGVANIGTRPTVAGLRQQLEV 257
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 495139333  258 HLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFG 307
Cdd:TIGR00083 239 HLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
17-197 6.00e-87

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: 258.24  E-value: 6.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  17 CVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYLARCGVDYVLCIRFDR 96
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  97 RFAALTAQNFVSDLLVErLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGVRISSTAVRQALAQDD 176
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 495139333 177 LSLAENLLGRPFAISGRVVHG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
12-167 2.12e-81

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: 243.24  E-value: 2.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   12 SEHHGCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYLARCGVDYVLC 91
Cdd:pfam06574   3 EDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495139333   92 IRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGVRISSTA 167
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
183-306 3.31e-63

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: 195.73  E-value: 3.31e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   183 LLGRPFAISGRVVHGDALGRTIGFPTANLPL-RRQVSPVKGVYAVEVlGISDKPLPGVANIGTRPTVAGlRQQLEVHLLD 261
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 495139333   262 VAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFF 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-308 4.64e-179

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 496.59  E-value: 4.64e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   2 KLIRGIHNLTSEHHgCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYL 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  82 ARCGVDYVLCIRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 162 RISSTAVRQALAQDDLSLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLgISDKPLPGVAN 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVRVK-VDGKPYPGVAN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495139333 242 IGTRPTVAGLRQQLEVHLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFGL 308
Cdd:PRK05627 239 IGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-307 2.20e-177

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: 492.25  E-value: 2.20e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   1 MKLIRGIHNLTSEHHGCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRY 80
Cdd:COG0196    1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  81 LARCGVDYVLCIRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEG 160
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 161 VRISSTAVRQALAQDDLSLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPL-RRQVSPVKGVYAVEVLgISDKPLPGV 239
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALpEEKLLPADGVYAVRVR-IDGRRYPGV 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495139333 240 ANIGTRPTVAGLRQQLEVHLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFG 307
Cdd:COG0196  240 ANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-307 1.34e-148

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: 418.77  E-value: 1.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   18 VLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPArLTRLREKLRYLARCGVDYVLCIRFDRR 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   98 FAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEgVRISSTAVRQALAQDDL 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQD-IRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  178 SLAENLLGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLGISDKPLPGVANIGTRPTVAGLRQQLEV 257
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 495139333  258 HLLDVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFG 307
Cdd:TIGR00083 239 HLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
17-197 6.00e-87

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: 258.24  E-value: 6.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  17 CVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYLARCGVDYVLCIRFDR 96
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  97 RFAALTAQNFVSDLLVErLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGVRISSTAVRQALAQDD 176
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 495139333 177 LSLAENLLGRPFAISGRVVHG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
12-167 2.12e-81

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: 243.24  E-value: 2.12e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   12 SEHHGCVLTIGNFDGVHRGHQALLAGLCAQGRERGLPVMVMIFEPQPLELFAADKAPARLTRLREKLRYLARCGVDYVLC 91
Cdd:pfam06574   3 EDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495139333   92 IRFDRRFAALTAQNFVSDLLVERLGVKFLATGDDFRFGAGREGDFLLLQKAGREYGFEVTSTQTFCEEGVRISSTA 167
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
183-306 3.31e-63

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: 195.73  E-value: 3.31e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333   183 LLGRPFAISGRVVHGDALGRTIGFPTANLPL-RRQVSPVKGVYAVEVlGISDKPLPGVANIGTRPTVAGlRQQLEVHLLD 261
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLdDRLLLPKNGVYAVRV-RVDGKIYPGVANIGTRPTFGG-DRSVEVHILD 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 495139333   262 VAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFF 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
184-306 5.21e-62

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: 192.59  E-value: 5.21e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  184 LGRPFAISGRVVHGDALGRTIGFPTANLPLRRQVSPVKGVYAVEVLGISDKPLPGVANIGTRPTVAGLRQQLEVHLLDVA 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPEKLLPANGVYAVWVRVDGGKVYPGVANIGTNPTFGNGKLTVEVHILDFD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 495139333  264 IDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFF 306
Cdd:pfam01687  81 GDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
PRK07143 PRK07143
hypothetical protein; Provisional
21-306 2.05e-11

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 63.10  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  21 IGNFDGVHRGHQALLAGLCAQGRERglpVMVMIFEPQPLELFAADKaparLTRLREKLRYLARCGVDYVLCIRFDRRFAA 100
Cdd:PRK07143  21 LGGFESFHLGHLELFKKAKESNDEI---VIVIFKNPENLPKNTNKK----FSDLNSRLQTLANLGFKNIILLDFNEELQN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 101 LTAQNFVSDLLveRLGVKFLATGDDFRFGAGREGDFLLLQkagrEYGFEVTSTQTFCEEGVRISSTAVRQALAQDDLSLA 180
Cdd:PRK07143  94 LSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDLK----EYFPNVHIVEILKINQQKISTSLLKEFIEFGDIELL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 181 ENLLGRPFAISGRVVHgdalgrtigfpTANLPLRRQVSPVK-GVYAVEVLgISDKPLPGVANIgtrptvaGLRQQLEVHL 259
Cdd:PRK07143 168 NSLLLYNYSISITINK-----------NFEFTYPQNIIKLHaGIYLAYVV-INNFKYHGILKI-------NFNNKNKIKF 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 495139333 260 LDVA-IDLYGRHIDVVLRKKIR--NEQRFASLDElkaqiaRDVITARDFF 306
Cdd:PRK07143 229 FDFDlIINKYQEIFIEIVKEIRiiSSNEDNNILN------DDIEIAKKFF 272
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
18-171 1.90e-09

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: 55.14  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333  18 VLTIGNFDGVHRGHQALLAGLCAQGRERglpVMVMIFEPQPLelfaaDKAPARLTRLREKLRYLARCG--VDYVLCIRFD 95
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEEALDE---VIIIIVSNPPK-----KKRNKDPFSLHERVEMLKEILkdRLKVVPVDFP 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495139333  96 RRFAALTAQNFVSDLLveRLGVKFLATGDDFRFGAGREGDFLLLQKagrEYGFEVTSTQTFcEEGVRISSTAVRQA 171
Cdd:cd02039   74 EVKILLAVVFILKILL--KVGPDKVVVGEDFAFGKNASYNKDLKEL---FLDIEIVEVPRV-RDGKKISSTLIREL 143
PLN02940 PLN02940
riboflavin kinase
187-310 3.42e-05

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 44.82  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495139333 187 PFAISGRVVHGDALG-RTIGFPTANLPLRR----QVSPVKGVYaVEVLGISDKPL-PGVANIGTRPTVAGLRQQLEVHLL 260
Cdd:PLN02940 238 PWHIGGPVIKGFGRGsKVLGIPTANLSTENysdvLSEHPSGVY-FGWAGLSTRGVyKMVMSIGWNPYFNNTEKTIEPWLL 316
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495139333 261 -DVAIDLYGRHIDVVLRKKIRNEQRFASLDELKAQIARDVITARDFFGLPT 310
Cdd:PLN02940 317 hDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPL 367
 
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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