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Conserved domains on  [gi|2484452365|gb|WFT76779|]
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bifunctional riboflavin kinase/FAD synthetase [Halobacillus naozhouensis]

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

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 ...
1-311 9.81e-149

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: 419.83  E-value: 9.81e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365   1 MKTIELSESLPKHdlhLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvQHARYITPLSE 80
Cdd:COG0196     1 MKIIRGLSELPAD---LRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  81 KEDILDGMGIDYLFVVRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRI 158
Cdd:COG0196    77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVdKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYgFEVEVVPPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 159 DQDHTKVSSTRIRELLKEGNVSAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITDMEEQYVPKTGVYAVTVGYQGERY 238
Cdd:COG0196   157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRY 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484452365 239 YGMANLGVKPTFqpEGSNPALEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:COG0196   237 PGVANIGTRPTF--DGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-311 9.81e-149

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: 419.83  E-value: 9.81e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365   1 MKTIELSESLPKHdlhLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvQHARYITPLSE 80
Cdd:COG0196     1 MKIIRGLSELPAD---LRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  81 KEDILDGMGIDYLFVVRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRI 158
Cdd:COG0196    77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVdKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYgFEVEVVPPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 159 DQDHTKVSSTRIRELLKEGNVSAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITDMEEQYVPKTGVYAVTVGYQGERY 238
Cdd:COG0196   157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRY 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484452365 239 YGMANLGVKPTFqpEGSNPALEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:COG0196   237 PGVANIGTRPTF--DGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
13-310 2.98e-131

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 375.26  E-value: 2.98e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  13 HDLHLEP-SSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKVQHARyITPLSEKEDILDGMGID 91
Cdd:PRK05627    7 HNIPQPPdCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPAR-LTPLRDKAELLAELGVD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  92 YLFVVRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRIDQDHTKVSSTR 169
Cdd:PRK05627   86 YVLVLPFDEEFAKLSAEEFIEDLLVkGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFgFEVTIVPEVKEDGERVSSTA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 170 IRELLKEGNVSAVNELLGREFNVEGTVVPGDRRGRTIGYPTANItDMEEQYVPKTGVYAVTVGYQGERYYGMANLGVKPT 249
Cdd:PRK05627  166 IRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANL-PLPDRVLPADGVYAVRVKVDGKPYPGVANIGTRPT 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2484452365 250 FqpEGSNPALEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYF 310
Cdd:PRK05627  245 V--DGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFL 303
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
21-311 1.98e-95

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: 283.95  E-value: 1.98e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  21 SVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvqHARYITPLSEKEDILDGMGIDYLFVVRFDQ 100
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWL--TAPALTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 101 SLAALPPDQFVDEYFVG-LNIKHVVAGFDFSYGHKGKGSMETLPQHAKGRLTYTVVDRIDQDHTKVSSTRIRELLKEGNV 179
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 180 SAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITdMEEQYVP-KTGVYAVTVGYQGERYYGMANLGVKPTFqpEGSNPA 258
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIK-LKNQVLPlKGGYYVVVVLLNGEPYPGVGNIGNRPTF--IGQQLV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2484452365 259 LEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
20-199 1.31e-76

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: 232.04  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  20 SSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvQHARYITPLSEKEDILDGMGIDYLFVVRFD 99
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPD-KAPPRLTTLEEKLELLESLGVDYLLVLPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 100 QSLAALPPDQFVDEYFVGLNIKHVVAGFDFSYGHKGKGSMETLPQHAKgRLTYTV--VDRIDQDHTKVSSTRIRELLKEG 177
Cdd:cd02064    80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGK-KYGFEVtvVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 2484452365 178 NVSAVNELLGREFNVEGTVVPG 199
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
16-169 3.45e-60

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: 189.31  E-value: 3.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  16 HLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKVQHARyITPLSEKEDILDGMGIDYLFV 95
Cdd:pfam06574   4 DLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFR-LTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2484452365  96 VRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRIDQDHTKVSSTR 169
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVdGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLgFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
185-311 9.89e-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: 186.88  E-value: 9.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  185 LLGREFNVEGTVVPGDRRGRTIGYPTANITDMEEQYVPKTGVYAVTVGYQGERYYGMANLGVKPTFqpeGSNPALEVHVF 264
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTF---GGDRSVEVHIL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2484452365  265 DFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
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 ...
1-311 9.81e-149

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: 419.83  E-value: 9.81e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365   1 MKTIELSESLPKHdlhLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvQHARYITPLSE 80
Cdd:COG0196     1 MKIIRGLSELPAD---LRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  81 KEDILDGMGIDYLFVVRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRI 158
Cdd:COG0196    77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVdKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYgFEVEVVPPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 159 DQDHTKVSSTRIRELLKEGNVSAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITDMEEQYVPKTGVYAVTVGYQGERY 238
Cdd:COG0196   157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRY 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484452365 239 YGMANLGVKPTFqpEGSNPALEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:COG0196   237 PGVANIGTRPTF--DGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
13-310 2.98e-131

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 375.26  E-value: 2.98e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  13 HDLHLEP-SSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKVQHARyITPLSEKEDILDGMGID 91
Cdd:PRK05627    7 HNIPQPPdCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPAR-LTPLRDKAELLAELGVD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  92 YLFVVRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRIDQDHTKVSSTR 169
Cdd:PRK05627   86 YVLVLPFDEEFAKLSAEEFIEDLLVkGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFgFEVTIVPEVKEDGERVSSTA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 170 IRELLKEGNVSAVNELLGREFNVEGTVVPGDRRGRTIGYPTANItDMEEQYVPKTGVYAVTVGYQGERYYGMANLGVKPT 249
Cdd:PRK05627  166 IRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANL-PLPDRVLPADGVYAVRVKVDGKPYPGVANIGTRPT 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2484452365 250 FqpEGSNPALEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYF 310
Cdd:PRK05627  245 V--DGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFL 303
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
21-311 1.98e-95

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: 283.95  E-value: 1.98e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  21 SVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvqHARYITPLSEKEDILDGMGIDYLFVVRFDQ 100
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWL--TAPALTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 101 SLAALPPDQFVDEYFVG-LNIKHVVAGFDFSYGHKGKGSMETLPQHAKGRLTYTVVDRIDQDHTKVSSTRIRELLKEGNV 179
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 180 SAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITdMEEQYVP-KTGVYAVTVGYQGERYYGMANLGVKPTFqpEGSNPA 258
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIK-LKNQVLPlKGGYYVVVVLLNGEPYPGVGNIGNRPTF--IGQQLV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2484452365 259 LEVHVFDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
20-199 1.31e-76

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: 232.04  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  20 SSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKvQHARYITPLSEKEDILDGMGIDYLFVVRFD 99
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPD-KAPPRLTTLEEKLELLESLGVDYLLVLPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 100 QSLAALPPDQFVDEYFVGLNIKHVVAGFDFSYGHKGKGSMETLPQHAKgRLTYTV--VDRIDQDHTKVSSTRIRELLKEG 177
Cdd:cd02064    80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGK-KYGFEVtvVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 2484452365 178 NVSAVNELLGREFNVEGTVVPG 199
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
16-169 3.45e-60

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: 189.31  E-value: 3.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  16 HLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLGIQTAVMTFDPHPSVVLNKKVQHARyITPLSEKEDILDGMGIDYLFV 95
Cdd:pfam06574   4 DLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFR-LTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2484452365  96 VRFDQSLAALPPDQFVDEYFV-GLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGR-LTYTVVDRIDQDHTKVSSTR 169
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVdGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLgFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
185-311 9.89e-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: 186.88  E-value: 9.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  185 LLGREFNVEGTVVPGDRRGRTIGYPTANITDMEEQYVPKTGVYAVTVGYQGERYYGMANLGVKPTFqpeGSNPALEVHVF 264
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTF---GGDRSVEVHIL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2484452365  265 DFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYFE 311
Cdd:smart00904  78 DFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
186-310 1.43e-54

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: 173.72  E-value: 1.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 186 LGREFNVEGTVVPGDRRGRTIGYPTANItDMEEQYVPKTGVYAVTVGYQG-ERYYGMANLGVKPTFqpEGSNPALEVHVF 264
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANL-PLPEKLLPANGVYAVWVRVDGgKVYPGVANIGTNPTF--GNGKLTVEVHIL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2484452365 265 DFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEKEIRRYF 310
Cdd:pfam01687  78 DFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
PRK07143 PRK07143
hypothetical protein; Provisional
1-269 5.13e-18

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 82.36  E-value: 5.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365   1 MKTIELSESLPKhdlhLEPSSVAVGFFDGVHKGHQEVIRTAQDRARKLgiqtAVMTF-DPHPSVVLNKKV---QHARYit 76
Cdd:PRK07143    2 MKVYTFPLKNFK----FEKPTFVLGGFESFHLGHLELFKKAKESNDEI----VIVIFkNPENLPKNTNKKfsdLNSRL-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  77 plsekeDILDGMGIDYLFVVRFDQSLAALPPDQFVDEyFVGLNIKHVVAGFDFSYGHKGKGSMETLPQHAKGrlTYtVVD 156
Cdd:PRK07143   72 ------QTLANLGFKNIILLDFNEELQNLSGNDFIEK-LTKNQVSFFVVGKDFRFGKNASWNADDLKEYFPN--VH-IVE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 157 RIDQDHTKVSSTRIRELLKEGNVSAVNELLGREFNVEGTVVpgdrRGRTIGYPTaNITDmeeqyvPKTGVYAVTVGYQGE 236
Cdd:PRK07143  142 ILKINQQKISTSLLKEFIEFGDIELLNSLLLYNYSISITIN----KNFEFTYPQ-NIIK------LHAGIYLAYVVINNF 210
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2484452365 237 RYYGmanlgvkpTFQPEGSNPAlEVHVFDFDDD 269
Cdd:PRK07143  211 KYHG--------ILKINFNNKN-KIKFFDFDLI 234
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
22-173 1.58e-06

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: 47.05  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365  22 VAVGFFDGVHKGHQEVIRTAQDRARKLGIqtaVMTFDPHPSVVLNKKVqhARYITPLSEKEDILdgMGIDYLFVVRFDQS 101
Cdd:cd02039     3 IIIGRFEPFHLGHLKLIKEALEEALDEVI---IIIVSNPPKKKRNKDP--FSLHERVEMLKEIL--KDRLKVVPVDFPEV 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484452365 102 LAALPPDqFVDEYFVGLNIKHVVAGFDFSYGHKGKGSMETLpqhAKGRLTYTVVDRIDQDHTKVSSTRIREL 173
Cdd:cd02039    76 KILLAVV-FILKILLKVGPDKVVVGEDFAFGKNASYNKDLK---ELFLDIEIVEVPRVRDGKKISSTLIREL 143
PLN02940 PLN02940
riboflavin kinase
194-304 3.21e-05

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 45.21  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484452365 194 GTVVPGDRRG-RTIGYPTANItdmeeqyvPKTGVYAVTVGYQGERYYGMANL---GVKPTFQPEGSNP-------ALE-- 260
Cdd:PLN02940  243 GPVIKGFGRGsKVLGIPTANL--------STENYSDVLSEHPSGVYFGWAGLstrGVYKMVMSIGWNPyfnntekTIEpw 314
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2484452365 261 -VHvfDFDDDLYGTRIKVFFHQFIRDEQKFDGVEEVTAQLHTDEK 304
Cdd:PLN02940  315 lLH--DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRR 357
Sugar-bind pfam04198
Putative sugar-binding domain; This probable domain is found in bacterial transcriptional ...
170-218 8.27e-04

Putative sugar-binding domain; This probable domain is found in bacterial transcriptional regulators such as DeoR and SorC. These proteins have an amino-terminal helix-turn-helix pfam00325 that binds to DNA. This domain is probably the ligand regulator binding region. SorC is regulated by sorbose and other members of this family are likely to be regulated by other sugar substrates.


Pssm-ID: 427778  Cd Length: 256  Bit Score: 40.30  E-value: 8.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2484452365 170 IRELLKEGnvsAVNELLGREFNVEGTVVPGDRRGRTIGYPTANITDMEE 218
Cdd:pfam04198 173 LAELRELG---AVGEIFGRFFDAEGRVVDTALNERVIGLDLEDLRDIPN 218
 
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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