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Conserved domains on  [gi|581975924|gb|EVT75890|]
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riboflavin biosynthesis protein RibF [Staphylococcus aureus M1557]

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 ...
1-312 3.88e-138

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: 393.25  E-value: 3.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   1 MKVIEVTHPIQSKQyitEDVAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKrKRTTYLTPLSD 80
Cdd:COG0196    1 MKIIRGLSELPADL---RGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  81 KTEKISQHDIDYCIVVNFSSRFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQ 156
Cdd:COG0196   77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKlGAKHVVVGDDFRFGKGRAGDVELLRELGEeygFEVEVVPPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 157 EIENEKISTTSIRQDLINGELQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGteNK 236
Cdd:COG0196  157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRID--GR 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581975924 237 LYRGVANIGVKPTFHDPnkaEVVIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:COG0196  235 RYPGVANIGTRPTFDGG---EPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-312 3.88e-138

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: 393.25  E-value: 3.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   1 MKVIEVTHPIQSKQyitEDVAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKrKRTTYLTPLSD 80
Cdd:COG0196    1 MKIIRGLSELPADL---RGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  81 KTEKISQHDIDYCIVVNFSSRFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQ 156
Cdd:COG0196   77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKlGAKHVVVGDDFRFGKGRAGDVELLRELGEeygFEVEVVPPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 157 EIENEKISTTSIRQDLINGELQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGteNK 236
Cdd:COG0196  157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRID--GR 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581975924 237 LYRGVANIGVKPTFHDPnkaEVVIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:COG0196  235 RYPGVANIGTRPTFDGG---EPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
21-313 8.79e-124

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 356.77  E-value: 8.79e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  21 AMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPkRKRTTYLTPLSDKTEKISQHDIDYCIVVNFSS 100
Cdd:PRK05627  16 VLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAP-DKAPARLTPLRDKAELLAELGVDYVLVLPFDE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 101 RFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTTSIRQDLINGE 176
Cdd:PRK05627  95 EFAKLSAEEFIEDLLVKGlNAKHVVVGFDFRFGKKRAGDFELLKEAGKefgFEVTIVPEVKEDGERVSSTAIRQALAEGD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 177 LQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPsDDYLLPRKGVYAVSIEIGteNKLYRGVANIGVKPTFHDPNKA 256
Cdd:PRK05627 175 LELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL-PDRVLPADGVYAVRVKVD--GKPYPGVANIGTRPTVDGGRQL 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 581975924 257 evvIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLAV 313
Cdd:PRK05627 252 ---LEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
21-312 1.92e-89

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: 268.93  E-value: 1.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   21 AMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNpkRKRTTYLTPLSDKTEKISQHDIDYCIVVNFSS 100
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFN--WLTAPALTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  101 RFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQeyDAFNTTI----VSKQEIENEKISTTSIRQDLING 175
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKHlHVKFLVVGDDFRFGHDRQGDFLLLQ--LFGNTTIfcviVKQLFCQDIRISSSAIRQALKNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  176 ELQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGTENklYRGVANIGVKPTFhdpNK 255
Cdd:TIGR00083 157 DLELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEP--YPGVGNIGNRPTF---IG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581975924  256 AEVVIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:TIGR00083 232 QQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
20-197 3.22e-71

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: 218.56  E-value: 3.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  20 VAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKRKRTtYLTPLSDKTEKISQHDIDYCIVVNFS 99
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPP-RLTTLEEKLELLESLGVDYLLVLPFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 100 SRFANVSVEDFVENYIIKNNVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTTSIRQDLINGE 176
Cdd:cd02064   80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKkygFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 581975924 177 LQKANDALGYIYSIKGTVVQG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
16-166 1.21e-63

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: 198.56  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   16 ITEDVAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKRKRTTyLTPLSDKTEKISQHDIDYCIV 95
Cdd:pfam06574   4 DLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFR-LTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581975924   96 VNFSSRFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTT 166
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVDGlNVKHVVVGFDFRFGKGRKGDVELLKELGAklgFEVTIVPPVELDGEKISST 157
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-312 1.75e-58

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: 184.18  E-value: 1.75e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   184 LGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGteNKLYRGVANIGVKPTFHDpnkaEVVIEVN 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVD--GKIYPGVANIGTRPTFGG----DRSVEVH 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 581975924   264 IFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:smart00904  76 ILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-312 3.88e-138

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: 393.25  E-value: 3.88e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   1 MKVIEVTHPIQSKQyitEDVAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKrKRTTYLTPLSD 80
Cdd:COG0196    1 MKIIRGLSELPADL---RGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPD-KAPKLLTTLEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  81 KTEKISQHDIDYCIVVNFSSRFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQ 156
Cdd:COG0196   77 KLELLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKlGAKHVVVGDDFRFGKGRAGDVELLRELGEeygFEVEVVPPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 157 EIENEKISTTSIRQDLINGELQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGteNK 236
Cdd:COG0196  157 TIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRID--GR 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 581975924 237 LYRGVANIGVKPTFHDPnkaEVVIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:COG0196  235 RYPGVANIGTRPTFDGG---EPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
21-313 8.79e-124

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 356.77  E-value: 8.79e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  21 AMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPkRKRTTYLTPLSDKTEKISQHDIDYCIVVNFSS 100
Cdd:PRK05627  16 VLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAP-DKAPARLTPLRDKAELLAELGVDYVLVLPFDE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 101 RFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTTSIRQDLINGE 176
Cdd:PRK05627  95 EFAKLSAEEFIEDLLVKGlNAKHVVVGFDFRFGKKRAGDFELLKEAGKefgFEVTIVPEVKEDGERVSSTAIRQALAEGD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 177 LQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPsDDYLLPRKGVYAVSIEIGteNKLYRGVANIGVKPTFHDPNKA 256
Cdd:PRK05627 175 LELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL-PDRVLPADGVYAVRVKVD--GKPYPGVANIGTRPTVDGGRQL 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 581975924 257 evvIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLAV 313
Cdd:PRK05627 252 ---LEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
21-312 1.92e-89

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: 268.93  E-value: 1.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   21 AMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNpkRKRTTYLTPLSDKTEKISQHDIDYCIVVNFSS 100
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFN--WLTAPALTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  101 RFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQeyDAFNTTI----VSKQEIENEKISTTSIRQDLING 175
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKHlHVKFLVVGDDFRFGHDRQGDFLLLQ--LFGNTTIfcviVKQLFCQDIRISSSAIRQALKNG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  176 ELQKANDALGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGTENklYRGVANIGVKPTFhdpNK 255
Cdd:TIGR00083 157 DLELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEP--YPGVGNIGNRPTF---IG 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581975924  256 AEVVIEVNIFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:TIGR00083 232 QQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
20-197 3.22e-71

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: 218.56  E-value: 3.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  20 VAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKRKRTtYLTPLSDKTEKISQHDIDYCIVVNFS 99
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPP-RLTTLEEKLELLESLGVDYLLVLPFD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 100 SRFANVSVEDFVENYIIKNNVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTTSIRQDLINGE 176
Cdd:cd02064   80 KEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGDAELLKELGKkygFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 581975924 177 LQKANDALGYIYSIKGTVVQG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
16-166 1.21e-63

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: 198.56  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   16 ITEDVAMAFGFFDGMHKGHDKVFDILNEIAEARSLKKAVMTFDPHPSVVLNPKRKRTTyLTPLSDKTEKISQHDIDYCIV 95
Cdd:pfam06574   4 DLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFR-LTTLEEKIELLAELGVDYLLV 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 581975924   96 VNFSSRFANVSVEDFVENYIIKN-NVKEVIAGFDFTFGKFGKGNMTVLQEYDA---FNTTIVSKQEIENEKISTT 166
Cdd:pfam06574  83 LPFTKEFASLSAEEFIENVLVDGlNVKHVVVGFDFRFGKGRKGDVELLKELGAklgFEVTIVPPVELDGEKISST 157
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-312 1.75e-58

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: 184.18  E-value: 1.75e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924   184 LGYIYSIKGTVVQGEKRGRTIGFPTANIQPSDDYLLPRKGVYAVSIEIGteNKLYRGVANIGVKPTFHDpnkaEVVIEVN 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVD--GKIYPGVANIGTRPTFGG----DRSVEVH 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 581975924   264 IFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLLA 312
Cdd:smart00904  76 ILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
184-311 1.04e-56

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: 179.50  E-value: 1.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  184 LGYIYSIKGTVVQGEKRGRTIGFPTANIQPsDDYLLPRKGVYAVSIEIGTEnKLYRGVANIGVKPTFHDPNKAevvIEVN 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPL-PEKLLPANGVYAVWVRVDGG-KVYPGVANIGTNPTFGNGKLT---VEVH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 581975924  264 IFDFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLL 311
Cdd:pfam01687  76 ILDFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
PRK07143 PRK07143
hypothetical protein; Provisional
13-274 6.19e-21

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 90.44  E-value: 6.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  13 KQYITEDVAMAFGFFDGMHKGHDKVFdilnEIAEARSLKKAVMTFDpHPSvvlNPKRKRTTYLTPLSDKTEKISQHDIDY 92
Cdd:PRK07143  10 KNFKFEKPTFVLGGFESFHLGHLELF----KKAKESNDEIVIVIFK-NPE---NLPKNTNKKFSDLNSRLQTLANLGFKN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  93 CIVVNFSSRFANVSVEDFVENyIIKNNVKEVIAGFDFTFGKFGKGNMTVLQEYDAfNTTIVSKQEIENEKISTTSIRQDL 172
Cdd:PRK07143  82 IILLDFNEELQNLSGNDFIEK-LTKNQVSFFVVGKDFRFGKNASWNADDLKEYFP-NVHIVEILKINQQKISTSLLKEFI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 173 INGELQKANDALGYIYSIKGTVVqgekrgRTIGFPT-ANIQPsddyllPRKGVYAVSIEIGteNKLYRGVANIGvkptFH 251
Cdd:PRK07143 160 EFGDIELLNSLLLYNYSISITIN------KNFEFTYpQNIIK------LHAGIYLAYVVIN--NFKYHGILKIN----FN 221
                        250       260
                 ....*....|....*....|...
gi 581975924 252 DPNKaevvIEVNIFDFEDNIYGE 274
Cdd:PRK07143 222 NKNK----IKFFDFDLIINKYQE 240
PLN02940 PLN02940
riboflavin kinase
190-311 4.40e-07

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 50.99  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924 190 IKGTVVQGEKRG-RTIGFPTANIqPSDDY--LLPR--KGVYAVSIEIGTENkLYRGVANIGVKPTFhdpNKAEVVIEVNI 264
Cdd:PLN02940 241 IGGPVIKGFGRGsKVLGIPTANL-STENYsdVLSEhpSGVYFGWAGLSTRG-VYKMVMSIGWNPYF---NNTEKTIEPWL 315
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 581975924 265 F-DFEDNIYGERVTVNWHHFLRPEIKFDGIDPLVKQMNDDKSRAKYLL 311
Cdd:PLN02940 316 LhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKAL 363
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
20-170 5.45e-05

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: 42.43  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581975924  20 VAMAFGFFDGMHKGHDKVFDILNEIAEARSLkkaVMTFDPhpsvvlNPKRKRTTYLTPLSDKTEKISQHDID-YCIVVNF 98
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVI---IIIVSN------PPKKKRNKDPFSLHERVEMLKEILKDrLKVVPVD 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581975924  99 SSRFANVSVEDFVENYIIKNNVKEVIAGFDFTFGKFGKGNMTVLQEYDAFnTTIVSKQEIENEKISTTSIRQ 170
Cdd:cd02039   72 FPEVKILLAVVFILKILLKVGPDKVVVGEDFAFGKNASYNKDLKELFLDI-EIVEVPRVRDGKKISSTLIRE 142
 
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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