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Conserved domains on  [gi|169242158|emb|CAM63186|]
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Probable bifunctional FAD synthetase/riboflavin biosynthesis protein RibF [Mycobacteroides abscessus ATCC 19977]

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;
2-319 6.69e-167

bifunctional riboflavin kinase/FAD synthetase;


:

Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 466.16  E-value: 6.69e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   2 QRWRGQDEIPSDWGrCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELA 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  82 EELGVDVFLVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 162 TFSSTYIRSCVDAGDMVAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFsAIPADGVYAAWFtllghgptmgtV 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDR-VLPADGVYAVRV-----------K 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158 242 VPGERYQAAVSVGSNPTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILAR 319
Cdd:PRK05627 228 VDGKPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-319 6.69e-167

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 466.16  E-value: 6.69e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   2 QRWRGQDEIPSDWGrCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELA 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  82 EELGVDVFLVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 162 TFSSTYIRSCVDAGDMVAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFsAIPADGVYAAWFtllghgptmgtV 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDR-VLPADGVYAVRV-----------K 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158 242 VPGERYQAAVSVGSNPTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILAR 319
Cdd:PRK05627 228 VDGKPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-320 1.38e-165

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: 462.98  E-value: 1.38e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   1 MQRWRGQDEIPSDWGRCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAEL 80
Cdd:COG0196    1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  81 AEELGVDVFLVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHA 160
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 161 VTFSSTYIRSCVDAGDMVAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWftllghgptmgT 240
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVR-----------V 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 241 VVPGERYQAAVSVGSNPTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILARN 320
Cdd:COG0196  230 RIDGRRYPGVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKL 309
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
17-197 2.20e-81

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: 244.37  E-value: 2.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  17 CVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELAEELGVDVFLVVPFTP 96
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  97 EFMKLSPERYVHELLVErLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAVTFSSTYIRSCVDAGD 176
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 169242158 177 MVAATEALGRPHRVEGVVVRG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-318 8.79e-79

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: 241.58  E-value: 8.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   18 VLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAqLTTLTRRAELAEELGVDVFLVVPFTPE 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   98 FMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVdAVTLVTEHAVTFSSTYIRSCVDAGDM 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCV-IVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  178 VAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWFTLlghgptmgtvvpGERYQAAVS-VGSN 256
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLL------------NGEPYPGVGnIGNR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169242158  257 PTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILA 318
Cdd:TIGR00083 227 PTFIGQQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
10-167 5.04e-75

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: 227.45  E-value: 5.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   10 IPSDWGRCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELAEELGVDVF 89
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158   90 LVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAVTFSSTY 167
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-318 7.55e-55

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: 174.55  E-value: 7.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   184 LGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWftllghgptmgTVVPGERYQAAVSVGSNPTFSGKa 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVR-----------VRVDGKIYPGVANIGTRPTFGGD- 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 169242158   264 RTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILA 318
Cdd:smart00904  70 RSVEVHILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
 
Name Accession Description Interval E-value
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-319 6.69e-167

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 466.16  E-value: 6.69e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   2 QRWRGQDEIPSDWGrCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELA 81
Cdd:PRK05627   1 QLIRGLHNIPQPPD-CVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  82 EELGVDVFLVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAV 161
Cdd:PRK05627  80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 162 TFSSTYIRSCVDAGDMVAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFsAIPADGVYAAWFtllghgptmgtV 241
Cdd:PRK05627 160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDR-VLPADGVYAVRV-----------K 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158 242 VPGERYQAAVSVGSNPTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILAR 319
Cdd:PRK05627 228 VDGKPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-320 1.38e-165

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: 462.98  E-value: 1.38e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   1 MQRWRGQDEIPSDWGRCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAEL 80
Cdd:COG0196    1 MKIIRGLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  81 AEELGVDVFLVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHA 160
Cdd:COG0196   81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 161 VTFSSTYIRSCVDAGDMVAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWftllghgptmgT 240
Cdd:COG0196  161 ERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVR-----------V 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 241 VVPGERYQAAVSVGSNPTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILARN 320
Cdd:COG0196  230 RIDGRRYPGVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKL 309
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
17-197 2.20e-81

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: 244.37  E-value: 2.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  17 CVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELAEELGVDVFLVVPFTP 96
Cdd:cd02064    1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  97 EFMKLSPERYVHELLVErLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAVTFSSTYIRSCVDAGD 176
Cdd:cd02064   81 EFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGD 159
                        170       180
                 ....*....|....*....|.
gi 169242158 177 MVAATEALGRPHRVEGVVVRG 197
Cdd:cd02064  160 VELANELLGRPYSIEGRVVHG 180
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-318 8.79e-79

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: 241.58  E-value: 8.79e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   18 VLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAqLTTLTRRAELAEELGVDVFLVVPFTPE 97
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA-LTPLEDKARQLQIKGVEQLLVVVFDEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   98 FMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVdAVTLVTEHAVTFSSTYIRSCVDAGDM 177
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCV-IVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  178 VAATEALGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWFTLlghgptmgtvvpGERYQAAVS-VGSN 256
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLL------------NGEPYPGVGnIGNR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169242158  257 PTFSGKARTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILA 318
Cdd:TIGR00083 227 PTFIGQQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
10-167 5.04e-75

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: 227.45  E-value: 5.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   10 IPSDWGRCVLTIGVFDGVHRGHAELIGRAVKAARELNLKSVLMTFDPHPMEVVFPGTHPAQLTTLTRRAELAEELGVDVF 89
Cdd:pfam06574   1 LPEDLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158   90 LVVPFTPEFMKLSPERYVHELLVERLHVAEVVVGENFTFGKKAAGNVQMLKKAGERFGFKVDAVTLVTEHAVTFSSTY 167
Cdd:pfam06574  81 LVLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
184-317 2.99e-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: 178.34  E-value: 2.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  184 LGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFsAIPADGVYAAWFTLLGhgptmgtvvpGERYQAAVSVGSNPTFSGKA 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPEK-LLPANGVYAVWVRVDG----------GKVYPGVANIGTNPTFGNGK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 169242158  264 RTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTIL 317
Cdd:pfam01687  70 LTVEVHILDFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-318 7.55e-55

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: 174.55  E-value: 7.55e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158   184 LGRPHRVEGVVVRGDGRGRELGFPTANVAPPMFSAIPADGVYAAWftllghgptmgTVVPGERYQAAVSVGSNPTFSGKa 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVR-----------VRVDGKIYPGVANIGTRPTFGGD- 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 169242158   264 RTVEAFILDTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTILA 318
Cdd:smart00904  70 RSVEVHILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
PLN02940 PLN02940
riboflavin kinase
187-317 1.14e-13

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 71.02  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158 187 PHRVEGVVVRGDGRGRE-LGFPTANVAPPMFSAIPAD---GVYAAWFTLLGHGPtmgtvvpgerYQAAVSVGSNPTFSGK 262
Cdd:PLN02940 238 PWHIGGPVIKGFGRGSKvLGIPTANLSTENYSDVLSEhpsGVYFGWAGLSTRGV----------YKMVMSIGWNPYFNNT 307
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169242158 263 ARTVEAFIL-DTTADLYGQHVAVDFVARIRSMEKFKSIDDLVVAMGKDAEKARTIL 317
Cdd:PLN02940 308 EKTIEPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKAL 363
PRK07143 PRK07143
hypothetical protein; Provisional
21-176 7.71e-13

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 67.72  E-value: 7.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  21 IGVFDGVHRGHAELIgravKAARELNLKSVLMTF-DPHPMevvfPGTHPAQLTTLTRRAELAEELGVDVFLVVPFTPEFM 99
Cdd:PRK07143  21 LGGFESFHLGHLELF----KKAKESNDEIVIVIFkNPENL----PKNTNKKFSDLNSRLQTLANLGFKNIILLDFNEELQ 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169242158 100 KLSPERYVHELLveRLHVAEVVVGENFTFGKKAAGNVQMLKkagERFGfKVDAVTLVTEHAVTFSSTYIRSCVDAGD 176
Cdd:PRK07143  93 NLSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDLK---EYFP-NVHIVEILKINQQKISTSLLKEFIEFGD 163
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
18-169 2.12e-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: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169242158  18 VLTIGVFDGVHRGHAELIgraVKAARELNLKSVLMTFDpHPMEVVFPGThpaqLTTLTRRAELAEELGVDVFLVVPFtpE 97
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLI---KEALEEALDEVIIIIVS-NPPKKKRNKD----PFSLHERVEMLKEILKDRLKVVPV--D 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169242158  98 FMKLSPERYVHELLVERLHVAE--VVVGENFTFGKKAAGNVQMLKkagerFGFKVDAVtlVTEHAVTF---SSTYIR 169
Cdd:cd02039   72 FPEVKILLAVVFILKILLKVGPdkVVVGEDFAFGKNASYNKDLKE-----LFLDIEIV--EVPRVRDGkkiSSTLIR 141
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
17-84 1.66e-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: 36.52  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169242158   17 CVLTIGVFDGVHRGHAELIGRavkAARELNLKSVLMTFDPhpmevVFPGTHPAQLTTLTRRAELAEEL 84
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLER---AKELFDELIVGVGSDQ-----FVNPLKGEPVFSLEERLEMLKAL 60
 
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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