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Conserved domains on  [gi|2514706932|gb|WIK87892|]
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bifunctional riboflavin kinase/FAD synthetase [Varibaculum cambriense]

Protein Classification

bifunctional riboflavin kinase/FMN adenylyltransferase( domain architecture ID 11481331)

bifunctional riboflavin biosynthesis protein having both ATP-riboflavin kinase and ATP-flavin mononucleotide adenylyltransferase activities

EC:  2.7.1.26|2.7.7.2
Gene Ontology:  GO:0005524|GO:0006747|GO:0009398|GO:0003919|GO:0008531|GO:0016310|GO:0009231
PubMed:  25801930

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-317 1.04e-132

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: 379.77  E-value: 1.04e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   1 MEIWTNSPQLEKGQR-SVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDA 79
Cdd:COG0196     1 MKIIRGLSELPADLRgTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  80 MAALGLDATWVVPYTWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqD 159
Cdd:COG0196    81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTI-D 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 160 SRRYSSTRVRACLAKGDVEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIrsVPGtnav 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVR--IDG---- 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2514706932 240 EHLPAAISVGTNPQFSGDKVTVEAHVLGrADLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGVPP 317
Cdd:COG0196   234 RRYPGVANIGTRPTFDGGEPTLEVHLLD-FDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-317 1.04e-132

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: 379.77  E-value: 1.04e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   1 MEIWTNSPQLEKGQR-SVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDA 79
Cdd:COG0196     1 MKIIRGLSELPADLRgTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  80 MAALGLDATWVVPYTWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqD 159
Cdd:COG0196    81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTI-D 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 160 SRRYSSTRVRACLAKGDVEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIrsVPGtnav 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVR--IDG---- 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2514706932 240 EHLPAAISVGTNPQFSGDKVTVEAHVLGrADLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGVPP 317
Cdd:COG0196   234 RRYPGVANIGTRPTFDGGEPTLEVHLLD-FDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-315 1.97e-115

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 335.97  E-value: 1.97e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   2 EIWTNSPQLEKGQRSVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMA 81
Cdd:PRK05627    1 QLIRGLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  82 ALGLDATWVVPYTWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDQDsR 161
Cdd:PRK05627   81 ELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDG-E 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 162 RYSSTRVRACLAKGDVEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLgKTAGLAIPADGVYAGRLirSVPGtnavEH 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANL-PLPDRVLPADGVYAVRV--KVDG----KP 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932 242 LPAAISVGTNPQFSGDKVTVEAHVLGRADlDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGV 315
Cdd:PRK05627  233 YPGVANIGTRPTVDGGRQLLEVHLLDFNG-DLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 16-197 3.81e-66

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: 205.85  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  16 SVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMAALGLDATWVVPYTW 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  96 DLANQSPQWFIDHYFVaGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqDSRRYSSTRVRACLAKG 175
Cdd:cd02064    81 EFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTL-DGERVSSTRIREALAEG 158

                         170       180
                  ....*....|....*....|..
gi 2514706932 176 DVEGAARILGRSYRLRGIVERG 197
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 17-314 9.58e-64

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: 203.45  E-value: 9.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  17 VAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIqPLPDRLDAMAALGLDATWVVPYTWD 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPALT-PLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  97 LANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIeVADITDQDsRRYSSTRVRACLAKGD 176
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVI-VKQLFCQD-IRISSSAIRQALKNGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 177 VEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIRSvpgtnaVEHLPAAISVGTNPQFSG 256
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLN------GEPYPGVGNIGNRPTFIG 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2514706932 257 DKVTVEAHVLGRAdLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILG 314
Cdd:TIGR00083 232 QQLVIEVHLLDFS-GELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 14-167 1.74e-54

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: 175.06  E-value: 1.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  14 QRSVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMAALGLDATWVVPY 93
Cdd:pfam06574   6 EGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPF 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932  94 TWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqDSRRYSSTR 167
Cdd:pfam06574  86 TKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVEL-DGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 183-313 1.79e-40

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: 137.95  E-value: 1.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  183 ILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIrsVPGTNavehLPAAISVGTNPQFSGDKvTVE 262
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVR--VDGKI----YPGVANIGTRPTFGGDR-SVE 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2514706932  263 AHVLGRaDLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEIL 313
Cdd:smart00904  74 VHILDF-SGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-317 1.04e-132

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: 379.77  E-value: 1.04e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   1 MEIWTNSPQLEKGQR-SVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDA 79
Cdd:COG0196     1 MKIIRGLSELPADLRgTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  80 MAALGLDATWVVPYTWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqD 159
Cdd:COG0196    81 LEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTI-D 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 160 SRRYSSTRVRACLAKGDVEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIrsVPGtnav 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVR--IDG---- 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2514706932 240 EHLPAAISVGTNPQFSGDKVTVEAHVLGrADLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGVPP 317
Cdd:COG0196   234 RRYPGVANIGTRPTFDGGEPTLEVHLLD-FDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-315 1.97e-115

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 335.97  E-value: 1.97e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   2 EIWTNSPQLEKGQRSVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMA 81
Cdd:PRK05627    1 QLIRGLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  82 ALGLDATWVVPYTWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDQDsR 161
Cdd:PRK05627   81 ELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDG-E 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 162 RYSSTRVRACLAKGDVEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLgKTAGLAIPADGVYAGRLirSVPGtnavEH 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANL-PLPDRVLPADGVYAVRV--KVDG----KP 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932 242 LPAAISVGTNPQFSGDKVTVEAHVLGRADlDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGV 315
Cdd:PRK05627  233 YPGVANIGTRPTVDGGRQLLEVHLLDFNG-DLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 16-197 3.81e-66

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: 205.85  E-value: 3.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  16 SVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMAALGLDATWVVPYTW 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  96 DLANQSPQWFIDHYFVaGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqDSRRYSSTRVRACLAKG 175
Cdd:cd02064    81 EFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTL-DGERVSSTRIREALAEG 158

                         170       180
                  ....*....|....*....|..
gi 2514706932 176 DVEGAARILGRSYRLRGIVERG 197
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 17-314 9.58e-64

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: 203.45  E-value: 9.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  17 VAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIqPLPDRLDAMAALGLDATWVVPYTWD 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPALT-PLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  97 LANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIeVADITDQDsRRYSSTRVRACLAKGD 176
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVI-VKQLFCQD-IRISSSAIRQALKNGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 177 VEGAARILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIRSvpgtnaVEHLPAAISVGTNPQFSG 256
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLN------GEPYPGVGNIGNRPTFIG 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2514706932 257 DKVTVEAHVLGRAdLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILG 314
Cdd:TIGR00083 232 QQLVIEVHLLDFS-GELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 14-167 1.74e-54

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: 175.06  E-value: 1.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  14 QRSVAAIGIFDGVHKGHTRILKTVVERARRAGVKAVAITFDPHPSQLHNPENPTLLIQPLPDRLDAMAALGLDATWVVPY 93
Cdd:pfam06574   6 EGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPF 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932  94 TWDLANQSPQWFIDHYFVAGLRVKELVVGEDMQFGRGNRGDIETLREAGRTQDFQVIEVADITDqDSRRYSSTR 167
Cdd:pfam06574  86 TKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVEL-DGEKISSTR 158
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 184-313 8.60e-45

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: 149.07  E-value: 8.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 184 LGRSYRLRGIVERGFRRGRQLGFPTANLgKTAGLAIPADGVYAGRLIRsvpgtNAVEHLPAAISVGTNPQFSGDKVTVEA 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANL-PLPEKLLPANGVYAVWVRV-----DGGKVYPGVANIGTNPTFGNGKLTVEV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2514706932 264 HVLGRaDLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEIL 313
Cdd:pfam01687  75 HILDF-DGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 183-313 1.79e-40

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: 137.95  E-value: 1.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  183 ILGRSYRLRGIVERGFRRGRQLGFPTANLGKTAGLAIPADGVYAGRLIrsVPGTNavehLPAAISVGTNPQFSGDKvTVE 262
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVR--VDGKI----YPGVANIGTRPTFGGDR-SVE 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2514706932  263 AHVLGRaDLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEIL 313
Cdd:smart00904  74 VHILDF-SGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
PRK07143 PRK07143
hypothetical protein; Provisional
 1-188 1.62e-13

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 69.64  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932   1 MEIWTNSPQLEKGQRSVAAIGIFDGVHKGHTRILKTVVERARRagvkaVAITFDPHPSQLhnPENPTLLIQPLPDRLDAM 80
Cdd:PRK07143    2 MKVYTFPLKNFKFEKPTFVLGGFESFHLGHLELFKKAKESNDE-----IVIVIFKNPENL--PKNTNKKFSDLNSRLQTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  81 AALGLDATWVVPYTWDLANQSPQWFIDHYFVAGlrVKELVVGEDMQFGRGNRGDIETLREAgrtqdFQVIEVADITDQDS 160
Cdd:PRK07143   75 ANLGFKNIILLDFNEELQNLSGNDFIEKLTKNQ--VSFFVVGKDFRFGKNASWNADDLKEY-----FPNVHIVEILKINQ 147

                         170       180
                  ....*....|....*....|....*...
gi 2514706932 161 RRYSSTRVRACLAKGDVEGAARILGRSY 188
Cdd:PRK07143  148 QKISTSLLKEFIEFGDIELLNSLLLYNY 175
PLN02940 PLN02940
riboflavin kinase
 192-317 1.28e-07

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 52.53  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932 192 GIVERGFRRGRQ-LGFPTANL---GKTAGLAIPADGVYAGRLIRSVPGTNAVehlpaAISVGTNPQFSGDKVTVEAHVLG 267
Cdd:PLN02940  243 GPVIKGFGRGSKvLGIPTANLsteNYSDVLSEHPSGVYFGWAGLSTRGVYKM-----VMSIGWNPYFNNTEKTIEPWLLH 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2514706932 268 RADLDLYDEPVAIDFLAHLRDMVKLESVEKLQSQMDEDLRACSEILGVPP 317
Cdd:PLN02940  318 DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPL 367
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 17-169 9.09e-07

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: 47.82  E-value: 9.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  17 VAAIGIFDGVHKGHTRILKTVVERARRagvKAVAITFDpHPSQLHNPENPtlliQPLPDRLDAMAALGLDATWVVPYT-W 95
Cdd:cd02039     2 GIIIGRFEPFHLGHLKLIKEALEEALD---EVIIIIVS-NPPKKKRNKDP----FSLHERVEMLKEILKDRLKVVPVDfP 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932  96 DLANQSPQWFIDHYFvAGLRVKELVVGEDMQFGRGNRGDietLREAGRTQDFQVIEVadITDQDSRRYSSTRVR 169
Cdd:cd02039    74 EVKILLAVVFILKIL-LKVGPDKVVVGEDFAFGKNASYN---KDLKELFLDIEIVEV--PRVRDGKKISSTLIR 141
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 19-170 2.39e-04

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 40.38  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  19 AIGIFDGVHKGHTRILktvvERARRAG--VKAVAITFDPhpsQLHNPENPtllIQPLPDRLDAMAALGLDATWVVPYTWD 96
Cdd:pfam01467   2 FGGTFDPIHLGHLRLL----EQAKELFdeDLIVGVPSDE---PPHKLKRP---LFSAEERLEMLELAKWVDEVIVVAPWE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2514706932  97 LANQspqwfidhyFVAGLRVKELVVGEDMQFGRGNRGDiETLREAGRTQdfQVIEVADITDQDSRRYSSTRVRA 170
Cdd:pfam01467  72 LTRE---------LLKELNPDVLVIGADSLLDFWYELD-EILGNVKLVV--VVRPVFFIPLKPTNGISSTDIRE 133
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 12-96 4.36e-03

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 38.66  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2514706932  12 KGQRSVAAIGIFDGVHKGHTRILktvvERARRAGVK-AVAITFDPHPSQLHNPENPtllIQPLPDRLDAMAALGlDATWV 90
Cdd:PRK11316  338 RGEKIVMTNGCFDILHAGHVSYL----ANARKLGDRlIVAVNSDASVKRLKGEGRP---VNPLEQRMAVLAALE-AVDWV 409


                  ....*.
gi 2514706932  91 VPYTWD 96
Cdd:PRK11316  410 VPFEED 415
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 17-92 9.39e-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: 34.20  E-value: 9.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2514706932  17 VAAIGIFDGVHKGHTRILktvvERARRAGVKA-VAITFDphpsQLHNPEnPTLLIQPLPDRLDamaaLGLDATWVVP 92
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLL----ERAKELFDELiVGVGSD----QFVNPL-KGEPVFSLEERLE----MLKALKYVDE 65
 
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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