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Conserved domains on  [gi|2221504030|gb|UOP04537|]
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bifunctional riboflavin kinase/FAD synthetase [Conchiformibius kuhniae]

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

CATH:  3.40.50.620|2.40.30.30
EC:  2.7.1.26|2.7.7.2
Gene Symbol:  ribF
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 ...
 1-310 1.37e-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: 394.02  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030   1 MDIRFGIQPCSDSL-PCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSRrtasAPLRLTPLRD 79
Cdd:COG0196     1 MKIIRGLSELPADLrGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDK----APKLLTTLEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  80 KLNLLRQsACVDAVRVLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPS 156
Cdd:COG0196    77 KLELLEE-LGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGeeyGFEVEVVPP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 157 ILAAGGRASSTAVRAALQQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRY-ALSGVFVVEAAGAFGT 235
Cdd:COG0196   156 VTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLlPADGVYAVRVRIDGRR 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221504030 236 RFGVASFGTNPTVSDTDcAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVGAR 310
Cdd:COG0196   236 YPGVANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKL 309
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-310 1.37e-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: 394.02  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030   1 MDIRFGIQPCSDSL-PCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSRrtasAPLRLTPLRD 79
Cdd:COG0196     1 MKIIRGLSELPADLrGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDK----APKLLTTLEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  80 KLNLLRQsACVDAVRVLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPS 156
Cdd:COG0196    77 KLELLEE-LGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGeeyGFEVEVVPP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 157 ILAAGGRASSTAVRAALQQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRY-ALSGVFVVEAAGAFGT 235
Cdd:COG0196   156 VTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLlPADGVYAVRVRIDGRR 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221504030 236 RFGVASFGTNPTVSDTDcAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVGAR 310
Cdd:COG0196   236 YPGVANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKL 309
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
6-309 5.14e-126

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 362.16  E-value: 5.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030   6 GIQPCSDSLPCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLR 85
Cdd:PRK05627    5 GLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPD----KAPARLTPLRDKAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  86 QsACVDAVRVLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGG 162
Cdd:PRK05627   81 E-LGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGkefGFEVTIVPEVKEDGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 163 RASSTAVRAALQQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRYALSGVFVVEaAGAFGTRF-GVAS 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVR-VKVDGKPYpGVAN 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2221504030 242 FGTNPTVSDTDcAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVGA 309
Cdd:PRK05627  239 IGTRPTVDGGR-QLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 17-308 1.33e-88

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: 266.23  E-value: 1.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  17 AVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFarSRRTASAplrLTPLRDKLNLLrQSACVDAVRVL 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQF--NWLTAPA---LTPLEDKARQL-QIKGVEQLLVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  97 RFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVErTPSILAAGGRASSTAVRAAL 173
Cdd:TIGR00083  75 VFDEEFANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGnttIFCVI-VKQLFCQDIRISSSAIRQAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 174 QQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRYALSGVFVVEAAGAFGTRF-GVASFGTNPTVsDTD 252
Cdd:TIGR00083 154 KNGDLELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYpGVGNIGNRPTF-IGQ 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221504030 253 CAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVG 308
Cdd:TIGR00083 233 QLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 16-198 1.35e-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: 206.24  E-value: 1.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  16 CAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLRQSAcVDAVRV 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPD----KAPPRLTTLEEKLELLESLG-VDYLLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  96 LRFHAEFAAQSAEAFVRTVLRDaLNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGGRASSTAVRAA 172
Cdd:cd02064    76 LPFDKEFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGkkyGFEVTVVPPVTLDGERVSSTRIREA 154

                         170       180
                  ....*....|....*....|....*.
gi 2221504030 173 LQQGRLEVAEQILGHRYALSGRVKHG 198
Cdd:cd02064   155 LAEGDVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 15-168 6.80e-58

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: 183.15  E-value: 6.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  15 PCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLRQsACVDAVR 94
Cdd:pfam06574   7 GCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPD----SAPFRLTTLEEKIELLAE-LGVDYLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221504030  95 VLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGGRASSTA 168
Cdd:pfam06574  82 VLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGaklGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 184-306 2.23e-52

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: 168.00  E-value: 2.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  184 ILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRY-ALSGVFVVEAAGAFGTRFGVASFGTNPTVSDTdcAKLEVHLFD 262
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLlPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGD--RSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2221504030  263 FHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNW 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREY 122
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 1-310 1.37e-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: 394.02  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030   1 MDIRFGIQPCSDSL-PCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSRrtasAPLRLTPLRD 79
Cdd:COG0196     1 MKIIRGLSELPADLrGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDK----APKLLTTLEE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  80 KLNLLRQsACVDAVRVLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPS 156
Cdd:COG0196    77 KLELLEE-LGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGeeyGFEVEVVPP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 157 ILAAGGRASSTAVRAALQQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRY-ALSGVFVVEAAGAFGT 235
Cdd:COG0196   156 VTIDGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLlPADGVYAVRVRIDGRR 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2221504030 236 RFGVASFGTNPTVSDTDcAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVGAR 310
Cdd:COG0196   236 YPGVANIGTRPTFDGGE-PTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKL 309
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
6-309 5.14e-126

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 362.16  E-value: 5.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030   6 GIQPCSDSLPCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLR 85
Cdd:PRK05627    5 GLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPD----KAPARLTPLRDKAELLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  86 QsACVDAVRVLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGG 162
Cdd:PRK05627   81 E-LGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGkefGFEVTIVPEVKEDGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 163 RASSTAVRAALQQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRYALSGVFVVEaAGAFGTRF-GVAS 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLPDRVLPADGVYAVR-VKVDGKPYpGVAN 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2221504030 242 FGTNPTVSDTDcAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVGA 309
Cdd:PRK05627  239 IGTRPTVDGGR-QLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFLAL 305
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 17-308 1.33e-88

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: 266.23  E-value: 1.33e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  17 AVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFarSRRTASAplrLTPLRDKLNLLrQSACVDAVRVL 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQF--NWLTAPA---LTPLEDKARQL-QIKGVEQLLVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  97 RFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVErTPSILAAGGRASSTAVRAAL 173
Cdd:TIGR00083  75 VFDEEFANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGnttIFCVI-VKQLFCQDIRISSSAIRQAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 174 QQGRLEVAEQILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRYALSGVFVVEAAGAFGTRF-GVASFGTNPTVsDTD 252
Cdd:TIGR00083 154 KNGDLELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKNQVLPLKGGYYVVVVLLNGEPYpGVGNIGNRPTF-IGQ 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221504030 253 CAKLEVHLFDFHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNWVG 308
Cdd:TIGR00083 233 QLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 16-198 1.35e-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: 206.24  E-value: 1.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  16 CAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLRQSAcVDAVRV 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPD----KAPPRLTTLEEKLELLESLG-VDYLLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  96 LRFHAEFAAQSAEAFVRTVLRDaLNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGGRASSTAVRAA 172
Cdd:cd02064    76 LPFDKEFASLSAEEFVEDLLVK-LNAKHVVVGFDFRFGKGRSGDAELLKELGkkyGFEVTVVPPVTLDGERVSSTRIREA 154

                         170       180
                  ....*....|....*....|....*.
gi 2221504030 173 LQQGRLEVAEQILGHRYALSGRVKHG 198
Cdd:cd02064   155 LAEGDVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 15-168 6.80e-58

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: 183.15  E-value: 6.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  15 PCAVTIGNFDGVHLGHRHILQTLRDEARARRLQTAVVVFEPQPPEFFARSrrtaSAPLRLTPLRDKLNLLRQsACVDAVR 94
Cdd:pfam06574   7 GCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPD----SAPFRLTTLEEKIELLAE-LGVDYLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2221504030  95 VLRFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFGRGREGDFAMLRGQG---GFVVERTPSILAAGGRASSTA 168
Cdd:pfam06574  82 VLPFTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGaklGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 184-306 2.23e-52

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: 168.00  E-value: 2.23e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  184 ILGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRY-ALSGVFVVEAAGAFGTRFGVASFGTNPTVSDTdcAKLEVHLFD 262
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLlPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGD--RSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2221504030  263 FHGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNW 306
Cdd:smart00904  79 FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREY 122
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 185-306 3.41e-52

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: 167.55  E-value: 3.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030 185 LGHRYALSGRVKHGAKLGRTLGCPTANIHLPAHRYALSGVFVVEAAGAFGTRF-GVASFGTNPTVSDTdCAKLEVHLFDF 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPEKLLPANGVYAVWVRVDGGKVYpGVANIGTNPTFGNG-KLTVEVHILDF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2221504030 264 HGTLYGQRLEVRFLHKLRDELRFDGLDALLKQIQADIDAARNW 306
Cdd:pfam01687  80 DGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 18-172 2.20e-05

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: 43.46  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  18 VTIGNFDGVHLGHRHILqtlrDEARaRRLQTAVVVFEPQPPEFFARSRRTASAPLRltplrdkLNLLRQSACVDAVRVLR 97
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLL----EQAK-ELFDEDLIVGVPSDEPPHKLKRPLFSAEER-------LEMLELAKWVDEVIVVA 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2221504030  98 FhaefaaqsaEAFVRTVLRDaLNTHYLLVGDDFRFGRGREGDfaMLRGQGGFVVERTPSILAAGGR---ASSTAVRAA 172
Cdd:pfam01467  69 P---------WELTRELLKE-LNPDVLVIGADSLLDFWYELD--EILGNVKLVVVVRPVFFIPLKPtngISSTDIRER 134
PRK07143 PRK07143
hypothetical protein; Provisional
 20-144 1.89e-04

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 42.29  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  20 IGNFDGVHLGHRHILQTLRDEArarrlQTAVVVFEpQPPEFFARSRRTasaplRLTPLRDKLNLLRQSAcVDAVRVLRFH 99
Cdd:PRK07143   21 LGGFESFHLGHLELFKKAKESN-----DEIVIVIF-KNPENLPKNTNK-----KFSDLNSRLQTLANLG-FKNIILLDFN 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2221504030 100 AEFAAQSAEAFVRTVLRdaLNTHYLLVGDDFRFGRGREGDFAMLR 144
Cdd:PRK07143   89 EELQNLSGNDFIEKLTK--NQVSFFVVGKDFRFGKNASWNADDLK 131
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 17-133 1.40e-03

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: 38.19  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221504030  17 AVTIGNFDGVHLGHRHILQTLRDEARARRLqtaVVVFEPQPPefFARSRRTASAPLRLTPLRDKLNllrqsacvDAVRVL 96
Cdd:cd02039     2 GIIIGRFEPFHLGHLKLIKEALEEALDEVI---IIIVSNPPK--KKRNKDPFSLHERVEMLKEILK--------DRLKVV 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2221504030  97 RFHAEFAAQSAEAFVRTVLRDALNTHYLLVGDDFRFG 133
Cdd:cd02039    69 PVDFPEVKILLAVVFILKILLKVGPDKVVVGEDFAFG 105
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
21-74 6.72e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 37.12  E-value: 6.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2221504030  21 GNFDGVHLGHRHILQTLrdearARRLQTAVVVF--EPQPPefFARSRRTASAPLRL 74
Cdd:PRK00071   11 GTFDPPHYGHLAIAEEA-----AERLGLDEVWFlpNPGPP--HKPQKPLAPLEHRL 59
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 16-53 9.73e-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: 9.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2221504030  16 CAVTIGNFDGVHLGHRHILQtlrdeaRARRLQTAVVVF 53
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLE------RAKELFDELIVG 32
 
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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