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Conserved domains on  [gi|913019572|gb|AKU70525|]
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riboflavin kinase [Prevotella fusca JCM 17724]

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 ...
 30-323 1.79e-136

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: 389.79  E-value: 1.79e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:COG0196   18 VVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTRE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:COG0196   98 FAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTS 269
Cdd:COG0196  178 EEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDG--RRYPGVANIGTRPTFDGGEPT 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFDE 323
Cdd:COG0196  255 LEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAK 308
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 30-323 1.79e-136

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: 389.79  E-value: 1.79e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:COG0196   18 VVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTRE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:COG0196   98 FAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTS 269
Cdd:COG0196  178 EEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDG--RRYPGVANIGTRPTFDGGEPT 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFDE 323
Cdd:COG0196  255 LEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAK 308
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
27-313 8.52e-117

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 339.43  E-value: 8.52e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  27 PEQVATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHF 106
Cdd:PRK05627  13 PDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 107 DESLAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQ 186
Cdd:PRK05627  93 DEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 187 GEIEAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSvgWKRGMMNIGKRPTFNGT 266
Cdd:PRK05627 173 GDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGK--PYPGVANIGTRPTVDGG 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 913019572 267 TTSMEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQD 313
Cdd:PRK05627 249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKD 295
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 30-321 2.19e-81

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: 248.90  E-value: 2.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPqLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAP-ALTPLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLpDDEKVSSSVIRNHIQQGEI 189
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFC-QDIRISSSAIRQALKNGDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTS 269
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK--NQVLPLKGGYYVVVVLLNGEPYP-GVGNIGNRPTFIGQQLV 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 913019572  270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 30-209 1.84e-70

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: 217.02  E-value: 1.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:cd02064    2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLyRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:cd02064   82 FASLSAEEFVEDLL-VKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDV 160

                        170       180
                 ....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNG 209
Cdd:cd02064  161 ELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 30-178 2.54e-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: 2.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:pfam06574   9 VVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKE 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913019572  110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSS 178
Cdd:pfam06574  89 FASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISST 157
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 195-322 4.76e-47

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: 154.90  E-value: 4.76e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   195 LLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTsMEVNL 274
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDG--KIYPGVANIGTRPTFGGDRS-VEVHI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 913019572   275 FNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:smart00904  77 LDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 30-323 1.79e-136

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: 389.79  E-value: 1.79e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:COG0196   18 VVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKAPKLLTTLEEKLELLEELGVDYVLVLPFTRE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:COG0196   98 FAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTIDGERVSSTRIREALAEGDV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTS 269
Cdd:COG0196  178 EEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPE-EKLLPADGVYAVRVRIDG--RRYPGVANIGTRPTFDGGEPT 254

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 913019572 270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFDE 323
Cdd:COG0196  255 LEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAK 308
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
27-313 8.52e-117

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 339.43  E-value: 8.52e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  27 PEQVATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHF 106
Cdd:PRK05627  13 PDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDKAPARLTPLRDKAELLAELGVDYVLVLPF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 107 DESLAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQ 186
Cdd:PRK05627  93 DEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGERVSSTAIRQALAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 187 GEIEAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSvgWKRGMMNIGKRPTFNGT 266
Cdd:PRK05627 173 GDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP--DRVLPADGVYAVRVKVDGK--PYPGVANIGTRPTVDGG 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 913019572 267 TTSMEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQD 313
Cdd:PRK05627 249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKD 295
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 30-321 2.19e-81

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: 248.90  E-value: 2.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPqLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAP-ALTPLEDKARQLQIKGVEQLLVVVFDEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLpDDEKVSSSVIRNHIQQGEI 189
Cdd:TIGR00083  80 FANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCVIVKQLFC-QDIRISSSAIRQALKNGDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  190 EAANRLLGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTS 269
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK--NQVLPLKGGYYVVVVLLNGEPYP-GVGNIGNRPTFIGQQLV 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 913019572  270 MEVNLFNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:TIGR00083 236 IEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
 30-209 1.84e-70

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: 217.02  E-value: 1.84e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:cd02064    2 VVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDKAPPRLTTLEEKLELLESLGVDYLLVLPFDKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 110 LAALPAREFMKEVLyRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEI 189
Cdd:cd02064   82 FASLSAEEFVEDLL-VKLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEGDV 160

                        170       180
                 ....*....|....*....|
gi 913019572 190 EAANRLLGYDYTIESTIVNG 209
Cdd:cd02064  161 ELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
 30-178 2.54e-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: 2.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMASAVITFDLHPRQVLQAGYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDES 109
Cdd:pfam06574   9 VVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRLTTLEEKIELLAELGVDYLLVLPFTKE 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913019572  110 LAALPAREFMKEVLYRQLNVKKLIIGYDNRFGHNRSEGFEHYVQYGRELGIEVILADAFLPDDEKVSSS 178
Cdd:pfam06574  89 FASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISST 157
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 196-321 2.62e-50

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: 163.32  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  196 LGYDYTIESTIVNGCQNGRRMGFPTANLDVNgcRQLLPAAGVYAVTVRLKDSVGWKrGMMNIGKRPTFNGTTTSMEVNLF 275
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLP--EKLLPANGVYAVWVRVDGGKVYP-GVANIGTNPTFGNGKLTVEVHIL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 913019572  276 NFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLF 321
Cdd:pfam01687  78 DFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 195-322 4.76e-47

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: 154.90  E-value: 4.76e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572   195 LLGYDYTIESTIVNGCQNGRRMGFPTANLDVNGcRQLLPAAGVYAVTVRLKDsvGWKRGMMNIGKRPTFNGTTTsMEVNL 274
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDG--KIYPGVANIGTRPTFGGDRS-VEVHI 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 913019572   275 FNFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:smart00904  77 LDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
PRK07143 PRK07143
hypothetical protein; Provisional
 33-207 9.31e-15

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 73.11  E-value: 9.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  33 IGFFDGVHRGHQFLIGRVRDEAERsgmasAVITFDLHPRQVLQagYQPQLLSTLDGKLLLLSKTRVDNIIVLHFDESLAA 112
Cdd:PRK07143  21 LGGFESFHLGHLELFKKAKESNDE-----IVIVIFKNPENLPK--NTNKKFSDLNSRLQTLANLGFKNIILLDFNEELQN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 113 LPAREFMKEVLyrQLNVKKLIIGYDNRFGHNRSEGFEHYvqygRELGIEVILADAFLPDDEKVSSSVIRNHIQQGEIEAA 192
Cdd:PRK07143  94 LSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDL----KEYFPNVHIVEILKINQQKISTSLLKEFIEFGDIELL 167

                        170
                 ....*....|....*
gi 913019572 193 NRLLGYDYTIESTIV 207
Cdd:PRK07143 168 NSLLLYNYSISITIN 182
PLN02940 PLN02940
riboflavin kinase
 202-322 1.30e-09

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 58.69  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 202 IESTIVNGCQNGRR-MGFPTANLDVNGCRQLLPA--AGVYavtvrlkdsVGW----KRGM----MNIGKRPTFNGTTTSM 270
Cdd:PLN02940 241 IGGPVIKGFGRGSKvLGIPTANLSTENYSDVLSEhpSGVY---------FGWaglsTRGVykmvMSIGWNPYFNNTEKTI 311

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 913019572 271 EVNLF-NFTGNLYGQELLVSFISKIRDERRFDSLDALSAQLMQDRDSVNRLFD 322
Cdd:PLN02940 312 EPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALD 364
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 30-182 3.68e-05

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 43.20  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572  30 VATIGFFDGVHRGHQFLIGRVRDEAERSGMasaVITFDlHPRQVLqagyQPQLLSTLDGKLLLLSK--TRVDNIIVLHFD 107
Cdd:cd02039    2 GIIIGRFEPFHLGHLKLIKEALEEALDEVI---IIIVS-NPPKKK----RNKDPFSLHERVEMLKEilKDRLKVVPVDFP 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 913019572 108 ESLAALPAREFMKEVLyrQLNVKKLIIGYDNRFGHNRSEG---FEHYvqygreLGIEVILADAFLpDDEKVSSSVIRN 182
Cdd:cd02039   74 EVKILLAVVFILKILL--KVGPDKVVVGEDFAFGKNASYNkdlKELF------LDIEIVEVPRVR-DGKKISSTLIRE 142
PBP1_ABC_HAAT-like cd19988
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 124-220 5.92e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380643 [Multi-domain]  Cd Length: 302  Bit Score: 38.03  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913019572 124 YRQLNVKKLIIGYDN-RFGhnRSeGFEHYVQYGRELGIEVILADAFLPDDEKVSSSVIRnhIQQGEIEAanrLLGYDYTI 202
Cdd:cd19988  131 FEKLKVTKIAVLYVNdDYG--RG-GIDAFKDAAKKYGIEVVVEESYNRGDKDFSPQLEK--IKDSGAQA---IVMWGQYT 202

                         90
                 ....*....|....*...
gi 913019572 203 ESTIVngCQNGRRMGFPT 220
Cdd:cd19988  203 EGALI--AKQARELGLKQ 218
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 30-56 8.51e-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: 34.59  E-value: 8.51e-03
                          10        20
                  ....*....|....*....|....*..
gi 913019572   30 VATIGFFDGVHRGHQFLIGRVRDEAER 56
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELFDE 28
 
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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