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Conserved domains on  [gi|1132324836|gb|APU98192|]
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riboflavin biosynthesis protein RibF [Sphingobacterium sp. B29]

Protein Classification

bifunctional riboflavin kinase/FMN adenylyltransferase( domain architecture ID 11415176)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-324 2.60e-150

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: 424.46  E-value: 2.60e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   1 MKIYRSLDDFSPV-ENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDsLRLINDIEEKVS 79
Cdd:COG0196     1 MKIIRGLSELPADlRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKA-PKLLTTLEEKLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  80 QLSKVGIDHLIIIPFSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDIN 159
Cdd:COG0196    80 LLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 160 DIAVSSTRVREALIKGDIRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVHePHKLIPAYGIYAVEVYIYNHIQNi 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALP-EEKLLPADGVYAVRVRIDGRRYP- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 240 ttgeykeenpvsiakGMGYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEI 319
Cdd:COG0196   238 ---------------GVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQA 302

                  ....*
gi 1132324836 320 RSLIG 324
Cdd:COG0196   303 RAILA 307
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-324 2.60e-150

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: 424.46  E-value: 2.60e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   1 MKIYRSLDDFSPV-ENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDsLRLINDIEEKVS 79
Cdd:COG0196     1 MKIIRGLSELPADlRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKA-PKLLTTLEEKLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  80 QLSKVGIDHLIIIPFSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDIN 159
Cdd:COG0196    80 LLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 160 DIAVSSTRVREALIKGDIRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVHePHKLIPAYGIYAVEVYIYNHIQNi 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALP-EEKLLPADGVYAVRVRIDGRRYP- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 240 ttgeykeenpvsiakGMGYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEI 319
Cdd:COG0196   238 ---------------GVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQA 302

                  ....*
gi 1132324836 320 RSLIG 324
Cdd:COG0196   303 RAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-322 1.94e-126

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 363.70  E-value: 1.94e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   2 KIYRSLDDFSPVENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDdSLRLINDIEEKVSQL 81
Cdd:PRK05627    1 QLIRGLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDK-APARLTPLRDKAELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  82 SKVGIDHLIIIPFSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDI 161
Cdd:PRK05627   80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 162 AVSSTRVREALIKGDIRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVhePHKLIPAYGIYAVEVYIYNHIQnitt 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL--PDRVLPADGVYAVRVKVDGKPY---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 242 geykeenpvsiaKGMGYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRS 321
Cdd:PRK05627  234 ------------PGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARA 301

                  .
gi 1132324836 322 L 322
Cdd:PRK05627  302 F 302
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
17-324 1.19e-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: 249.29  E-value: 1.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  17 VVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDSLrlINDIEEKVSQLSKVGIDHLIIIPFSR 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA--LTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  97 DFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVdEIPEQDINDIAVSSTRVREALIKGD 176
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCV-IVKQLFCQDIRISSSAIRQALKNGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 177 IRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVHePHKLIPAYGiYAVEVYIYNHIqnittgeykeenpvsIAKGM 256
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK-NQVLPLKGG-YYVVVVLLNGE---------------PYPGV 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132324836 257 GYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRSLIG 324
Cdd:TIGR00083 221 GNIGNRPTFIGQQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
16-197 4.46e-72

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: 220.87  E-value: 4.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  16 AVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDdSLRLINDIEEKVSQLSKVGIDHLIIIPFS 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDK-APPRLTTLEEKLELLESLGVDYLLVLPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  96 RDFSNQTPEEYISNVLVgKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDIAVSSTRVREALIKG 175
Cdd:cd02064    80 KEFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 1132324836 176 DIRTANLYLGYPFELTGTVIRG 197
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
14-167 1.99e-60

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: 190.47  E-value: 1.99e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  14 ENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDSLRLiNDIEEKVSQLSKVGIDHLIIIP 93
Cdd:pfam06574   6 EGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRL-TTLEEKIELLAELGVDYLLVLP 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132324836  94 FSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDIAVSSTR 167
Cdd:pfam06574  85 FTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-323 1.35e-50

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: 163.76  E-value: 1.35e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  184 LGYPFELTGTVIRGDQIGRTIGFPTANLQVHEpHKLIPAYGIYAVEVYIYNHIQNittgeykeenpvsiakGMGYIGTRP 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDGKIYP----------------GVANIGTRP 64
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  264 TVDGmNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRSLI 323
Cdd:smart00904  65 TFGG-DRSVEVHILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-324 2.60e-150

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: 424.46  E-value: 2.60e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   1 MKIYRSLDDFSPV-ENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDsLRLINDIEEKVS 79
Cdd:COG0196     1 MKIIRGLSELPADlRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRPDKA-PKLLTTLEEKLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  80 QLSKVGIDHLIIIPFSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDIN 159
Cdd:COG0196    80 LLEELGVDYVLVLPFTREFAALSPEEFVEEILVDKLGAKHVVVGDDFRFGKGRAGDVELLRELGEEYGFEVEVVPPVTID 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 160 DIAVSSTRVREALIKGDIRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVHePHKLIPAYGIYAVEVYIYNHIQNi 239
Cdd:COG0196   160 GERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALP-EEKLLPADGVYAVRVRIDGRRYP- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 240 ttgeykeenpvsiakGMGYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEI 319
Cdd:COG0196   238 ---------------GVANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQA 302

                  ....*
gi 1132324836 320 RSLIG 324
Cdd:COG0196   303 RAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-322 1.94e-126

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 363.70  E-value: 1.94e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   2 KIYRSLDDFSPVENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDdSLRLINDIEEKVSQL 81
Cdd:PRK05627    1 QLIRGLHNIPQPPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAPDK-APARLTPLRDKAELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  82 SKVGIDHLIIIPFSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDI 161
Cdd:PRK05627   80 AELGVDYVLVLPFDEEFAKLSAEEFIEDLLVKGLNAKHVVVGFDFRFGKKRAGDFELLKEAGKEFGFEVTIVPEVKEDGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 162 AVSSTRVREALIKGDIRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVhePHKLIPAYGIYAVEVYIYNHIQnitt 241
Cdd:PRK05627  160 RVSSTAIRQALAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPL--PDRVLPADGVYAVRVKVDGKPY---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 242 geykeenpvsiaKGMGYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRS 321
Cdd:PRK05627  234 ------------PGVANIGTRPTVDGGRQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARA 301

                  .
gi 1132324836 322 L 322
Cdd:PRK05627  302 F 302
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
17-324 1.19e-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: 249.29  E-value: 1.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  17 VVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDSLrlINDIEEKVSQLSKVGIDHLIIIPFSR 96
Cdd:TIGR00083   1 SLAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPA--LTPLEDKARQLQIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  97 DFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVdEIPEQDINDIAVSSTRVREALIKGD 176
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKHLHVKFLVVGDDFRFGHDRQGDFLLLQLFGNTTIFCV-IVKQLFCQDIRISSSAIRQALKNGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 177 IRTANLYLGYPFELTGTVIRGDQIGRTIGFPTANLQVHePHKLIPAYGiYAVEVYIYNHIqnittgeykeenpvsIAKGM 256
Cdd:TIGR00083 158 LELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLK-NQVLPLKGG-YYVVVVLLNGE---------------PYPGV 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132324836 257 GYIGTRPTVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRSLIG 324
Cdd:TIGR00083 221 GNIGNRPTFIGQQLVIEVHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWFN 288
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
16-197 4.46e-72

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: 220.87  E-value: 4.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  16 AVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDdSLRLINDIEEKVSQLSKVGIDHLIIIPFS 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVFLPDK-APPRLTTLEEKLELLESLGVDYLLVLPFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  96 RDFSNQTPEEYISNVLVgKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDIAVSSTRVREALIKG 175
Cdd:cd02064    80 KEFASLSAEEFVEDLLV-KLNAKHVVVGFDFRFGKGRSGDAELLKELGKKYGFEVTVVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 1132324836 176 DIRTANLYLGYPFELTGTVIRG 197
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
14-167 1.99e-60

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: 190.47  E-value: 1.99e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  14 ENAVVTIGTFDGVHIGHQKILAHLKEAAHKINGETILLTFFPHPRLIINPDDDSLRLiNDIEEKVSQLSKVGIDHLIIIP 93
Cdd:pfam06574   6 EGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNPDSAPFRL-TTLEEKIELLAELGVDYLLVLP 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132324836  94 FSRDFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASIFDYSVDEIPEQDINDIAVSSTR 167
Cdd:pfam06574  85 FTKEFASLSAEEFIENVLVDGLNVKHVVVGFDFRFGKGRKGDVELLKELGAKLGFEVTIVPPVELDGEKISSTR 158
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
184-320 3.65e-51

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: 165.24  E-value: 3.65e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 184 LGYPFELTGTVIRGDQIGRTIGFPTANLQVhePHKLIPAYGIYAVEVYIynhiqnittgeykeeNPVSIAKGMGYIGTRP 263
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPL--PEKLLPANGVYAVWVRV---------------DGGKVYPGVANIGTNP 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1132324836 264 TVDGMNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIR 320
Cdd:pfam01687  64 TFGNGKLTVEVHILDFDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQAR 120
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
184-323 1.35e-50

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: 163.76  E-value: 1.35e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  184 LGYPFELTGTVIRGDQIGRTIGFPTANLQVHEpHKLIPAYGIYAVEVYIYNHIQNittgeykeenpvsiakGMGYIGTRP 263
Cdd:smart00904   2 LGRPYSISGRVVHGDKRGRTLGFPTANLPLDD-RLLLPKNGVYAVRVRVDGKIYP----------------GVANIGTRP 64
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  264 TVDGmNRAIEISLFDFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKADEVEIRSLI 323
Cdd:smart00904  65 TFGG-DRSVEVHILDFSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYL 123
PRK07143 PRK07143
hypothetical protein; Provisional
1-234 3.62e-19

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 85.44  E-value: 3.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836   1 MKIYRSLDDFSPVENAVVTIGTFDGVHIGHQKILAHLKEaahkINGETILLTFfphpRLIINPDDDSLRLINDIEEKVSQ 80
Cdd:PRK07143    2 MKVYTFPLKNFKFEKPTFVLGGFESFHLGHLELFKKAKE----SNDEIVIVIF----KNPENLPKNTNKKFSDLNSRLQT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  81 LSKVGIDHLIIIPFSRDFSNQTPEEYISNVLvgKLGTKKIVIGYDHHFGKDRKGTMGDLEQFASifdySVDEIPEQDIND 160
Cdd:PRK07143   74 LANLGFKNIILLDFNEELQNLSGNDFIEKLT--KNQVSFFVVGKDFRFGKNASWNADDLKEYFP----NVHIVEILKINQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132324836 161 IAVSSTRVREALIKGDIRTANLYLGYPFELTGTVirgdqigrtigfpTANLQVHEPHKLIPAY-GIYAVEVYIYN 234
Cdd:PRK07143  148 QKISTSLLKEFIEFGDIELLNSLLLYNYSISITI-------------NKNFEFTYPQNIIKLHaGIYLAYVVINN 209
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
17-171 8.80e-08

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: 50.52  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836  17 VVTIGTFDGVHIGHQKIlahLKEAAHKINGETILLTFFPHPRLIINPDDDSLrlindiEEKVSQLSKVGIDHLIIIPFSR 96
Cdd:cd02039     2 GIIIGRFEPFHLGHLKL---IKEALEEALDEVIIIIVSNPPKKKRNKDPFSL------HERVEMLKEILKDRLKVVPVDF 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1132324836  97 DFSNQTPEEYISNVLVGKLGTKKIVIGYDHHFGKDRKGtmgdleQFASIFDYSVDEI--PEQDINDIAVSSTRVREA 171
Cdd:cd02039    73 PEVKILLAVVFILKILLKVGPDKVVVGEDFAFGKNASY------NKDLKELFLDIEIveVPRVRDGKKISSTLIREL 143
PLN02940 PLN02940
riboflavin kinase
187-315 1.00e-06

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 49.83  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132324836 187 PFELTGTVIRGdqIGR---TIGFPTANLqvhephkliPAYGiYAvevyiyNHIQNITTGEYKEENPVS---IAKGMGYIG 260
Cdd:PLN02940  238 PWHIGGPVIKG--FGRgskVLGIPTANL---------STEN-YS------DVLSEHPSGVYFGWAGLStrgVYKMVMSIG 299
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1132324836 261 TRPTVDGMNRAIEISLF-DFDQDIYGKTLRVKFLHFIRHDERFDSLEEMKAQIKAD 315
Cdd:PLN02940  300 WNPYFNNTEKTIEPWLLhDFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHED 355
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
17-51 1.99e-03

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


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 36.13  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1132324836  17 VVTIGTFDGVHIGHQKILahlkEAAHKINGETILL 51
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLL----ERAKELFDELIVG 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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