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Conserved domains on  [gi|1699920966|gb|QDJ27863|]
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riboflavin biosynthesis protein RibF [Lactococcus paracarnosus]

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 ...
1-296 1.19e-125

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: 360.90  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966   1 MKVFE-FNAQNVDNAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRN 79
Cdd:COG0196     1 MKIIRgLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRP--DKAPKLLTTLEEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  80 QLFEENGVDFLYFTDFTSHFAKLTSHDFIEKYL-KKLAISAIVIGFDYQFGS----DHGSLAQLSE---YDAYQVSELTD 151
Cdd:COG0196    79 ELLEELGVDYVLVLPFTREFAALSPEEFVEEILvDKLGAKHVVVGDDFRFGKgragDVELLRELGEeygFEVEVVPPVTI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 152 MGEKISSSRIRQAIIDGDVTLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKSMQYLPLIGVYVVDIAVGDKKYRG 231
Cdd:COG0196   159 DGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRYPG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699920966 232 MASIGYNDTFGGKNKTLEVNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:COG0196   239 VANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQAR 303
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-296 1.19e-125

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: 360.90  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966   1 MKVFE-FNAQNVDNAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRN 79
Cdd:COG0196     1 MKIIRgLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRP--DKAPKLLTTLEEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  80 QLFEENGVDFLYFTDFTSHFAKLTSHDFIEKYL-KKLAISAIVIGFDYQFGS----DHGSLAQLSE---YDAYQVSELTD 151
Cdd:COG0196    79 ELLEELGVDYVLVLPFTREFAALSPEEFVEEILvDKLGAKHVVVGDDFRFGKgragDVELLRELGEeygFEVEVVPPVTI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 152 MGEKISSSRIRQAIIDGDVTLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKSMQYLPLIGVYVVDIAVGDKKYRG 231
Cdd:COG0196   159 DGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRYPG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699920966 232 MASIGYNDTFGGKNKTLEVNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:COG0196   239 VANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQAR 303
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
13-296 7.23e-124

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 356.00  E-value: 7.23e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  13 NAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRNQLFEENGVDFLYF 92
Cdd:PRK05627   12 PPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAP--DKAPARLTPLRDKAELLAELGVDYVLV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  93 TDFTSHFAKLTSHDFIEKYLKK-LAISAIVIGFDYQFGSDH-GS---LAQLSE---YDAYQVSELTDMGEKISSSRIRQA 164
Cdd:PRK05627   90 LPFDEEFAKLSAEEFIEDLLVKgLNAKHVVVGFDFRFGKKRaGDfelLKEAGKefgFEVTIVPEVKEDGERVSSTAIRQA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 165 IIDGDVTLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKsMQYLPLIGVYVVDIAVGDKKYRGMASIGYNDTFGGK 244
Cdd:PRK05627  170 LAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP-DRVLPADGVYAVRVKVDGKPYPGVANIGTRPTVDGG 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1699920966 245 NKTLEVNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:PRK05627  249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETAR 300
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-298 4.49e-71

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: 221.17  E-value: 4.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  18 LVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKFNENLLKQLtsKEKRNQLfEENGVDFLYFTDFTS 97
Cdd:TIGR00083   2 LAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPALTPL--EDKARQL-QIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  98 HFAKLTSHDFIEKYLKK-LAISAIVIGFDYQFGSDHGSLAQLSEYD------AYQVSELTDMGEKISSSRIRQAIIDGDV 170
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFgnttifCVIVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 171 TLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKSmQYLPLIGV-YVVDIAVGDKKYRGMASIGYNDTFGGKNKTLE 249
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKN-QVLPLKGGyYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1699920966 250 VNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISRYF 298
Cdd:TIGR00083 238 VHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKW 286
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
16-190 5.58e-60

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: 188.90  E-value: 5.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  16 TILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFekFNENLLKQLTSKEKRNQLFEENGVDFLYFTDF 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVF--LPDKAPPRLTTLEEKLELLESLGVDYLLVLPF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  96 TSHFAKLTSHDFIEKYLKKLAISAIVIGFDYQFGSDHGS----LAQLSE---YDAYQVSELTDMGEKISSSRIRQAIIDG 168
Cdd:cd02064    79 DKEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGdaelLKELGKkygFEVTVVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 1699920966 169 DVTLANRLLGYNYEISGLVVHG 190
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
176-296 4.28e-58

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: 182.25  E-value: 4.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  176 LLGYNYEISGLVVHGEARGRTIGYPTANIESKSMQYLPLIGVYVVDIAVGDKKYRGMASIGYNDTFGGKNkTLEVNIFDF 255
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR-SVEVHILDF 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1699920966  256 HDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:smart00904  80 SGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAR 120
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
177-296 4.53e-55

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: 174.49  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 177 LGYNYEISGLVVHGEARGRTIGYPTANIESKSmQYLPLIGVYVVDIAV-GDKKYRGMASIGYNDTFGGKNKTLEVNIFDF 255
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPE-KLLPANGVYAVWVRVdGGKVYPGVANIGTNPTFGNGKLTVEVHILDF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1699920966 256 HDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:pfam01687  80 DGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQAR 120
 
Name Accession Description Interval E-value
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
1-296 1.19e-125

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: 360.90  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966   1 MKVFE-FNAQNVDNAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRN 79
Cdd:COG0196     1 MKIIRgLSELPADLRGTVVTIGNFDGVHLGHQALIARLVELARELGLPSVVLTFEPHPREVFRP--DKAPKLLTTLEEKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  80 QLFEENGVDFLYFTDFTSHFAKLTSHDFIEKYL-KKLAISAIVIGFDYQFGS----DHGSLAQLSE---YDAYQVSELTD 151
Cdd:COG0196    79 ELLEELGVDYVLVLPFTREFAALSPEEFVEEILvDKLGAKHVVVGDDFRFGKgragDVELLRELGEeygFEVEVVPPVTI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 152 MGEKISSSRIRQAIIDGDVTLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKSMQYLPLIGVYVVDIAVGDKKYRG 231
Cdd:COG0196   159 DGERVSSTRIREALAEGDVEEAAELLGRPYSISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDGRRYPG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1699920966 232 MASIGYNDTFGGKNKTLEVNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:COG0196   239 VANIGTRPTFDGGEPTLEVHLLDFDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQAR 303
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
13-296 7.23e-124

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 356.00  E-value: 7.23e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  13 NAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRNQLFEENGVDFLYF 92
Cdd:PRK05627   12 PPDCVLTIGNFDGVHRGHQALLARAREIARERGLPSVVMTFEPHPREVFAP--DKAPARLTPLRDKAELLAELGVDYVLV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  93 TDFTSHFAKLTSHDFIEKYLKK-LAISAIVIGFDYQFGSDH-GS---LAQLSE---YDAYQVSELTDMGEKISSSRIRQA 164
Cdd:PRK05627   90 LPFDEEFAKLSAEEFIEDLLVKgLNAKHVVVGFDFRFGKKRaGDfelLKEAGKefgFEVTIVPEVKEDGERVSSTAIRQA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 165 IIDGDVTLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKsMQYLPLIGVYVVDIAVGDKKYRGMASIGYNDTFGGK 244
Cdd:PRK05627  170 LAEGDLELANKLLGRPYSISGRVVHGQKLGRTLGFPTANLPLP-DRVLPADGVYAVRVKVDGKPYPGVANIGTRPTVDGG 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1699920966 245 NKTLEVNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:PRK05627  249 RQLLEVHLLDFNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETAR 300
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
18-298 4.49e-71

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: 221.17  E-value: 4.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  18 LVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKFNENLLKQLtsKEKRNQLfEENGVDFLYFTDFTS 97
Cdd:TIGR00083   2 LAIGYFDGLHLGHQALLQELKQIAEEKGLPPAVLLFEPHPSEQFNWLTAPALTPL--EDKARQL-QIKGVEQLLVVVFDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  98 HFAKLTSHDFIEKYLKK-LAISAIVIGFDYQFGSDHGSLAQLSEYD------AYQVSELTDMGEKISSSRIRQAIIDGDV 170
Cdd:TIGR00083  79 EFANLSALQFIDQLIVKhLHVKFLVVGDDFRFGHDRQGDFLLLQLFgnttifCVIVKQLFCQDIRISSSAIRQALKNGDL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 171 TLANRLLGYNYEISGLVVHGEARGRTIGYPTANIESKSmQYLPLIGV-YVVDIAVGDKKYRGMASIGYNDTFGGKNKTLE 249
Cdd:TIGR00083 159 ELANKLLGRPYFICGTVIHGQKLGRTLGFPTANIKLKN-QVLPLKGGyYVVVVLLNGEPYPGVGNIGNRPTFIGQQLVIE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1699920966 250 VNIFDFHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISRYF 298
Cdd:TIGR00083 238 VHLLDFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKW 286
FAD_synthetase_N cd02064
FAD synthetase, N-terminal domain of the bifunctional enzyme; FAD synthetase_N. N-terminal ...
16-190 5.58e-60

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: 188.90  E-value: 5.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  16 TILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFekFNENLLKQLTSKEKRNQLFEENGVDFLYFTDF 95
Cdd:cd02064     1 TVVAIGNFDGVHLGHQALIKTLKKIARERGLPSAVLTFDPHPREVF--LPDKAPPRLTTLEEKLELLESLGVDYLLVLPF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  96 TSHFAKLTSHDFIEKYLKKLAISAIVIGFDYQFGSDHGS----LAQLSE---YDAYQVSELTDMGEKISSSRIRQAIIDG 168
Cdd:cd02064    79 DKEFASLSAEEFVEDLLVKLNAKHVVVGFDFRFGKGRSGdaelLKELGKkygFEVTVVPPVTLDGERVSSTRIREALAEG 158
                         170       180
                  ....*....|....*....|..
gi 1699920966 169 DVTLANRLLGYNYEISGLVVHG 190
Cdd:cd02064   159 DVELANELLGRPYSIEGRVVHG 180
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
176-296 4.28e-58

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: 182.25  E-value: 4.28e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  176 LLGYNYEISGLVVHGEARGRTIGYPTANIESKSMQYLPLIGVYVVDIAVGDKKYRGMASIGYNDTFGGKNkTLEVNIFDF 255
Cdd:smart00904   1 LLGRPYSISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDGKIYPGVANIGTRPTFGGDR-SVEVHILDF 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1699920966  256 HDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:smart00904  80 SGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAR 120
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
177-296 4.53e-55

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: 174.49  E-value: 4.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 177 LGYNYEISGLVVHGEARGRTIGYPTANIESKSmQYLPLIGVYVVDIAV-GDKKYRGMASIGYNDTFGGKNKTLEVNIFDF 255
Cdd:pfam01687   1 LGRPYSISGKVVHGDGRGRTLGFPTANLPLPE-KLLPANGVYAVWVRVdGGKVYPGVANIGTNPTFGNGKLTVEVHILDF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1699920966 256 HDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKISR 296
Cdd:pfam01687  80 DGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQAR 120
FAD_syn pfam06574
FAD synthetase; This family corresponds to the N terminal domain of the bifunctional enzyme ...
12-160 3.71e-47

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: 155.42  E-value: 3.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  12 DNAPTILVLGYFDGLHRGHQTLFDKARELAAEKKATISVLTFPESPILVFEKfnENLLKQLTSKEKRNQLFEENGVDFLY 91
Cdd:pfam06574   4 DLEGCVVTIGNFDGVHLGHQALIAKAKEIARELGLPSVVVTFEPHPREVFNP--DSAPFRLTTLEEKIELLAELGVDYLL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699920966  92 FTDFTSHFAKLTSHDFIEKYL-KKLAISAIVIGFDYQFGSDH-GSLAQLSEY------DAYQVSELTDMGEKISSSR 160
Cdd:pfam06574  82 VLPFTKEFASLSAEEFIENVLvDGLNVKHVVVGFDFRFGKGRkGDVELLKELgaklgfEVTIVPPVELDGEKISSTR 158
PRK07143 PRK07143
hypothetical protein; Provisional
1-298 1.45e-26

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 105.08  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966   1 MKVFEFNAQNVDNAPTILVLGYFDGLHRGHQTLFDKARELaaEKKATISVLTFPespilvfEKFNENLLKQLTSKEKRNQ 80
Cdd:PRK07143    2 MKVYTFPLKNFKFEKPTFVLGGFESFHLGHLELFKKAKES--NDEIVIVIFKNP-------ENLPKNTNKKFSDLNSRLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  81 LFEENGVDFLYFTDFTSHFAKLTSHDFIEKyLKKLAISAIVIGFDYQFGSD-HGSLAQLSEY--DAYQVSELTDMGEKIS 157
Cdd:PRK07143   73 TLANLGFKNIILLDFNEELQNLSGNDFIEK-LTKNQVSFFVVGKDFRFGKNaSWNADDLKEYfpNVHIVEILKINQQKIS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 158 SSRIRQAIIDGDVTLANRLLGYNYEISGLVVHgeargrtigyptanieSKSMQYLPLI-----GVYVVDIAVGDKKYRGM 232
Cdd:PRK07143  152 TSLLKEFIEFGDIELLNSLLLYNYSISITINK----------------NFEFTYPQNIiklhaGIYLAYVVINNFKYHGI 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699920966 233 ASIgyndtfgGKNKTLEVNIFDF-HDEIYGETVTVYFLKFIRGMIKFDSVDALitqmDDDEKISRYF 298
Cdd:PRK07143  216 LKI-------NFNNKNKIKFFDFdLIINKYQEIFIEIVKEIRIISSNEDNNIL----NDDIEIAKKF 271
PLN02940 PLN02940
riboflavin kinase
183-295 1.68e-08

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 54.84  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966 183 ISGLVVHGEARG-RTIGYPTANIESKSmqYLPLI-----GVYVVDIAVGDKK-YRGMASIGYNDTFGGKNKTLEVNIF-D 254
Cdd:PLN02940  241 IGGPVIKGFGRGsKVLGIPTANLSTEN--YSDVLsehpsGVYFGWAGLSTRGvYKMVMSIGWNPYFNNTEKTIEPWLLhD 318
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1699920966 255 FHDEIYGETVTVYFLKFIRGMIKFDSVDALITQMDDDEKIS 295
Cdd:PLN02940  319 FGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIA 359
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
18-164 9.55e-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: 50.13  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699920966  18 LVLGYFDGLHRGHQTLFDKARELAAEkkatisvltfpESPILVFEKFNENLL-KQLTSKEKRNQLFEENGVDFLYFTDFT 96
Cdd:cd02039     3 IIIGRFEPFHLGHLKLIKEALEEALD-----------EVIIIIVSNPPKKKRnKDPFSLHERVEMLKEILKDRLKVVPVD 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1699920966  97 SHFAK-LTSHDFIEKYLKKLAISAIVIGFDYQFGSD-HGSLAQLSEYDAYQVSELTDM--GEKISSSRIRQA 164
Cdd:cd02039    72 FPEVKiLLAVVFILKILLKVGPDKVVVGEDFAFGKNaSYNKDLKELFLDIEIVEVPRVrdGKKISSTLIREL 143
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
17-41 2.89e-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: 35.75  E-value: 2.89e-03
                          10        20
                  ....*....|....*....|....*
gi 1699920966  17 ILVLGYFDGLHRGHQTLFDKARELA 41
Cdd:TIGR00125   2 VIFVGTFDPFHLGHLDLLERAKELF 26
 
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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