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Conserved domains on  [gi|269973877|ref|NP_060809|]
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riboflavin kinase [Homo sapiens]

Protein Classification

riboflavin kinase( domain architecture ID 10483779)

riboflavin kinase catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), and hence, is the rate-limiting enzyme in the synthesis of FAD

CATH:  2.40.30.30
EC:  2.7.1.26
Gene Ontology:  GO:0008531|GO:0009231|GO:0046872|GO:0005524
PubMed:  19641494|14580199
SCOP:  4002669

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02940 super family cl31957
riboflavin kinase
 5-147 6.04e-56

riboflavin kinase


The actual alignment was detected with superfamily member PLN02940:

Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 179.64  E-value: 6.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMH 84
Cdd:PLN02940 238 PWHIGGPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTIEPWLLH 317

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269973877  85 TFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVS 147
Cdd:PLN02940 318 DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLTNS 380
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 5-147 6.04e-56

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 179.64  E-value: 6.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMH 84
Cdd:PLN02940 238 PWHIGGPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTIEPWLLH 317

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269973877  85 TFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVS 147
Cdd:PLN02940 318 DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLTNS 380
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 5-130 7.97e-54

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: 166.01  E-value: 7.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877    5 PYFCRGQVVRGFGRGsKQLGIPTAN--FPEQVvdnLPADistGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHI 82
Cdd:pfam01687   4 PYSISGKVVHGDGRG-RTLGFPTANlpLPEKL---LPAN---GVYAVWVRVDGGKVYPGVANIGTNPTFGNGKLTVEVHI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 269973877   83 MHtFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRL 130
Cdd:pfam01687  77 LD-FDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 5-131 9.41e-48

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: 150.67  E-value: 9.41e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877     5 PYFCRGQVVRGFGRGSKqLGIPTANFPEQVVDNLPADistGIYYGWASVGsGDVHKMVVSIGWNPYYkNTKKSMETHIMH 84
Cdd:smart00904   5 PYSISGRVVHGDKRGRT-LGFPTANLPLDDRLLLPKN---GVYAVRVRVD-GKIYPGVANIGTRPTF-GGDRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 269973877    85 tFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLE 131
Cdd:smart00904  79 -FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 5-131 7.84e-35

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: 122.84  E-value: 7.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGsKQLGIPTAN--FPEQVVdnLPADistGIYYGWASVGsGDVHKMVVSIGWNPYYKNTKKSMETHI 82
Cdd:COG0196  187 PYSISGRVVHGDKRG-RTLGFPTANlaLPEEKL--LPAD---GVYAVRVRID-GRRYPGVANIGTRPTFDGGEPTLEVHL 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 269973877  83 MHtFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLE 131
Cdd:COG0196  260 LD-FDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 5-147 6.04e-56

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 179.64  E-value: 6.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMH 84
Cdd:PLN02940 238 PWHIGGPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRGVYKMVMSIGWNPYFNNTEKTIEPWLLH 317

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269973877  85 TFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVS 147
Cdd:PLN02940 318 DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLTNS 380
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 5-130 7.97e-54

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: 166.01  E-value: 7.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877    5 PYFCRGQVVRGFGRGsKQLGIPTAN--FPEQVvdnLPADistGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHI 82
Cdd:pfam01687   4 PYSISGKVVHGDGRG-RTLGFPTANlpLPEKL---LPAN---GVYAVWVRVDGGKVYPGVANIGTNPTFGNGKLTVEVHI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 269973877   83 MHtFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRL 130
Cdd:pfam01687  77 LD-FDGDLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 5-131 9.41e-48

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: 150.67  E-value: 9.41e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877     5 PYFCRGQVVRGFGRGSKqLGIPTANFPEQVVDNLPADistGIYYGWASVGsGDVHKMVVSIGWNPYYkNTKKSMETHIMH 84
Cdd:smart00904   5 PYSISGRVVHGDKRGRT-LGFPTANLPLDDRLLLPKN---GVYAVRVRVD-GKIYPGVANIGTRPTF-GGDRSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 269973877    85 tFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLE 131
Cdd:smart00904  79 -FSGDLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 5-131 7.84e-35

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: 122.84  E-value: 7.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGsKQLGIPTAN--FPEQVVdnLPADistGIYYGWASVGsGDVHKMVVSIGWNPYYKNTKKSMETHI 82
Cdd:COG0196  187 PYSISGRVVHGDKRG-RTLGFPTANlaLPEEKL--LPAD---GVYAVRVRID-GRRYPGVANIGTRPTFDGGEPTLEVHL 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 269973877  83 MHtFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLE 131
Cdd:COG0196  260 LD-FDGDLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILA 307
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
5-128 3.87e-29

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 107.93  E-value: 3.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269973877   5 PYFCRGQVVRGFGRGsKQLGIPTAN--FPEQVvdnLPADistGIYYGWASVGsGDVHKMVVSIGWNPYYKNTKKSMETHI 82
Cdd:PRK05627 185 PYSISGRVVHGQKLG-RTLGFPTANlpLPDRV---LPAD---GVYAVRVKVD-GKPYPGVANIGTRPTVDGGRQLLEVHL 256

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 269973877  83 MHtFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKK 128
Cdd:PRK05627 257 LD-FNGDLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARA 301
 
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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