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Conserved domains on  [gi|1101084540|gb|OIO44588|]
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MAG: hypothetical protein AUJ41_02435 [Candidatus Pacebacteria bacterium CG1_02_43_31]

Protein Classification

riboflavin kinase( domain architecture ID 10658229)

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:  14580199
SCOP:  4002669

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 5-123 1.32e-40

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: 131.02  E-value: 1.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540    5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDWKKGVYAVEVSIGDnfdKKYLSVLFYGPK-TIahETKNSLELHIIDFDE 83
Cdd:smart00904   7 SISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDG---KIYPGVANIGTRpTF--GGDRSVEVHILDFSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1101084540   84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:smart00904  82 DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEARE 121
 
Name Accession Description Interval E-value
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 5-123 1.32e-40

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: 131.02  E-value: 1.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540    5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDWKKGVYAVEVSIGDnfdKKYLSVLFYGPK-TIahETKNSLELHIIDFDE 83
Cdd:smart00904   7 SISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDG---KIYPGVANIGTRpTF--GGDRSVEVHILDFSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1101084540   84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:smart00904  82 DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEARE 121
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 5-124 2.93e-40

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: 130.19  E-value: 2.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDwKKGVYAVEVSIGDnfDKKYLSVLFYGPK-TIaHETKNSLELHIIDFDE 83
Cdd:pfam01687   6 SISGKVVHGDGRGRTLGFPTANLPLPEKLLP-ANGVYAVWVRVDG--GKVYPGVANIGTNpTF-GNGKLTVEVHILDFDG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1101084540  84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKNS 124
Cdd:pfam01687  82 DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 5-123 9.64e-37

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: 126.70  E-value: 9.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDWKKGVYAVEVSIGDnfdKKYLSVLFYGPK-TIaHETKNSLELHIIDFDE 83
Cdd:COG0196   189 SISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDG---RRYPGVANIGTRpTF-DGGEPTLEVHLLDFDG 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1101084540  84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:COG0196   265 DLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARA 304
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
7-123 4.83e-35

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 122.18  E-value: 4.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   7 KGKVIEGFKLGRKIGIPTANLDPKVFKSDwKKGVYAVEVSIGDnfdKKYLSVLFYGPKTIAHETKNSLELHIIDFDENIY 86
Cdd:PRK05627  189 SGRVVHGQKLGRTLGFPTANLPLPDRVLP-ADGVYAVRVKVDG---KPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLY 264

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1101084540  87 GQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:PRK05627  265 GEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARA 301
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 5-122 8.20e-26

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: 97.90  E-value: 8.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSdWKKGVYAVEVSIGDNfdKKYLSVLFYGPKTIAHETKNSLELHIIDFDEN 84
Cdd:TIGR00083 170 FICGTVIHGQKLGRTLGFPTANIKLKNQVL-PLKGGYYVVVVLLNG--EPYPGVGNIGNRPTFIGQQLVIEVHLLDFSGE 246

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1101084540  85 IYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAK 122
Cdd:TIGR00083 247 LYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAK 284
 
Name Accession Description Interval E-value
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 5-123 1.32e-40

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: 131.02  E-value: 1.32e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540    5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDWKKGVYAVEVSIGDnfdKKYLSVLFYGPK-TIahETKNSLELHIIDFDE 83
Cdd:smart00904   7 SISGRVVHGDKRGRTLGFPTANLPLDDRLLLPKNGVYAVRVRVDG---KIYPGVANIGTRpTF--GGDRSVEVHILDFSG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1101084540   84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:smart00904  82 DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEARE 121
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 5-124 2.93e-40

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: 130.19  E-value: 2.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDwKKGVYAVEVSIGDnfDKKYLSVLFYGPK-TIaHETKNSLELHIIDFDE 83
Cdd:pfam01687   6 SISGKVVHGDGRGRTLGFPTANLPLPEKLLP-ANGVYAVWVRVDG--GKVYPGVANIGTNpTF-GNGKLTVEVHILDFDG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1101084540  84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKNS 124
Cdd:pfam01687  82 DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 5-123 9.64e-37

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: 126.70  E-value: 9.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSDWKKGVYAVEVSIGDnfdKKYLSVLFYGPK-TIaHETKNSLELHIIDFDE 83
Cdd:COG0196   189 SISGRVVHGDKRGRTLGFPTANLALPEEKLLPADGVYAVRVRIDG---RRYPGVANIGTRpTF-DGGEPTLEVHLLDFDG 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1101084540  84 NIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:COG0196   265 DLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARA 304
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
7-123 4.83e-35

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 122.18  E-value: 4.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   7 KGKVIEGFKLGRKIGIPTANLDPKVFKSDwKKGVYAVEVSIGDnfdKKYLSVLFYGPKTIAHETKNSLELHIIDFDENIY 86
Cdd:PRK05627  189 SGRVVHGQKLGRTLGFPTANLPLPDRVLP-ADGVYAVRVKVDG---KPYPGVANIGTRPTVDGGRQLLEVHLLDFNGDLY 264

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1101084540  87 GQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKN 123
Cdd:PRK05627  265 GEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARA 301
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 5-122 8.20e-26

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: 97.90  E-value: 8.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKIGIPTANLDPKVFKSdWKKGVYAVEVSIGDNfdKKYLSVLFYGPKTIAHETKNSLELHIIDFDEN 84
Cdd:TIGR00083 170 FICGTVIHGQKLGRTLGFPTANIKLKNQVL-PLKGGYYVVVVLLNG--EPYPGVGNIGNRPTFIGQQLVIEVHLLDFSGE 246

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1101084540  85 IYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAK 122
Cdd:TIGR00083 247 LYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAK 284
PLN02940 PLN02940
riboflavin kinase
 5-125 1.17e-12

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 62.93  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540   5 FFKGKVIEGFKLGRKI-GIPTANLDPKVFkSD------------W----KKGVYAVEVSIGDN--FDKKylsvlfygPKT 65
Cdd:PLN02940  240 HIGGPVIKGFGRGSKVlGIPTANLSTENY-SDvlsehpsgvyfgWaglsTRGVYKMVMSIGWNpyFNNT--------EKT 310

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101084540  66 IahetkNSLELHiiDFDENIYGQEISVSLLKFIRGVMIFSDVKSLVVQIQKDIEVAKNSI 125
Cdd:PLN02940  311 I-----EPWLLH--DFGEDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKAL 363
 
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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