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Conserved domains on  [gi|219118032|ref|XP_002179799|]
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predicted protein, partial [Phaeodactylum tricornutum CCAP 1055/1]

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:  14580199
SCOP:  4002669

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 2-137 5.30e-39

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: 128.26  E-value: 5.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032    2 RLRGKVDSGYGRGgKKLGFPTANLPsrlFQNALqdVPA-GVYFGWALLESDELaapgrniaHKAVVNVGFSPTFEgqeNA 80
Cdd:pfam01687   6 SISGKVVHGDGRG-RTLGFPTANLP---LPEKL--LPAnGVYAVWVRVDGGKV--------YPGVANIGTNPTFG---NG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219118032   81 EKIVEAHLMAEEPltDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:pfam01687  69 KLTVEVHILDFDG--DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
 
Name Accession Description Interval E-value
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 2-137 5.30e-39

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: 128.26  E-value: 5.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032    2 RLRGKVDSGYGRGgKKLGFPTANLPsrlFQNALqdVPA-GVYFGWALLESDELaapgrniaHKAVVNVGFSPTFEgqeNA 80
Cdd:pfam01687   6 SISGKVVHGDGRG-RTLGFPTANLP---LPEKL--LPAnGVYAVWVRVDGGKV--------YPGVANIGTNPTFG---NG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219118032   81 EKIVEAHLMAEEPltDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:pfam01687  69 KLTVEVHILDFDG--DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 2-138 1.36e-32

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: 111.76  E-value: 1.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032     2 RLRGKVDSGYGRGgKKLGFPTANLPSrlfqNALQDVPA-GVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGqena 80
Cdd:smart00904   7 SISGRVVHGDKRG-RTLGFPTANLPL----DDRLLLPKnGVYAVRVRVD---------GKIYPGVANIGTRPTFGG---- 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 219118032    81 EKIVEAHLMAEEPltDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALD 138
Cdd:smart00904  69 DRSVEVHILDFSG--DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
PLN02940 PLN02940
riboflavin kinase
 5-148 5.45e-32

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 116.86  E-value: 5.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032   5 GKVDSGYGRGGKKLGFPTANLPSRLFQNALQDVPAGVYFGWALLESdelaapgRNIaHKAVVNVGFSPTFegqENAEKIV 84
Cdd:PLN02940 243 GPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLST-------RGV-YKMVMSIGWNPYF---NNTEKTI 311

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219118032  85 EAHLMAEEPlTDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALDVSPFVGFKSD 148
Cdd:PLN02940 312 EPWLLHDFG-EDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDD 374
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 2-141 5.88e-31

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: 112.83  E-value: 5.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032   2 RLRGKVDSGYGRGgKKLGFPTANL--PSRLFqnalqdVPA-GVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGQe 78
Cdd:COG0196  189 SISGRVVHGDKRG-RTLGFPTANLalPEEKL------LPAdGVYAVRVRID---------GRRYPGVANIGTRPTFDGG- 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219118032  79 naEKIVEAHLMaeepltDF----YNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALDVSP 141
Cdd:COG0196  252 --EPTLEVHLL------DFdgdlYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 2-137 3.59e-16

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: 73.25  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032    2 RLRGKVDSGYGRGgKKLGFPTANLPSRlfqNALQDVPAGVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGQENAe 81
Cdd:TIGR00083 170 FICGTVIHGQKLG-RTLGFPTANIKLK---NQVLPLKGGYYVVVVLLN---------GEPYPGVGNIGNRPTFIGQQLV- 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 219118032   82 kiVEAHLMaeEPLTDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:TIGR00083 236 --IEVHLL--DFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
 
Name Accession Description Interval E-value
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 2-137 5.30e-39

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: 128.26  E-value: 5.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032    2 RLRGKVDSGYGRGgKKLGFPTANLPsrlFQNALqdVPA-GVYFGWALLESDELaapgrniaHKAVVNVGFSPTFEgqeNA 80
Cdd:pfam01687   6 SISGKVVHGDGRG-RTLGFPTANLP---LPEKL--LPAnGVYAVWVRVDGGKV--------YPGVANIGTNPTFG---NG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219118032   81 EKIVEAHLMAEEPltDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:pfam01687  69 KLTVEVHILDFDG--DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAIL 123
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 2-138 1.36e-32

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: 111.76  E-value: 1.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032     2 RLRGKVDSGYGRGgKKLGFPTANLPSrlfqNALQDVPA-GVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGqena 80
Cdd:smart00904   7 SISGRVVHGDKRG-RTLGFPTANLPL----DDRLLLPKnGVYAVRVRVD---------GKIYPGVANIGTRPTFGG---- 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 219118032    81 EKIVEAHLMAEEPltDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALD 138
Cdd:smart00904  69 DRSVEVHILDFSG--DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEAREYLA 124
PLN02940 PLN02940
riboflavin kinase
 5-148 5.45e-32

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 116.86  E-value: 5.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032   5 GKVDSGYGRGGKKLGFPTANLPSRLFQNALQDVPAGVYFGWALLESdelaapgRNIaHKAVVNVGFSPTFegqENAEKIV 84
Cdd:PLN02940 243 GPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLST-------RGV-YKMVMSIGWNPYF---NNTEKTI 311

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219118032  85 EAHLMAEEPlTDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALDVSPFVGFKSD 148
Cdd:PLN02940 312 EPWLLHDFG-EDFYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDD 374
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 2-141 5.88e-31

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: 112.83  E-value: 5.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032   2 RLRGKVDSGYGRGgKKLGFPTANL--PSRLFqnalqdVPA-GVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGQe 78
Cdd:COG0196  189 SISGRVVHGDKRG-RTLGFPTANLalPEEKL------LPAdGVYAVRVRID---------GRRYPGVANIGTRPTFDGG- 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219118032  79 naEKIVEAHLMaeepltDF----YNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEALDVSP 141
Cdd:COG0196  252 --EPTLEVHLL------DFdgdlYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARAILAKLK 310
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
2-137 3.58e-27

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 102.92  E-value: 3.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032   2 RLRGKVDSGYGRGgKKLGFPTANLPsrlfqnaLQD--VPA-GVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGQE 78
Cdd:PRK05627 187 SISGRVVHGQKLG-RTLGFPTANLP-------LPDrvLPAdGVYAVRVKVD---------GKPYPGVANIGTRPTVDGGR 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219118032  79 NAekiVEAHLMaeepltDF----YNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:PRK05627 250 QL---LEVHLL------DFngdlYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETARAFL 303
ribF TIGR00083
riboflavin kinase/FMN adenylyltransferase; multifunctional enzyme: riboflavin kinase (EC 2.7.1. ...
 2-137 3.59e-16

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: 73.25  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118032    2 RLRGKVDSGYGRGgKKLGFPTANLPSRlfqNALQDVPAGVYFGWALLEsdelaapgrNIAHKAVVNVGFSPTFEGQENAe 81
Cdd:TIGR00083 170 FICGTVIHGQKLG-RTLGFPTANIKLK---NQVLPLKGGYYVVVVLLN---------GEPYPGVGNIGNRPTFIGQQLV- 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 219118032   82 kiVEAHLMaeEPLTDFYNETMRLQLHGFLRPEIKFSSFPDLIKQINADVVDAKEAL 137
Cdd:TIGR00083 236 --IEVHLL--DFSGELYGQEIKVTLVKKIRPEQKFSSLDELKNQIQQDILQAKKWF 287
 
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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