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Protein Domain : IPR017938

Name  Riboflavin synthase-like beta-barrel Short Name  Riboflavin_synthase-like_b-brl
Type  Domain Description  This entry represents a structural domain with a closed beta-barrel fold with greek-key topology. Domains with this structure can be found in the following proteins:Riboflavin synthase, which contains two homologous domains of this structure [].The FAD-binding (N-terminal) domain of ferredoxin reductase (flavodoxin reductase), where the FAD-binding domain is coupled with a NADP-binding domain of the alpha/beta class [].The FAD-binding domain of NADPH-cytochrome p450 reductase; however, this domain has an additional alpha-helical domain inserted into it [].Riboflavin synthase () catalyses the final step in the biosynthesis of vitamin B2, namely the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine to yield riboflavin and 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine (which is recycled) [].Flavins can act as primary and secondary emitters in bacterial luminescence. Lumazine proteins are involved in the bioluminescence of certain marine bacteria. These proteins are catalytically inactive, but they resemble riboflavin synthase []. Lumazine is non-covalently bound to the fluorophore 6,7-dimethyl-8-ribityllumazine, which is the substrate of riboflavin synthase.Ferredoxin reductase is a FAD-containing oxidoreductase that transports electrons between flavodoxin or ferredoxin and NADPH. In Escherichia coli, ferredoxin reductase together with flavodoxin is involved in the reductive activation of three enzymes: cobalamin-dependent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase []. An additional function for the oxidoreductase appears to be to protect the bacteria against oxygen radicals. The beta-barrel domain found in ferredoxin reductase is similar to that found in: NAD(P)H:flavin oxidoreductase [], the core domain of nitrate reductase [], cytochrome b5 reductase [], phthalate dioxygenase reductase (which contains an additional 2Fe-2S ferredoxin domain) [], benzoate dioxygenase reductase [], the PyrK subunit of dihydroorotate dehydrogenase B [], the central domain of flavohaemoglobin (which contains an additional globin domain) [], and methane monooxygenase component C (MmoC) []. Microsomal NADPH-cytochrome P450 reductase () (CPR) (NADPH-haemoprotein reductase) is a membrane-bound protein that contains both FAD and FMN. CPR catalyses electron transfer from NADPH to all known microsomal cytochromes P450. The beta-barrel domain found in NADPH-cytochrome p450 reductase is similar to that found in: sulphite reductase flavoprotein [], and the FAD/NADP+ domain of neuronal nitric-oxide synthase [].

Publication Counts Displayer

1 Child Features

DB identifier Name Short Name Type
IPR017927 Ferredoxin reductase-type FAD-binding domain Fd_Rdtase_FAD-bd Domain

0 Contains

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
SSF63380 SSF IPR017938

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

4 Found In

DB identifier Name Short Name Type
IPR001094 Flavodoxin Flavdoxin Family
IPR001221 Phenol hydroxylase reductase Phe_hydroxylase Family
IPR000951 Phthalate dioxygenase reductase Ph_dOase_redase Family
IPR001783 Lumazine-binding protein Lumazine-bd Family

2 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Riboflavin synthase-like beta-barrel   GO:0016491 oxidoreductase activity
Riboflavin synthase-like beta-barrel   GO:0055114 oxidation-reduction process

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Riboflavin synthase-like beta-barrel   GO:0016491 oxidoreductase activity
Riboflavin synthase-like beta-barrel   GO:0055114 oxidation-reduction process

0 Parent Features

104 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0079777 Q27571 Drosophila melanogaster
FBpp0078880 Q27597 Drosophila melanogaster
FBpp0078881 Q8IPJ7 Drosophila melanogaster
FBpp0075811 Q9I7R1 Drosophila melanogaster
FBpp0075810 Q4LDP7 Drosophila melanogaster
FBpp0085713 A1ZBK6 Drosophila melanogaster
FBpp0074465 Q9VWK8 Drosophila melanogaster
FBpp0076337 Q9VSJ5 Drosophila melanogaster
FBpp0082740 Q9VEV2 Drosophila melanogaster
FBpp0289611 Q9VQH2 Drosophila melanogaster
FBpp0111562 A8DWJ8 Drosophila melanogaster
FBpp0110168 Q0E8F4 Drosophila melanogaster
FBpp0110169 Q0E8F5 Drosophila melanogaster
FBpp0290358 E1JHY0 Drosophila melanogaster
FBpp0276994 Q292E3 Drosophila pseudoobscura
FBpp0275583 B5DQC6 Drosophila pseudoobscura
FBpp0287916 Q29KF2 Drosophila pseudoobscura
FBpp0280292 Q29GQ2 Drosophila pseudoobscura
FBpp0276894 Q291S3 Drosophila pseudoobscura
FBpp0281499 Q295W6 Drosophila pseudoobscura
FBpp0285624 Q29JN6 Drosophila pseudoobscura
FBpp0286242 Q29DY6 Drosophila pseudoobscura
FBpp0287477 Q29KP6 Drosophila pseudoobscura
FBpp0161070 B4KYV3 Drosophila mojavensis
FBpp0160748 B4KFY5 Drosophila mojavensis
FBpp0161318 B4KF94 Drosophila mojavensis
FBpp0162048 B4KYD9 Drosophila mojavensis
FBpp0163527 B4L8Q7 Drosophila mojavensis
FBpp0167029 B4KKM7 Drosophila mojavensis
FBpp0169077 B4KR60 Drosophila mojavensis