modENCODE |  Help |  blog

Protein Domain : IPR017927

Name  Ferredoxin reductase-type FAD-binding domain Short Name  Fd_Rdtase_FAD-bd
Type  Domain Description  Flavoenzymes have the ability to catalyse a wide range of biochemical reactions. They are involved in the dehydrogenation of a variety of metabolites, in electron transfer from and to redox centres, in light emission, in the activation of oxygen for oxidation and hydroxylation reactions []. About 1% of all eukaryotic and prokaryotic proteins are predicted to encode a flavin adenine dinucleotide (FAD)-binding domain []. According to structural similarities and conserved sequence motifs, FAD-binding domains have been grouped in three main families: (i)the ferredoxin reductase (FR)-type FAD-binding domain, (ii) the FAD-binding domains that adopt a Rossmann fold and (iii) the PCMH-type FAD-binding domain [].The FAD cofactor consists of adenosine monophosphate (AMP) linked to flavin mononucleotide (FMN) by a pyrophosphate bond. The AMP moiety is composed of the adenine ring bonded to a ribose that is linked to a phosphate group. The FMN moiety is composed of the isoalloxazine-flavin ring linked to a ribitol, which is connected to a phosphate group. The flavin functions mainly in a redox capacity, being able to take up two electrons from one substrate and release them two at a time to a substrate or coenzyme, or one at a time to an electron acceptor. The catalytic function of the FAD is concentrated in the isoalloxazine ring, whereas the ribityl phosphate and the AMP moiety mainly stabilise cofactor binding to protein residues [].The structural core of all FR family members is well conserved. The FAD-binding fold characteristic of the FR family is a cylindrical beta-domain with a flattened six-stranded antiparallel beta-barrel organised into two orthogonal sheets (B1-B2-B5 and B4-B3-B6) separated by one alpha-helix []. Thecylinder is open between strands B4 and B5 which makes space for the isoalloxazine and ribityl moieties of the FAD. One end of the cylinder is covered by the only helix of the domain, which is essential for the binding of the pyrophosphate groups of the FAD. The FR family contains two conserved motifs, one (R-x-Y-[ST]) located in B4 where the invariant positively charge Arg residue forms hydrogen bonds to the negative pyrophosphate oxygen atom. The other conserved sequence motif is G-x(2)-[ST]-x(2)-L-x(5)-G-x(7)-P-x-G, which is part of H1-B6 and is known as the phosphate-binding motif [, ].

Publication Counts Displayer

4 Child Features

DB identifier Name Short Name Type
IPR003097 FAD-binding, type 1 FAD-binding_1 Domain
IPR008333 Oxidoreductase, FAD-binding domain OxRdtase_FAD-bd_dom Domain
IPR013112 FAD-binding 8 FAD-bd_8 Domain
IPR013113 FAD-binding 9, siderophore-interacting FAD-bd_9_SIP Domain

0 Contains

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PS51384 PROFILE IPR017927

3 Data Sets

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

3 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

2 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Ferredoxin reductase-type FAD-binding domain   GO:0016491 oxidoreductase activity
Ferredoxin reductase-type FAD-binding domain   GO:0055114 oxidation-reduction process

2 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Ferredoxin reductase-type FAD-binding domain   GO:0016491 oxidoreductase activity
Ferredoxin reductase-type FAD-binding domain   GO:0055114 oxidation-reduction process

1 Parent Features

DB identifier Name Short Name Type
IPR017938 Riboflavin synthase-like beta-barrel Riboflavin_synthase-like_b-brl Domain

102 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
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
FBpp0170407 B4KT92 Drosophila mojavensis