| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 28885.m000111 |
| Family | AA7 |
| Protein Properties | Length: 546 Molecular Weight: 59967.8 Isoelectric Point: 6.332 |
| Chromosome | Chromosome/Scaffold: 28885 Start: 47533 End: 49173 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 76 | 532 | 0 |
| KPLAIVIPETVEELVKTVTCCREAFLEIRVRCGGHSYEGTSYVASDGATFVVIDMMNLNKVSVDLEAKMAVVEGGATLGETYAAIAEASGVHGFSAGSCP TVGVGGHIGGGGFGLLSRKYGLAADNVVDALLVDANGRLLDRKEMGEDVFWAIRGGGGGVWGILYAWKIKLLKVPRVVTGFIVSRPGTKGHVAKLVNKWQ HVAPGLDDDFYLSCFVGAGLPEAKTTGISATFKGFYLGPRSEAVSILNKNFPELGIVEEDCKEMSWIESVLFFSGLSNGSTVSDLKNRHLQGKSYFKAKS DYVKSEISSAGIKIALDILQKEPKGYVILDPYGGVMHNISSEAIAFPHRNGNLFTIQYLVEWKEKDKNKSNVYIDWIREFYYLMTPFVSRGPRAAYINYM DFDIGAMGMIKKSVPSEDAVEIARVWGEKYFLRNFDRLVRAKTLIDPDNVFNNEQSI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 546 Download |
| MVNFPARILS STPIFLSFLL APSLSVIANQ FTSCLTQNLI SNFTTFPSSK NDSTDYYNLL 60 EFSIQNLRFA DLEMPKPLAI VIPETVEELV KTVTCCREAF LEIRVRCGGH SYEGTSYVAS 120 DGATFVVIDM MNLNKVSVDL EAKMAVVEGG ATLGETYAAI AEASGVHGFS AGSCPTVGVG 180 GHIGGGGFGL LSRKYGLAAD NVVDALLVDA NGRLLDRKEM GEDVFWAIRG GGGGVWGILY 240 AWKIKLLKVP RVVTGFIVSR PGTKGHVAKL VNKWQHVAPG LDDDFYLSCF VGAGLPEAKT 300 TGISATFKGF YLGPRSEAVS ILNKNFPELG IVEEDCKEMS WIESVLFFSG LSNGSTVSDL 360 KNRHLQGKSY FKAKSDYVKS EISSAGIKIA LDILQKEPKG YVILDPYGGV MHNISSEAIA 420 FPHRNGNLFT IQYLVEWKEK DKNKSNVYID WIREFYYLMT PFVSRGPRAA YINYMDFDIG 480 AMGMIKKSVP SEDAVEIARV WGEKYFLRNF DRLVRAKTLI DPDNVFNNEQ SIPPLPLESV 540 GSRAEI 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01679 | bact_FAD_ox | 0.007 | 77 | 154 | 79 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
| TIGR01678 | FAD_lactone_ox | 0.0005 | 76 | 256 | 186 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
| pfam08031 | BBE | 1.0e-16 | 470 | 533 | 64 | + Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. | ||
| COG0277 | GlcD | 1.0e-19 | 77 | 535 | 478 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-27 | 77 | 216 | 141 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0016491 | oxidoreductase activity |
| GO:0050660 | flavin adenine dinucleotide binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI16966.1 | 0 | 15 | 545 | 292 | 777 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI16966.1 | 0 | 373 | 513 | 85 | 224 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 0 | 15 | 535 | 16 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002329230.1 | 0 | 16 | 546 | 1 | 537 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002533924.1 | 0 | 1 | 546 | 1 | 546 | d-lactate dehydrogenase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3d2j_A | 0 | 10 | 535 | 3 | 519 | A Chain A, Crystal Structure Of The Exo84p C-Terminal Domains |
| PDB | 3d2h_A | 0 | 10 | 535 | 3 | 519 | A Chain A, Crystal Structure Of The Exo84p C-Terminal Domains |
| PDB | 3d2d_A | 0 | 10 | 535 | 3 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
| PDB | 4ec3_A | 0 | 29 | 535 | 6 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 29 | 535 | 6 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
