| Basic Information | |
|---|---|
| Species | Capsella rubella |
| Cazyme ID | Carubv10026198m |
| Family | AA7 |
| Protein Properties | Length: 541 Molecular Weight: 60883.9 Isoelectric Point: 10.3707 |
| Chromosome | Chromosome/Scaffold: 8 Start: 1691579 End: 1693527 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 86 | 308 | 0 |
| KPWFIINPIHESHVQASIICAKKLGMHHRVRSGGHDYEGLSYVSQIVKPFILLDLSKMRQVDVNIKDNTAWVQSGATVGELYYRIAEKSKVHGFPAGLCS SLGVGGHITGGAYGSMMRKYGLGADNVLDAKIVDANGRLLDRAAMGEDTFWAIRGGAGGSFGIILAWKIKLVPVPKTVTVFTVTKTLQQDVGNKIISKWQ RVADKLVEELFIRVLFNVAGTGK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 541 Download |
| MKSSRPFTVF SFLSILALYF SLYTITPTSS SPSLQDQFIK CVQRNTHVYF PLEKTFFDPA 60 KNVSMFSQVL ESTAQNLRFL KKSLPKPWFI INPIHESHVQ ASIICAKKLG MHHRVRSGGH 120 DYEGLSYVSQ IVKPFILLDL SKMRQVDVNI KDNTAWVQSG ATVGELYYRI AEKSKVHGFP 180 AGLCSSLGVG GHITGGAYGS MMRKYGLGAD NVLDAKIVDA NGRLLDRAAM GEDTFWAIRG 240 GAGGSFGIIL AWKIKLVPVP KTVTVFTVTK TLQQDVGNKI ISKWQRVADK LVEELFIRVL 300 FNVAGTGKNK TVTMSYNTLF LGGKGTLMNV MKKSFPELGL TLKDCIEMSW LESISYISGF 360 PVHTPTNVLL KGKSPYPKIS FKSKSDFVKT PIPESGLQGI FKKLLKEDIP LMIWTPYGGM 420 MAKIPESQIP FPHRKGVLFK IQYVTSWLDN DKMPSRHINW VRDLHNYMTP YVSSNPRQAY 480 VNYRDLDLGK NTKDTKTCFK QAQGWGANYF KNNFNRLVRI KTKVDPKNFF RHEQSIPPMP 540 * 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR00387 | glcD | 2.0e-5 | 136 | 225 | 91 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
| pfam08031 | BBE | 2.0e-19 | 479 | 537 | 59 | + 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 | 4.0e-22 | 99 | 256 | 168 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 1.0e-27 | 87 | 226 | 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 |
| GenBank | AAL24314.1 | 0 | 1 | 540 | 1 | 541 | berberine bridge enzyme-like protein [Arabidopsis thaliana] |
| EMBL | CAN81654.1 | 0 | 9 | 540 | 2 | 528 | hypothetical protein [Vitis vinifera] |
| RefSeq | NP_199251.1 | 0 | 1 | 540 | 1 | 540 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199252.1 | 0 | 1 | 540 | 1 | 541 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199253.1 | 0 | 1 | 539 | 1 | 536 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 35 | 540 | 4 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 26 | 539 | 1 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 4dns_A | 0 | 26 | 539 | 1 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_B | 0 | 32 | 539 | 5 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_A | 0 | 32 | 539 | 5 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
