| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb07g003960.1 |
| Family | AA7 |
| Protein Properties | Length: 513 Molecular Weight: 54641 Isoelectric Point: 8.5308 |
| Chromosome | Chromosome/Scaffold: 7 Start: 4864992 End: 4866722 |
| 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 | 67 | 328 | 0 |
| AGAPKPFAVVVPASLQELRDSVRCARAAGLVLRLRSGGHSYEGLSYTTDDDDRTAFAVVDLAALDRVDADRRTGTAWVQSGATLGQTYHAVAAAASGSGP AAALAFSAGSCPTVGSGGHIAGGGFGLLSRKFGLAADNVVDAVLVDAAGRVLDRAAMGEDVFWAIRGGGGGTWGAVYAWRVRLSAVPDRVTAFVVNRAPG SVRSVASLVSTWQHVAPWLPDEFYISAFVGAGLPELKKKKLNRTGISVTFKGLYLGPAHEAL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 513 Download |
| MAAFAMLSLV LLRLFAVQAA GVGVVDDGRS FTACLAAAGV GNVTTRESPA YAAALLVSVQ 60 NLRFAGAGAP KPFAVVVPAS LQELRDSVRC ARAAGLVLRL RSGGHSYEGL SYTTDDDDRT 120 AFAVVDLAAL DRVDADRRTG TAWVQSGATL GQTYHAVAAA ASGSGPAAAL AFSAGSCPTV 180 GSGGHIAGGG FGLLSRKFGL AADNVVDAVL VDAAGRVLDR AAMGEDVFWA IRGGGGGTWG 240 AVYAWRVRLS AVPDRVTAFV VNRAPGSVRS VASLVSTWQH VAPWLPDEFY ISAFVGAGLP 300 ELKKKKLNRT GISVTFKGLY LGPAHEALEI LTARAIDLLS KQPKAYVILD PYGGAMDRVG 360 SADLPFPHRK GNIHGIQYLI EWAASDDDHK EEYMDWLRRF YDFMGAYVPK KPRTAYINYM 420 DLDLGTNNWS GHRTDNDIDK SPHPEVEAAR AWGERYFLGN YDRLVRAKTL IDPENVFRNA 480 QSIPPLGGVQ CMIRSTRGIS PKITSNGSTY DS* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 0.0006 | 65 | 152 | 88 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-9 | 72 | 155 | 84 | + 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. | ||
| pfam08031 | BBE | 4.0e-16 | 415 | 484 | 70 | + 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. | ||
| 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 | AAU20769.1 | 0 | 6 | 486 | 1 | 518 | berberine bridge enzyme [Thalictrum flavum subsp. glaucum] |
| DDBJ | BAC65012.1 | 0 | 34 | 512 | 34 | 562 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
| GenBank | EAZ05661.1 | 0 | 34 | 512 | 34 | 562 | hypothetical protein OsI_27888 [Oryza sativa Indica Group] |
| RefSeq | XP_002445090.1 | 0 | 1 | 512 | 1 | 512 | hypothetical protein SORBIDRAFT_07g003960 [Sorghum bicolor] |
| RefSeq | XP_002533924.1 | 0 | 29 | 486 | 29 | 535 | 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 | 28 | 495 | 24 | 528 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2h_A | 0 | 28 | 495 | 24 | 528 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2d_A | 0 | 28 | 495 | 24 | 528 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
| PDB | 4ec3_A | 0 | 28 | 495 | 5 | 509 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 28 | 495 | 5 | 509 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
