| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb07g003930.1 |
| Family | AA7 |
| Protein Properties | Length: 559 Molecular Weight: 59302.9 Isoelectric Point: 7.1167 |
| Chromosome | Chromosome/Scaffold: 7 Start: 4846168 End: 4847844 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 79 | 554 | 0 |
| NNPSVGKPAAVVFPASKEELQRAVICARNTSLAIRVRSGGHSYEGLSYTTENNVPFVVIDLANLNRVHVDGGSATAWAESGATLGELYYAVGRSNRTLAF PGGTCSTVGLGGIISGGGFGLLSRKFGLAADNVLDATLIDRNGNTLTRATMDGDVFWAIRGGGGGSFGVVYSWTLRLVPVPDKITVFSGERIGPADLIAP LIHKWQFVGPHLPDEFYISTRIYFPGIIPGNNNLNMTFTGQFLAPKQQVMSVLNETYPELGLAVSELSEVSWVESAAKFAELKSVAELTDRQNGVGEYAK RKSDYAQAPISKQDMAEVARYMARAPTTGSVQLNPYGGAMARIGSSETPFPHRAGYLYSIQYAIDWTAADDNAAGGRGGEFMAWLRAFYAFMAPHVSSNP RGAYVNYVDLDLGTDNWTEPTTGAIGASSSYNAMVGVGQKAAASWGQRYFLHNFDRLVRAKSKIDPENVFNHAQSI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 559 Download |
| MDMIHTMVAA AALALNLFAA AAAGGAGAGA GAGSPPPHAH DISSCLTSNS NVVTNFSLPS 60 SPSFTPLLSS SIRYLRFVNN PSVGKPAAVV FPASKEELQR AVICARNTSL AIRVRSGGHS 120 YEGLSYTTEN NVPFVVIDLA NLNRVHVDGG SATAWAESGA TLGELYYAVG RSNRTLAFPG 180 GTCSTVGLGG IISGGGFGLL SRKFGLAADN VLDATLIDRN GNTLTRATMD GDVFWAIRGG 240 GGGSFGVVYS WTLRLVPVPD KITVFSGERI GPADLIAPLI HKWQFVGPHL PDEFYISTRI 300 YFPGIIPGNN NLNMTFTGQF LAPKQQVMSV LNETYPELGL AVSELSEVSW VESAAKFAEL 360 KSVAELTDRQ NGVGEYAKRK SDYAQAPISK QDMAEVARYM ARAPTTGSVQ LNPYGGAMAR 420 IGSSETPFPH RAGYLYSIQY AIDWTAADDN AAGGRGGEFM AWLRAFYAFM APHVSSNPRG 480 AYVNYVDLDL GTDNWTEPTT GAIGASSSYN AMVGVGQKAA ASWGQRYFLH NFDRLVRAKS 540 KIDPENVFNH AQSIPPSL* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01677 | pln_FAD_oxido | 0.0001 | 87 | 176 | 92 | + plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. | ||
| pfam08031 | BBE | 2.0e-13 | 481 | 555 | 75 | + 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 | 2.0e-20 | 84 | 264 | 187 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-25 | 86 | 225 | 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 | EAZ05659.1 | 0 | 39 | 556 | 30 | 527 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
| RefSeq | NP_001061035.1 | 0 | 45 | 556 | 36 | 527 | Os08g0158200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002445086.1 | 0 | 40 | 556 | 37 | 558 | hypothetical protein SORBIDRAFT_07g003920 [Sorghum bicolor] |
| RefSeq | XP_002445087.1 | 0 | 1 | 558 | 1 | 558 | hypothetical protein SORBIDRAFT_07g003930 [Sorghum bicolor] |
| RefSeq | XP_002445088.1 | 0 | 41 | 532 | 43 | 519 | hypothetical protein SORBIDRAFT_07g003940 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4ec3_A | 0 | 40 | 556 | 6 | 499 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 40 | 556 | 6 | 499 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3fw9_A | 0 | 41 | 556 | 1 | 493 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3d2j_A | 0 | 40 | 556 | 25 | 518 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3d2h_A | 0 | 40 | 556 | 25 | 518 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| 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 |
