Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi3g16460.1 |
Family | AA7 |
Protein Properties | Length: 585 Molecular Weight: 62158.1 Isoelectric Point: 5.9202 |
Chromosome | Chromosome/Scaffold: 3 Start: 14632981 End: 14634836 |
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 | |||
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Family | Start | End | Evalue |
AA7 | 79 | 552 | 0 |
GAGPAAVVVPSSLAGLRAAVLCSRESRLAIRLRSGGHSYEGLSYTTSGDEEEGGGGAFVVVDLVALDAVHVDAASRTAWVQSGATLGQLYHAVAMATSSS PASLAFSAGSCPTVGSGGHVAGGGFGLLSRKHGLAADNVVDAVLVDAGGRVLDRSAMGEDVFWALRGGGGGAWGAVYAWRVQLSAVPDRVTVFVVNRPGT VEAVARLVSTWQHVAPWLPDEFYLSAFVGAGLPESDKTGIISVTFKGFFLGPAHEAIQILSTRFPEIGLSDLDPKEMSWIESVVFFSGLPAGSPVSELTD RVLHGKNYFKAKSDFVRRPMAIDDLTKAIDFLSKEPKAYVILDPYGGAMDRIEATDLPFPHRKGNIHGIQYLIDWTADEDSHRDSYMDWLRRFYDLMGAY VSNGPRTAYINYQDLDLGTNDWSGLMAKGDDENANPVETARIWGERYFLGNYDRLVRAKTAIDPENVFRNAQSI |
Full Sequence |
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Protein Sequence Length: 585 Download |
MAMAVSFLLL LSLLPPLLAT AAAHGSGHFS DADDAAAALL TSCLATAGVR NVTSRRSPAY 60 AAALAFSVQN LRFASSGAGA GPAAVVVPSS LAGLRAAVLC SRESRLAIRL RSGGHSYEGL 120 SYTTSGDEEE GGGGAFVVVD LVALDAVHVD AASRTAWVQS GATLGQLYHA VAMATSSSPA 180 SLAFSAGSCP TVGSGGHVAG GGFGLLSRKH GLAADNVVDA VLVDAGGRVL DRSAMGEDVF 240 WALRGGGGGA WGAVYAWRVQ LSAVPDRVTV FVVNRPGTVE AVARLVSTWQ HVAPWLPDEF 300 YLSAFVGAGL PESDKTGIIS VTFKGFFLGP AHEAIQILST RFPEIGLSDL DPKEMSWIES 360 VVFFSGLPAG SPVSELTDRV LHGKNYFKAK SDFVRRPMAI DDLTKAIDFL SKEPKAYVIL 420 DPYGGAMDRI EATDLPFPHR KGNIHGIQYL IDWTADEDSH RDSYMDWLRR FYDLMGAYVS 480 NGPRTAYINY QDLDLGTNDW SGLMAKGDDE NANPVETARI WGERYFLGNY DRLVRAKTAI 540 DPENVFRNAQ SIPPLFTGAR GTTRRTPRGI SPKVASEDDK AYDS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 0.0009 | 95 | 172 | 78 | + 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 | 486 | 553 | 68 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC65012.1 | 0 | 38 | 584 | 29 | 562 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
GenBank | EAZ05661.1 | 0 | 38 | 584 | 29 | 562 | hypothetical protein OsI_27888 [Oryza sativa Indica Group] |
GenBank | EAZ41578.1 | 0 | 260 | 584 | 42 | 362 | hypothetical protein OsJ_26112 [Oryza sativa Japonica Group] |
RefSeq | XP_002445090.1 | 0 | 6 | 584 | 3 | 512 | hypothetical protein SORBIDRAFT_07g003960 [Sorghum bicolor] |
RefSeq | XP_002533924.1 | 0 | 37 | 555 | 28 | 535 | d-lactate dehydrogenase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3fw9_A | 0 | 40 | 555 | 2 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 40 | 555 | 8 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 40 | 555 | 8 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 40 | 555 | 27 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 40 | 555 | 27 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
Metabolic Pathways | |||
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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 |