y
Basic Information | |
---|---|
Species | Sorghum bicolor |
Cazyme ID | Sb07g003920.1 |
Family | AA7 |
Protein Properties | Length: 560 Molecular Weight: 58819.2 Isoelectric Point: 8.4297 |
Chromosome | Chromosome/Scaffold: 7 Start: 4842344 End: 4844023 |
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 | 71 | 297 | 0 |
RFALPDVGKPAAVVLPASKRDLQRAVVCARESSLAIRVRSGGHSYEGLSYTTENHVPFVVIDVANLNRVRVDRGSATAWAESGATLGELYYAVGRSSRSL AFSAGSCSTIGLGGIVSGGGFGLLSRKFGLAADNVLDAVLVDADGRVLDRTTMGADVFWAIRGGGGGSWGVVYAWKLRLVPVPRNVTVFSVGRTGPVDLV AGLIHRWQFVAPSLPDDFYLSVYLPTG |
Full Sequence |
---|
Protein Sequence Length: 560 Download |
MSCSIAALLV LVSLFLPLHQ STSSCYAAGA DDGAAAHSLS SCLLSHGVNN FTLRTSPSYA 60 AILNSSISNL RFALPDVGKP AAVVLPASKR DLQRAVVCAR ESSLAIRVRS GGHSYEGLSY 120 TTENHVPFVV IDVANLNRVR VDRGSATAWA ESGATLGELY YAVGRSSRSL AFSAGSCSTI 180 GLGGIVSGGG FGLLSRKFGL AADNVLDAVL VDADGRVLDR TTMGADVFWA IRGGGGGSWG 240 VVYAWKLRLV PVPRNVTVFS VGRTGPVDLV AGLIHRWQFV APSLPDDFYL SVYLPTGGLR 300 SSSSSSDGNV SVSFSGQVLG PKHRALSALR QSFPELGLTE SELAETSWLE ATAQFAGLDT 360 AADLPNRLLG RSKQYSKGKS DYVRSPISRR AMAGIVRYLS TGPPRQGQGQ GQGGGYVILD 420 PYGGAMARIG SGDTPCPHRA GTLYGVQYQV YWDEDDGDLG GRAAAAGEFC VGWLRSLYAF 480 MAPHVSKDPR AAYVNYLDLD LGADNWTAPA GGSSEAAVAR ARSSWGAAYF GDNFDRLVRA 540 KTLADPGNVF NNAQSIPPL* 600 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01677 | pln_FAD_oxido | 3.0e-5 | 64 | 173 | 114 | + 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. | ||
COG0277 | GlcD | 1.0e-9 | 78 | 176 | 100 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-15 | 492 | 557 | 66 | + 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. | ||
pfam01565 | FAD_binding_4 | 2.0e-17 | 80 | 179 | 101 | + 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 | 1 | 559 | 1 | 528 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
RefSeq | NP_001061035.1 | 0 | 1 | 559 | 1 | 528 | Os08g0158200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001140781.1 | 0 | 1 | 559 | 1 | 548 | hypothetical protein LOC100272856 [Zea mays] |
RefSeq | XP_002445086.1 | 0 | 1 | 559 | 1 | 559 | hypothetical protein SORBIDRAFT_07g003920 [Sorghum bicolor] |
RefSeq | XP_002445088.1 | 0 | 39 | 534 | 44 | 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 | 3d2j_A | 0 | 12 | 559 | 11 | 519 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3d2h_A | 0 | 12 | 559 | 11 | 519 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3d2d_A | 0 | 12 | 559 | 11 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 4ec3_A | 0 | 32 | 559 | 1 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 32 | 559 | 1 | 500 | 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 |