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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb06g014450.1 |
Family | AA7 |
Protein Properties | Length: 488 Molecular Weight: 52242.8 Isoelectric Point: 9.4544 |
Chromosome | Chromosome/Scaffold: 6 Start: 39970615 End: 39972162 |
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 | 33 | 271 | 0 |
ARPLCVATPANASHVQAAVLCGRRHGVRLRVRSGGHDLEGLSYRSAARAGDDAAFAVLDLAPGLRAVRVDVEAGTAWVDSGATVGELYYAVGKASGDRLA FPAGLCPTIGVGGHLSGGGFGMLLRKYGVAADHVVDALLVDARGRVLDRDGMGADVFWAIRGGGGASFGVVLSWQVRLVPVPRVVTAFKVPVSVDRGAVG VLTKWQTAAPAFPDDLFVRVLVQGKVAEFQSLYLGTCAA |
Full Sequence |
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Protein Sequence Length: 488 Download |
MARPGEIPRS SPSFASVLAS SIRNPKFMVP GTARPLCVAT PANASHVQAA VLCGRRHGVR 60 LRVRSGGHDL EGLSYRSAAR AGDDAAFAVL DLAPGLRAVR VDVEAGTAWV DSGATVGELY 120 YAVGKASGDR LAFPAGLCPT IGVGGHLSGG GFGMLLRKYG VAADHVVDAL LVDARGRVLD 180 RDGMGADVFW AIRGGGGASF GVVLSWQVRL VPVPRVVTAF KVPVSVDRGA VGVLTKWQTA 240 APAFPDDLFV RVLVQGKVAE FQSLYLGTCA ALLPVMRGRF PELGLNRTHC REMTWLQSVP 300 YIYLGSGAAV EDILNRTTSL AAASKATSDY VREPLAGAAW TEIFRWLAKP NAGLMILDPY 360 GGKIGSVAES DTPFPHRGGV LFNIQYMNFW PAADGDAAAG TKWIRDMYAF MEPHVSKNPR 420 EAYFNYRDLD LGQNVVVGNV SSYEAGKVWG DKYFKGNFRR LAMAKAQIDP HDYFRNEQSV 480 PPLVASN* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-10 | 31 | 289 | 268 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-11 | 35 | 180 | 146 | + 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 | 6.0e-15 | 422 | 481 | 60 | + 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 | BAD53702.1 | 0 | 9 | 485 | 49 | 521 | putative CPRD2 [Oryza sativa Japonica Group] |
RefSeq | NP_001057833.1 | 0 | 9 | 485 | 54 | 526 | Os06g0549900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002438542.1 | 0 | 9 | 487 | 51 | 526 | hypothetical protein SORBIDRAFT_10g021690 [Sorghum bicolor] |
RefSeq | XP_002438543.1 | 0 | 9 | 487 | 53 | 529 | hypothetical protein SORBIDRAFT_10g021700 [Sorghum bicolor] |
RefSeq | XP_002446333.1 | 0 | 1 | 487 | 1 | 487 | hypothetical protein SORBIDRAFT_06g014450 [Sorghum bicolor] |
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 | 4dns_B | 0 | 9 | 484 | 29 | 497 | 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 | 9 | 484 | 29 | 497 | 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 | 9 | 484 | 27 | 497 | 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 | 9 | 484 | 27 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsh_A | 0 | 9 | 484 | 27 | 497 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FF356562 | 274 | 187 | 457 | 0 |
GO842810 | 238 | 251 | 488 | 0 |
FE654807 | 255 | 224 | 475 | 0 |
CJ906867 | 252 | 195 | 443 | 0 |
GO842810 | 25 | 228 | 252 | 0.014 |
Sequence Alignments (This image is cropped. Click for full image.) |
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