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Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.001G462100.1 |
Family | AA7 |
Protein Properties | Length: 488 Molecular Weight: 54361.3 Isoelectric Point: 9.4601 |
Chromosome | Chromosome/Scaffold: 01 Start: 49604411 End: 49605874 |
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 | 23 | 481 | 0 |
RFNTGATPKPLVIVKPLNVAHIQAAIACSHKHGLQIRVRSGGHDYEGLSYVTVVPFVVIDLINMRTVTVDVGNKIAWVQAGATLGEVYYRIAEKSRTLAF PGGVCPTVGSGGHISGGGHGMMMRKFGLAADHIIDAKLIDAKGRILDRASMGEDLFWAIRGAGGNTFGVVVAWKLELVTVPPTVTVFNVSRTLEQNATKL VHQWQSAIGKFDEDLFSRIFLSRVNTSQEGKTTILAVYTSLFLGGVDRLLSMMQQSFPQLGLVKEDCIEMSWIESTVYFAQFPRNTSLDVLLDRSPGSTG SFKAKTDYVKAPIPEIALEGIWERLNQLDAQVAELQFTAYGGKMDEISETSTPFPHRAGNLFQIHYAVFWGDQDSERSQIYTSWIRKLYSYMTPYVTKNP RQAYINYRDLDLGMNSLGNTSYKQARIWGTKYFKNNFDRLVHVKTKVDPANFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 488 Download |
MVIFTPINSS YSSVLQFSLR NGRFNTGATP KPLVIVKPLN VAHIQAAIAC SHKHGLQIRV 60 RSGGHDYEGL SYVTVVPFVV IDLINMRTVT VDVGNKIAWV QAGATLGEVY YRIAEKSRTL 120 AFPGGVCPTV GSGGHISGGG HGMMMRKFGL AADHIIDAKL IDAKGRILDR ASMGEDLFWA 180 IRGAGGNTFG VVVAWKLELV TVPPTVTVFN VSRTLEQNAT KLVHQWQSAI GKFDEDLFSR 240 IFLSRVNTSQ EGKTTILAVY TSLFLGGVDR LLSMMQQSFP QLGLVKEDCI EMSWIESTVY 300 FAQFPRNTSL DVLLDRSPGS TGSFKAKTDY VKAPIPEIAL EGIWERLNQL DAQVAELQFT 360 AYGGKMDEIS ETSTPFPHRA GNLFQIHYAV FWGDQDSERS QIYTSWIRKL YSYMTPYVTK 420 NPRQAYINYR DLDLGMNSLG NTSYKQARIW GTKYFKNNFD RLVHVKTKVD PANFFRNEQS 480 IPPLTPW* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 0.002 | 29 | 192 | 168 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
pfam08031 | BBE | 4.0e-19 | 425 | 482 | 58 | + 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-19 | 32 | 484 | 471 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-25 | 32 | 169 | 139 | + 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 | |
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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 |
RefSeq | XP_002299021.1 | 0 | 1 | 487 | 47 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299024.1 | 0 | 9 | 484 | 1 | 476 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299025.1 | 0 | 1 | 487 | 1 | 487 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300557.1 | 0 | 2 | 487 | 46 | 531 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 2 | 487 | 46 | 531 | predicted protein [Populus trichocarpa] |
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 | 3vte_A | 0 | 2 | 486 | 24 | 515 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 3 | 484 | 26 | 496 | 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 | 3 | 484 | 26 | 496 | 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 | 2 | 484 | 23 | 496 | 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 | 2 | 484 | 23 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
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 |
HO777438 | 489 | 2 | 485 | 0 |
CV270507 | 214 | 275 | 488 | 0 |
CV267888 | 205 | 284 | 488 | 0 |
CV261512 | 200 | 289 | 488 | 0 |
CV130588 | 277 | 115 | 390 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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