Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.001G462900.1 |
Family | AA7 |
Protein Properties | Length: 236 Molecular Weight: 26827.7 Isoelectric Point: 6.143 |
Chromosome | Chromosome/Scaffold: 01 Start: 49712808 End: 49713803 |
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 | 2 | 117 | 3.9e-35 |
LDISKLLSISVDIDDSSAWVEAGATNGELYYRIAEKSKTHDFPAGLCTSYGSMVRKYGLAADNVIDARIIDVHGRVLDRKAMREDLFWAISGGGGGSFGI ITSWKVKWQEVADKLD |
Full Sequence |
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Protein Sequence Length: 236 Download |
FLDISKLLSI SVDIDDSSAW VEAGATNGEL YYRIAEKSKT HDFPAGLCTS YGSMVRKYGL 60 AADNVIDARI IDVHGRVLDR KAMREDLFWA ISGGGGGSFG IITSWKVKWQ EVADKLDEDL 120 FIRVTIQLAT AVGRRNLFKN YFKAKPDYAK EPIPETILEG LWEWLLKEDS PNIAFTPYGG 180 MMSKISENQT PFPHRKGTLF MIRYLTIWDD PSENVAKHLD WIRKVYEYMT PYVQL* 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 2.0e-6 | 19 | 79 | 72 | + 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_002299031.1 | 0 | 3 | 235 | 5 | 237 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317090.1 | 0 | 2 | 234 | 129 | 461 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002326177.1 | 0 | 2 | 233 | 102 | 436 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523162.1 | 0 | 2 | 235 | 131 | 467 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523164.1 | 0 | 2 | 235 | 131 | 467 | Reticuline oxidase precursor, 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 | 4dns_B | 0 | 2 | 233 | 106 | 428 | 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 | 2 | 233 | 106 | 428 | 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 | 233 | 104 | 428 | 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 | 233 | 104 | 428 | 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 | 2 | 233 | 104 | 428 | 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 |
berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
dehydroscoulerine biosynthesis | RXN-10888 | EC-1.21.3 | reticuline oxidase |
sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |