Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.011G161500.1 |
Family | AA7 |
Protein Properties | Length: 540 Molecular Weight: 60886.5 Isoelectric Point: 9.1787 |
Chromosome | Chromosome/Scaffold: 11 Start: 17974662 End: 17976325 |
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 | 70 | 528 | 0 |
LRFTLPSLPKPEFIFTPLEESHIQAAVICSKQLGIHLRVRSGGHDYEGLSYVSETDTPFVVVDIAELHSISVDIDNNSAWVQAGATNGELYYRIAEQSTT HGYPAGTCTSLGIGGHITGGAYGSMMRKYGLAVDNVIDARIINVHGRVLDRQTMGEDLYWAIRGGGGGSFGIITAWKVKLVPVPSTVTIFTVTKSLEQGA TKLLFRWQQVADKLDEDLFIRVNIQTVNVSNKGGRTITTSYDALFLGDANRLLQVMRESFPELGLARQDCIETSWINSTVYLGGYTINTSPEVLLQRRNI LKHYFKAKSDFVRQPIPETALKGLWEIMLEEDNPAIVLTPYGGNMGKISESQTPFPHRKGTLFMIQYLANWQDAKENVRKHTDWTRMVYRYMKPYVSMFP RQAYVNYRDLDLGINKETNTSFPEASVWGTKYFKDNFYRLVRVKTKVDPDNFFRHEQSI |
Full Sequence |
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Protein Sequence Length: 540 Download |
MVPSRFSVLS ILVVLVLTPS RMGSHPIQDQ DRFLQCLSRN SESSIPFSTV LYSPINSSFT 60 AILRSSAQNL RFTLPSLPKP EFIFTPLEES HIQAAVICSK QLGIHLRVRS GGHDYEGLSY 120 VSETDTPFVV VDIAELHSIS VDIDNNSAWV QAGATNGELY YRIAEQSTTH GYPAGTCTSL 180 GIGGHITGGA YGSMMRKYGL AVDNVIDARI INVHGRVLDR QTMGEDLYWA IRGGGGGSFG 240 IITAWKVKLV PVPSTVTIFT VTKSLEQGAT KLLFRWQQVA DKLDEDLFIR VNIQTVNVSN 300 KGGRTITTSY DALFLGDANR LLQVMRESFP ELGLARQDCI ETSWINSTVY LGGYTINTSP 360 EVLLQRRNIL KHYFKAKSDF VRQPIPETAL KGLWEIMLEE DNPAIVLTPY GGNMGKISES 420 QTPFPHRKGT LFMIQYLANW QDAKENVRKH TDWTRMVYRY MKPYVSMFPR QAYVNYRDLD 480 LGINKETNTS FPEASVWGTK YFKDNFYRLV RVKTKVDPDN FFRHEQSIPT LPHHMRKRN* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR00387 | glcD | 0.001 | 141 | 281 | 152 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
COG0277 | GlcD | 6.0e-15 | 80 | 276 | 209 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-17 | 80 | 219 | 141 | + 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 | 5.0e-20 | 472 | 529 | 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. |
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_002326177.1 | 0 | 30 | 532 | 1 | 503 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330562.1 | 0 | 24 | 539 | 23 | 534 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330564.1 | 0 | 24 | 539 | 23 | 536 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330565.1 | 0 | 30 | 536 | 27 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330617.1 | 0 | 22 | 539 | 1 | 518 | 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 | 30 | 534 | 4 | 516 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 28 | 531 | 8 | 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 | 28 | 531 | 8 | 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 | 26 | 531 | 4 | 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 | 26 | 531 | 4 | 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 |